A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. They are ubiquitous enzymes that have a preference for acidic proteins. Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins.
A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression.
A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.
A casein kinase that was originally described as a monomeric enzyme with a molecular weight of 30-40 kDa. Several ISOENZYMES of casein kinase I have been found which are encoded by separate genes. Many of the casein kinase I isoenzymes have been shown to play distinctive roles in intracellular SIGNAL TRANSDUCTION.
A casein kinase I isoenzyme with specificity for proteins involved the regulation of the CIRCADIAN RHYTHM.
A casein kinase I isoenzyme that plays a regulatory role in a variety of cellular functions including vesicular transport, CHROMOSOME SEGREGATION; CYTOKINESIS, developmental processes, and the CIRCADIAN RHYTHM.
A casein kinase I isoenzyme that plays a role in intracellular signaling pathways including the WNT SIGNALING PATHWAY, the CELL CYCLE, membrane trafficking, and RNA processing. Multiple isoforms of casein kinase I alpha exist and are due to ALTERNATIVE SPLICING.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
Agents that inhibit PROTEIN KINASES.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.
Phosphoproteins are proteins that have been post-translationally modified with the addition of a phosphate group, usually on serine, threonine or tyrosine residues, which can play a role in their regulation, function, interaction with other molecules, and localization within the cell.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
The rate dynamics in chemical or physical systems.
A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.
Phosphoprotein with protein kinase activity that functions in the G2/M phase transition of the CELL CYCLE. It is the catalytic subunit of the MATURATION-PROMOTING FACTOR and complexes with both CYCLIN A and CYCLIN B in mammalian cells. The maximal activity of cyclin-dependent kinase 1 is achieved when it is fully dephosphorylated.
A subgroup of mitogen-activated protein kinases that activate TRANSCRIPTION FACTOR AP-1 via the phosphorylation of C-JUN PROTEINS. They are components of intracellular signaling pathways that regulate CELL PROLIFERATION; APOPTOSIS; and CELL DIFFERENTIATION.
An RNA polymerase II transcriptional inhibitor. This compound terminates transcription prematurely by selective inhibition of RNA synthesis. It is used in research to study underlying mechanisms of cellular regulation.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A family of serine-threonine kinases that bind to and are activated by MONOMERIC GTP-BINDING PROTEINS such as RAC GTP-BINDING PROTEINS and CDC42 GTP-BINDING PROTEIN. They are intracellular signaling kinases that play a role the regulation of cytoskeletal organization.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.
Protein kinases that control cell cycle progression in all eukaryotes and require physical association with CYCLINS to achieve full enzymatic activity. Cyclin-dependent kinases are regulated by phosphorylation and dephosphorylation events.
A 44-kDa extracellular signal-regulated MAP kinase that may play a role the initiation and regulation of MEIOSIS; MITOSIS; and postmitotic functions in differentiated cells. It phosphorylates a number of TRANSCRIPTION FACTORS; and MICROTUBULE-ASSOCIATED PROTEINS.
The phosphoric acid ester of serine.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Proteins prepared by recombinant DNA technology.
A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Phosphopeptides are short peptide sequences that contain phosphorylated amino acid residues, typically serine, threonine or tyrosine, and play crucial roles in intracellular signaling transduction pathways by modulating protein-protein interactions and enzymatic activities.
A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins.
Established cell cultures that have the potential to propagate indefinitely.
Mitogen-activated protein kinase kinase kinases (MAPKKKs) are serine-threonine protein kinases that initiate protein kinase signaling cascades. They phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES; (MAPKKs) which in turn phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs).
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
A dsRNA-activated cAMP-independent protein serine/threonine kinase that is induced by interferon. In the presence of dsRNA and ATP, the kinase autophosphorylates on several serine and threonine residues. The phosphorylated enzyme catalyzes the phosphorylation of the alpha subunit of EUKARYOTIC INITIATION FACTOR-2, leading to the inhibition of protein synthesis.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
An egg yolk phosphoglycoprotein which contains about 90% of the yolk protein phosphorus. It is synthesized in the liver of the hen and transferred to the developing oocyte, where it is bound to lipoproteins within the yolk granules.
The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
An abundant 43-kDa mitogen-activated protein kinase kinase subtype with specificity for MITOGEN-ACTIVATED PROTEIN KINASE 1 and MITOGEN-ACTIVATED PROTEIN KINASE 3.
The sum of the weight of all the atoms in a molecule.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
An enzyme that catalyzes the conversion of ATP and thymidine to ADP and thymidine 5'-phosphate. Deoxyuridine can also act as an acceptor and dGTP as a donor. (From Enzyme Nomenclature, 1992) EC 2.7.1.21.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
A protein serine-threonine kinase that catalyzes the PHOSPHORYLATION of I KAPPA B PROTEINS. This enzyme also activates the transcription factor NF-KAPPA B and is composed of alpha and beta catalytic subunits, which are protein kinases and gamma, a regulatory subunit.
A mitogen-activated protein kinase subfamily that is widely expressed and plays a role in regulation of MEIOSIS; MITOSIS; and post mitotic functions in differentiated cells. The extracellular signal regulated MAP kinases are regulated by a broad variety of CELL SURFACE RECEPTORS and can be activated by certain CARCINOGENS.
A mitogen-activated protein kinase kinase with specificity for JNK MITOGEN-ACTIVATED PROTEIN KINASES; P38 MITOGEN-ACTIVATED PROTEIN KINASES and the RETINOID X RECEPTORS. It takes part in a SIGNAL TRANSDUCTION pathway that is activated in response to cellular stress.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
An enzyme that catalyzes the conversion of phosphatidylinositol (PHOSPHATIDYLINOSITOLS) to phosphatidylinositol 4-phosphate, the first committed step in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
A family of cell cycle-dependent kinases that are related in structure to CDC28 PROTEIN KINASE; S CEREVISIAE; and the CDC2 PROTEIN KINASE found in mammalian species.
A family of highly conserved serine-threonine kinases that are involved in the regulation of MITOSIS. They are involved in many aspects of cell division, including centrosome duplication, SPINDLE APPARATUS formation, chromosome alignment, attachment to the spindle, checkpoint activation, and CYTOKINESIS.
A group of intracellular-signaling serine threonine kinases that bind to RHO GTP-BINDING PROTEINS. They were originally found to mediate the effects of rhoA GTP-BINDING PROTEIN on the formation of STRESS FIBERS and FOCAL ADHESIONS. Rho-associated kinases have specificity for a variety of substrates including MYOSIN-LIGHT-CHAIN PHOSPHATASE and LIM KINASES.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A ubiquitously expressed protein kinase that is involved in a variety of cellular SIGNAL PATHWAYS. Its activity is regulated by a variety of signaling protein tyrosine kinase.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A cytoplasmic serine threonine kinase involved in regulating CELL DIFFERENTIATION and CELLULAR PROLIFERATION. Overexpression of this enzyme has been shown to promote PHOSPHORYLATION of BCL-2 PROTO-ONCOGENE PROTEINS and chemoresistance in human acute leukemia cells.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
A class of protein-serine-threonine kinases that was originally found as one of the three types of kinases that phosphorylate GLYCOGEN SYNTHASE. Glycogen synthase kinases along with CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASES and CYCLIC AMP-DEPENDENT PROTEIN KINASES regulate glycogen synthase activity.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
A cell line derived from cultured tumor cells.
A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Circadian rhythm signaling proteins that influence circadian clock by interacting with other circadian regulatory proteins and transporting them into the CELL NUCLEUS.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
An enzyme of the transferase class that uses ATP to catalyze the phosphorylation of diacylglycerol to a phosphatidate. EC 2.7.1.107.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
A serine-threonine kinase that plays important roles in CELL DIFFERENTIATION; CELL MIGRATION; and CELL DEATH of NERVE CELLS. It is closely related to other CYCLIN-DEPENDENT KINASES but does not seem to participate in CELL CYCLE regulation.
A trinitrobenzene derivative with antispasmodic properties that is used primarily as a laboratory reagent.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.
A peptide which is a homopolymer of lysine.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A phosphoprotein that was initially identified as a major target of DOPAMINE activated ADENYLYL CYCLASE in the CORPUS STRIATUM. It regulates the activities of PROTEIN PHOSPHATASE-1 and PROTEIN KINASE A, and it is a key mediator of the biochemical, electrophysiological, transcriptional, and behavioral effects of DOPAMINE.
Proteins which are present in or isolated from SOYBEANS.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
Transport proteins that carry specific substances in the blood or across cell membranes.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.
A Janus kinase subtype that is involved in signaling from GROWTH HORMONE RECEPTORS; PROLACTIN RECEPTORS; and a variety of CYTOKINE RECEPTORS such as ERYTHROPOIETIN RECEPTORS and INTERLEUKIN RECEPTORS. Dysregulation of Janus kinase 2 due to GENETIC TRANSLOCATIONS have been associated with a variety of MYELOPROLIFERATIVE DISORDERS.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A family of non-receptor, PROLINE-rich protein-tyrosine kinases.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
Proteins which are present in or isolated from vegetables or vegetable products used as food. The concept is distinguished from PLANT PROTEINS which refers to non-dietary proteins from plants.
MAMMARY GLANDS in the non-human MAMMALS.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
A group of compounds with the heterocyclic ring structure of benzo(c)pyridine. The ring structure is characteristic of the group of opium alkaloids such as papaverine. (From Stedman, 25th ed)
A family of ribosomal protein S6 kinases that are structurally distinguished from RIBOSOMAL PROTEIN S6 KINASES, 70-KDA by their apparent molecular size and the fact they contain two functional kinase domains. Although considered RIBOSOMAL PROTEIN S6 KINASES, members of this family are activated via the MAP KINASE SIGNALING SYSTEM and have been shown to act on a diverse array of substrates that are involved in cellular regulation such as RIBOSOMAL PROTEIN S6 and CAMP RESPONSE ELEMENT-BINDING PROTEIN.
A protein kinase C subtype that was originally characterized as a CALCIUM-independent, serine-threonine kinase that is activated by PHORBOL ESTERS and DIACYLGLYCEROLS. It is targeted to specific cellular compartments in response to extracellular signals that activate G-PROTEIN-COUPLED RECEPTORS; TYROSINE KINASE RECEPTORS; and intracellular protein tyrosine kinase.
Elements of limited time intervals, contributing to particular results or situations.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A 195-kDa MAP kinase kinase kinase with broad specificity for MAP KINASE KINASES. It is found localized in the CYTOSKELETON and can activate a variety of MAP kinase-dependent pathways.
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A scaffolding protein that is a critical component of the axin signaling complex which binds to ADENOMATOUS POLYPOSIS COLI PROTEIN; GLYCOGEN SYNTHASE KINASE 3; and CASEIN KINASE I.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
PKC beta encodes two proteins (PKCB1 and PKCBII) generated by alternative splicing of C-terminal exons. It is widely distributed with wide-ranging roles in processes such as B-cell receptor regulation, oxidative stress-induced apoptosis, androgen receptor-dependent transcriptional regulation, insulin signaling, and endothelial cell proliferation.
The relationship between the dose of an administered drug and the response of the organism to the drug.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Pyrvinium compounds are antihelminthic agents, specifically pyrazinylquinolines, that have been used in the treatment of intestinal infections caused by certain parasitic worms, such as pinworms and hookworms, by inhibiting their microtubular function and causing severe vacuolation within the worm's tissues.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A 44 kDa mitogen-activated protein kinase kinase with specificity for MITOGEN-ACTIVATED PROTEIN KINASE 1 and MITOGEN-ACTIVATED PROTEIN KINASE 3.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
A key regulator of CELL CYCLE progression. It partners with CYCLIN E to regulate entry into S PHASE and also interacts with CYCLIN A to phosphorylate RETINOBLASTOMA PROTEIN. Its activity is inhibited by CYCLIN-DEPENDENT KINASE INHIBITOR P27 and CYCLIN-DEPENDENT KINASE INHIBITOR P21.
A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.
A group of cyclic GMP-dependent enzymes that catalyze the phosphorylation of SERINE or THREONINE residues of proteins.
Derivatives of the steroid androstane having two double bonds at any site in any of the rings.
A group of phenyl benzopyrans named for having structures like FLAVONES.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
Benzopyrroles with the nitrogen at the number one carbon adjacent to the benzyl portion, in contrast to ISOINDOLES which have the nitrogen away from the six-membered ring.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
A serine threonine kinase that controls a wide range of growth-related cellular processes. The protein is referred to as the target of RAPAMYCIN due to the discovery that SIROLIMUS (commonly known as rapamycin) forms an inhibitory complex with TACROLIMUS BINDING PROTEIN 1A that blocks the action of its enzymatic activity.
Unstable isotopes of phosphorus that decay or disintegrate emitting radiation. P atoms with atomic weights 28-34 except 31 are radioactive phosphorus isotopes.
Protein hydrolysates are defined as complex mixtures of peptides produced by the enzymatic or chemical breakdown of whole proteins, which can vary in their degree of hydrolysis and molecular weight, and are used in various medical and nutritional applications due to their improved digestibility and bioavailability compared to intact proteins.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
An enzyme catalyzing the transfer of a phosphate group from 3-phospho-D-glycerate in the presence of ATP to yield 3-phospho-D-glyceroyl phosphate and ADP. EC 2.7.2.3.
Wnt proteins are a large family of secreted glycoproteins that play essential roles in EMBRYONIC AND FETAL DEVELOPMENT, and tissue maintenance. They bind to FRIZZLED RECEPTORS and act as PARACRINE PROTEIN FACTORS to initiate a variety of SIGNAL TRANSDUCTION PATHWAYS. The canonical Wnt signaling pathway stabilizes the transcriptional coactivator BETA CATENIN.
Chromones are a class of chemical compounds that contain a benzopyran-4-one core structure, which are found in various natural and synthetic substances, including some medications used to treat asthma and allergies.
A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.
A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.
Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
An enzyme that catalyzes the phosphorylation of the guanidine nitrogen of arginine in the presence of ATP and a divalent cation with formation of phosphorylarginine and ADP. EC 2.7.3.3.
A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
An enzyme that catalyzes reversible reactions of a nucleoside triphosphate, e.g., ATP, with a nucleoside monophosphate, e.g., UMP, to form ADP and UDP. Many nucleoside monophosphates can act as acceptor while many ribo- and deoxyribonucleoside triphosphates can act as donor. EC 2.7.4.4.
A mitogen-activated protein kinase kinase with specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES.
The major protein constituents of milk are CASEINS and whey proteins such as LACTALBUMIN and LACTOGLOBULINS. IMMUNOGLOBULINS occur in high concentrations in COLOSTRUM and in relatively lower concentrations in milk. (Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p554)
Morpholines are organic compounds containing a morpholine ring, which is a saturated six-membered heterocycle made up of four carbon atoms and two oxygen atoms (OCC1CCO), often used as functional groups in pharmaceuticals, agrochemicals, and materials science due to their versatile chemical properties.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
A mitogen-activated protein kinase kinase with specificity for a subset of P38 MITOGEN-ACTIVATED PROTEIN KINASES that includes MITOGEN-ACTIVATED PROTEIN KINASE 12; MITOGEN-ACTIVATED PROTEIN KINASE 13; and MITOGEN-ACTIVATED PROTEIN KINASE 14.
A c-jun amino-terminal kinase that is activated by environmental stress and pro-inflammatory cytokines. Several isoforms of the protein with molecular sizes of 43 and 48 KD exist due to multiple ALTERNATIVE SPLICING.
An aurora kinase that localizes to the CENTROSOME during MITOSIS and is involved in centrosome regulation and formation of the MITOTIC SPINDLE. Aurora A overexpression in many malignant tumor types suggests that it may be directly involved in NEOPLASTIC CELL TRANSFORMATION.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
Highly conserved protein-serine threonine kinases that phosphorylate and activate a group of AGC protein kinases, especially in response to the production of the SECOND MESSENGERS, phosphatidylinositol 3,4,-biphosphate (PtdIns(3,4)P2) and phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3).
A non-receptor protein-tyrosine kinase that is expressed primarily in the BRAIN; OSTEOBLASTS; and LYMPHOID CELLS. In the CENTRAL NERVOUS SYSTEM focal adhesion kinase 2 modulates ION CHANNEL function and MITOGEN-ACTIVATED PROTEIN KINASES activity.
A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508)
Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
A biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
A phosphatidylinositol 3-kinase that catalyzes the conversion of 1-phosphatidylinositol into 1-phosphatidylinositol 3-phosphate.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).

Optimal sequences for non-phosphate-directed phosphorylation by protein kinase CK1 (casein kinase-1)--a re-evaluation. (1/481)

A variety of synthetic peptides derived from either the inhibitor-2 (I-2) phosphoacceptor sites or the optimal sequences selected in an oriented peptide library have been compared for their susceptibility to phosphorylation by protein kinase CK1 (also termed casein kinase-1). The I-2-derived peptides are by far preferred over the library peptides by both rat liver CK1 (and by the alpha/beta, gamma and delta/epsilon isoforms immunoprecipitated from it) and recombinant Xenopus laevis CK1 alpha. The superiority of the I-2-derived peptides over the library ones is reflected by Vmax values one to two orders of magnitude higher while the Km values are comparable. Individual substitutions of any of the aspartic acids with alanine in the I-2-derived peptide RRKHAAIGDDDDAYSITA is detrimental, producing both a fall in Vmax and an increase in Km which are more pronounced at position n -3, but also quite significant at positions n -4, n -5 and, to a lesser extent, n -6. The unfavourable effect of these substitutions is more evident with rat liver CK1 than with recombinant Xenopus laevis CK1 alpha. The chimeric peptide IGDDDDAY-S-IIIFFA, resulting from the combination of the N-terminal acidic sequence of the I-2 (Ser86) site and the C-terminal hydrophobic cluster selected in the library peptides (MAEFDTG-S-IIIFFAKKK and MAYYDAA-S-IIIFFAKKK) is phosphorylated as efficiently as the I-2-derived peptide in terms of both Km and Vmax. These combined data strongly support the conclusion that, at variance with the optimal sequences selected in the library, optimal non-phosphate-directed phosphorylation of peptide substrates by CK1 critically relies on the presence of a cluster of acidic residues (preferably aspartic acid) upstream from position n -2, while the highly hydrophobic region downstream from serine selected in the library appears to be dispensable. The reason for these discrepancies remains unclear. The possibility that the library data are biased by the invariant elements forming its scaffold (MA-x-x-x-x-x-SI-x-x-x-x-AKKK) would be consistent with the observation that the library-selected peptides, despite their low Km values, fail to compete against the phosphorylation of protein and peptide substrates by CK1, suggesting that they bind to elements partially distinct from those responsible for substrate recognition.  (+info)

The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization. (2/481)

Casein kinase 1 protein kinases are ubiquitous and abundant Ser/Thr-specific protein kinases with activity on acidic substrates. In yeast, the products of the redundant YCK1 and YCK2 genes are together essential for cell viability. Mutants deficient for these proteins display defects in cellular morphogenesis, cytokinesis, and endocytosis. Yck1p and Yck2p are peripheral plasma membrane proteins, and we report here that the localization of Yck2p within the membrane is dynamic through the cell cycle. Using a functional green fluorescent protein (GFP) fusion, we have observed that Yck2p is concentrated at sites of polarized growth during bud morphogenesis. At cytokinesis, GFP-Yck2p becomes associated with a ring at the bud neck and then appears as a patch of fluorescence, apparently coincident with the dividing membranes. The bud neck association of Yck2p at cytokinesis does not require an intact septin ring, and septin assembly is altered in a Yck-deficient mutant. The sites of GFP-Yck2p concentration and the defects observed for Yck-deficient cells together suggest that Yck plays distinct roles in morphogenesis and cytokinesis that are effected by differential localization.  (+info)

A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in 'reverse signalling'. (3/481)

We have identified a putative signalling feature of the cytoplasmic domains of the tumour necrosis factor (TNF) family members based on available amino acid sequence data. A casein kinase I (CKI) consensus sequence is conserved in the cytoplasmic domain of six of 15 members of the type II integral membrane TNF ligand family. We examined the phosphorylation state of transmembrane tumour necrosis factor-alpha (mTNF) with [32P]orthophosphate labelling and in vitro kinase assays, in lipopolysaccharide-stimulated RAW264.7 cells. A dimeric form of the type I soluble TNF receptor (sTNFR) was found to dephosphorylate mTNF. This effect could be prevented by treatment with phosphatase inhibitors. Recombinant CKI was able to phosphorylate mTNF that had been dephosphorylated by sTNFR ligation in vivo, and this was less effective if phosphatase inhibitors had been used to prevent mTNF dephosphorylation. A mutated form of mTNF, lacking the CKI recognition site, cannot be phosphorylated by the enzyme. Binding of sTNFR to mTNF induced an increase in intracellular calcium levels in RAW264.7 cells, implying the presence of an associated signalling pathway. We predict that this CKI motif is phosphorylated in other TNF ligand members, and that it represents a new insight into the mechanism of 'reverse signalling' in this cytokine family.  (+info)

Insertion of a casein kinase recognition sequence induces phosphorylation of ovine beta-lactoglobulin in transgenic mice. (4/481)

We have shown that the cellular mechanisms of the mammary gland can be used to produce a phosphorylated form of a normally unphosphorylated milk protein. This was achieved by the insertion of a beta-casein DNA sequence coding for a group of mammary gland casein kinase recognition sites into ovine beta-lactoglobulin. Transgenic mice carrying this modified gene were generated and lactating females were shown to produce a novel beta-lactoglobulin in their milk. The infrared spectrum, reactivity to antiphosphoserine antibody and reduction of electrophoretic mobility on treatment with alkaline phosphatase showed that the novel protein recovered from the milk whey (serum) was phosphorylated and molecular mass determination by mass spectrometry was consistent with the phosphorylation of one or two residues. A similar level of phosphorylation was measured by quantitative infrared spectroscopy. Centrifugation of the milk to pellet the casein micelles showed that most of the phosphorylated beta-lactoglobulin was in the whey and hence not incorporated into casein micelles.  (+info)

Alterations in C3 activation and binding caused by phosphorylation by a casein kinase released from activated human platelets. (5/481)

A casein kinase released from activated human platelets phosphorylates a number of plasma proteins extracellularly, and that activation of platelets in systemic lupus erythematosus patients parallels an increase in the phosphate content of plasma proteins, including C3. The present study was undertaken to characterize this platelet protein kinase and to further elucidate the effect(s) on C3 function of phosphorylation by platelet casein kinase. The phosphate content of human plasma C3 was increased from 0.15 to 0.60 mol phosphate/mol of C3 after platelet activation in whole blood or platelet-rich plasma. The platelet casein kinase was distinct from other casein kinases in terms of its dependence on cations, inhibition by specific protein kinase inhibitors, and immunological reactivity. C3 that had been phosphorylated with platelet casein kinase was tested for its susceptibility to cleavage by trypsin or the classical and alternative pathway convertases and its binding to EAC and IgG. Phosphorylation did not affect the cleavage of C3 into C3a and C3b, but the binding of fragments from phosphorylated C3 to EAC14oxy2 cells and to IgG in purified systems and in serum was increased by 1.6-4.5 times over that of unphosphorylated C3. A covariation was seen between the enhanced binding of C3 fragments to IgG after phosphorylation and an increased ratio of glycerol/glycine binding, from 2.0 for unphosphorylated C3 to 4.9 for phosphorylated C3. The present study suggests that an overall effect of phosphorylation of C3 by platelet casein kinase is to enhance the opsonization of immune complexes.  (+info)

Angiotensin II stimulates serine phosphorylation of the adaptor protein Nck: physical association with the serine/threonine kinases Pak1 and casein kinase I. (6/481)

Nck is a small adaptor protein consisting exclusively of three SH3 domains and one SH2 domain. Nck is thought to have an important role in cell signalling by coupling receptor tyrosine kinases, via its SH2 domain, to downstream SH3-binding effectors. We report here that angiotensin II, working through the AT1 receptor subtype, stimulates the phosphorylation of Nck in rat aortic smooth muscle cells. Phosphopeptide mapping analysis revealed that Nck is phosphorylated on four peptides containing exclusively phosphoserine in quiescent cells. Treatment with angiotensin II resulted in increased phosphorylation of these four peptides, without the appearance of new phosphopeptides. We show that Nck, via its SH3 domains, specifically binds three major phosphoproteins of 95, 82 and 66 kDa both in vitro and in intact cells. Notably, the phosphorylation of these Nck-binding proteins was found to increase in parallel with that of Nck on stimulation by angiotensin II. One candidate for the 66 kDa phosphoprotein is the serine/threonine kinase p21-activated kinase 1 (Pak1), which was found to form a stable complex with Nck in aortic smooth muscle cells. We have also identified the gamma2 isoform of casein kinase I as another protein kinase that associates with Nck in these cells. These findings indicate that Nck is a target of G-protein-coupled receptors and suggest a role for Pak1 and casein kinase I-gamma2 in downstream signalling or regulation of the AT1 receptor.  (+info)

Serine phosphorylation of the ligand-activated beta-platelet-derived growth factor receptor by casein kinase I-gamma2 inhibits the receptor's autophosphorylating activity. (7/481)

Platelet-derived growth factor (PDGF) receptors (PDGFRs) are membrane protein-tyrosine kinases that, upon activation, become tyrosine-phosphorylated and associate with numerous SH2 domain-containing molecules involved in mediating signal transduction. In Rat-2 fibroblasts, we have characterized the phosphorylation of the beta-PDGFR following its activation by PDGF. In contrast to tyrosine phosphorylation, which was transient and returned to near basal levels by 30 min, PDGF-stimulated Ser/Thr phosphorylation of the beta-PDGFR was increased by 5 min and remained elevated after 30 min. In vivo, after 5 min of PDGF stimulation, serine phosphorylation of the beta-PDGFR was greatly reduced by CKI-7, a specific inhibitor of casein kinase I (CKI). In vitro, recombinant CKI-gamma2 phosphorylated the ligand-activated beta-PDGFR on serine residues in a CKI-7-sensitive manner and resulted in a marked inhibition of the receptor's autophosphorylating activity. Furthermore, in Rat-2 fibroblasts, expression of hemagglutinin epitope-tagged active CKI-gamma2 resulted in a dramatic decrease in the tyrosine phosphorylation state of the beta-PDGFR in response to PDGF, consistent with receptor inactivation. Our data suggest that upon PDGF stimulation, CKI-gamma2 is activated and/or translocated in proximity to the beta-PDGFR, whereby it phosphorylates the beta-PDGFR on serine residues and negatively regulates its tyrosine kinase activity, leading to receptor inactivation.  (+info)

The casein kinase Ialpha isoform is both physically positioned and functionally competent to regulate multiple events of mRNA metabolism. (8/481)

Casein kinase I is a highly conserved family of serine/threonine protein kinases present in every organism tested from yeast to humans. To date, little is known about the function of the higher eukaryotic isoforms in this family. The CKI isoforms in Saccharomyces cerevisiae, however, have been genetically linked to the regulation of DNA repair, cell cycle progression and cytokinesis. It has also been established that the nuclear localization of two of these isoforms is essential for their function. The work presented here demonstrates that the higher eukaryotic CKIalpha isoform is also present within nuclei of certain established cell lines and associated with discrete nuclear structures. The nature of its nuclear localization was characterized. In this regard, CKIalpha was shown to colocalize with factors involved in pre-mRNA splicing at nuclear speckles and that its association with these structures exhibited several biochemical properties in common with known splicing factors. The kinase was also shown to be associated with a complex that contained certain splicing factors. Finally, in vitro, CKIalpha was shown to be capable of phosphorylating particular splicing factors within a region rich in serine/arginine dipeptide repeat motifs suggesting that it has both the opportunity and the capacity to regulate one or more steps of mRNA metabolism.  (+info)

Casein kinases are a family of protein kinases that play important roles in various cellular processes, including signal transduction, cell cycle regulation, and DNA damage repair. These enzymes phosphorylate serine and threonine residues on their target proteins by transferring a phosphate group from ATP to the hydroxyl side chain of these amino acids.

There are several isoforms of casein kinases, including Casein Kinase 1 (CK1) and Casein Kinase 2 (CK2), which differ in their structure, substrate specificity, and cellular functions. CK1 is involved in various signaling pathways, such as the Wnt signaling pathway, and regulates processes such as gene transcription, DNA repair, and circadian rhythm. CK2, on the other hand, is a highly conserved serine/threonine protein kinase that plays a role in many cellular processes, including cell division, apoptosis, and transcriptional regulation.

Dysregulation of casein kinases has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, these enzymes are considered important targets for the development of new therapeutic strategies.

Casein Kinase II (CK2) is a serine/threonine protein kinase that is widely expressed in eukaryotic cells and is involved in the regulation of various cellular processes. It is a heterotetrameric enzyme, consisting of two catalytic subunits (alpha and alpha') and two regulatory subunits (beta).

CK2 phosphorylates a wide range of substrates, including transcription factors, signaling proteins, and other kinases. It is known to play roles in cell cycle regulation, apoptosis, DNA damage response, and protein stability, among others. CK2 activity is often found to be elevated in various types of cancer, making it a potential target for cancer therapy.

Caseins are a group of phosphoproteins found in the milk of mammals, including cows and humans. They are the major proteins in milk, making up about 80% of the total protein content. Caseins are characterized by their ability to form micelles, or tiny particles, in milk when it is mixed with calcium. This property allows caseins to help transport calcium and other minerals throughout the body.

Caseins are also known for their nutritional value, as they provide essential amino acids and are easily digestible. They are often used as ingredients in infant formula and other food products. Additionally, caseins have been studied for their potential health benefits, such as reducing the risk of cardiovascular disease and improving bone health. However, more research is needed to confirm these potential benefits.

Casein Kinase 1 (CK1) is a type of serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, signal transduction, and DNA damage response. CK1 phosphorylates specific serine or threonine residues on its target proteins, thereby modulating their activity, localization, or stability.

There are several isoforms of CK1, including CK1α, CK1δ, CK1ε, and CK1γ, which exhibit distinct subcellular distributions and functions. Dysregulation of CK1 has been implicated in several human diseases, such as cancer, neurodegenerative disorders, and metabolic syndromes. Therefore, understanding the molecular mechanisms underlying CK1 function is essential for developing novel therapeutic strategies to treat these conditions.

Casein Kinase 1 Epsilon (CSNK1E or CK1ε) is a serine/threonine protein kinase that plays a role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, localization, or stability. Mutations in the CSNK1E gene have been associated with certain human diseases, such as Familiial Advanced Sleep Phase Disorder (FASPD).

Casein Kinase 1 Delta (CK1δ) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific target proteins on serine or threonine residues, thereby modulating their activity, stability, or localization. CK1δ is widely expressed in various tissues and has been implicated in several diseases, such as cancer, neurodegenerative disorders, and inflammatory conditions. Inhibitors of CK1δ are being investigated as potential therapeutic agents for these diseases.

Casein Kinase 1 Alpha (CK1α) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, stability, or localization. CK1α is widely expressed in different tissues and has been implicated in several diseases, such as cancer and neurodegenerative disorders. Inhibition of CK1α has emerged as a potential therapeutic strategy for treating these conditions.

Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

Phosphatidylinositol 3-Kinases (PI3Ks) are a family of enzymes that play a crucial role in intracellular signal transduction. They phosphorylate the 3-hydroxyl group of the inositol ring in phosphatidylinositol and its derivatives, which results in the production of second messengers that regulate various cellular processes such as cell growth, proliferation, differentiation, motility, and survival.

PI3Ks are divided into three classes based on their structure and substrate specificity. Class I PI3Ks are further subdivided into two categories: class IA and class IB. Class IA PI3Ks are heterodimers consisting of a catalytic subunit (p110α, p110β, or p110δ) and a regulatory subunit (p85α, p85β, p55γ, or p50γ). They are primarily activated by receptor tyrosine kinases and G protein-coupled receptors. Class IB PI3Ks consist of a catalytic subunit (p110γ) and a regulatory subunit (p101 or p84/87). They are mainly activated by G protein-coupled receptors.

Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders. Therefore, PI3Ks have emerged as important targets for drug development in these areas.

Mitogen-activated protein kinase (MAPK) signaling system is a crucial pathway for the transmission and regulation of various cellular responses in eukaryotic cells. It plays a significant role in several biological processes, including proliferation, differentiation, apoptosis, inflammation, and stress response. The MAPK cascade consists of three main components: MAP kinase kinase kinase (MAP3K or MEKK), MAP kinase kinase (MAP2K or MEK), and MAP kinase (MAPK).

The signaling system is activated by various extracellular stimuli, such as growth factors, cytokines, hormones, and stress signals. These stimuli initiate a phosphorylation cascade that ultimately leads to the activation of MAPKs. The activated MAPKs then translocate into the nucleus and regulate gene expression by phosphorylating various transcription factors and other regulatory proteins.

There are four major MAPK families: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5. Each family has distinct functions, substrates, and upstream activators. Dysregulation of the MAPK signaling system can lead to various diseases, including cancer, diabetes, cardiovascular diseases, and neurological disorders. Therefore, understanding the molecular mechanisms underlying this pathway is crucial for developing novel therapeutic strategies.

Protein kinase inhibitors (PKIs) are a class of drugs that work by interfering with the function of protein kinases. Protein kinases are enzymes that play a crucial role in many cellular processes by adding a phosphate group to specific proteins, thereby modifying their activity, localization, or interaction with other molecules. This process of adding a phosphate group is known as phosphorylation and is a key mechanism for regulating various cellular functions, including signal transduction, metabolism, and cell division.

In some diseases, such as cancer, protein kinases can become overactive or mutated, leading to uncontrolled cell growth and division. Protein kinase inhibitors are designed to block the activity of these dysregulated kinases, thereby preventing or slowing down the progression of the disease. These drugs can be highly specific, targeting individual protein kinases or families of kinases, making them valuable tools for targeted therapy in cancer and other diseases.

Protein kinase inhibitors can work in various ways to block the activity of protein kinases. Some bind directly to the active site of the enzyme, preventing it from interacting with its substrates. Others bind to allosteric sites, changing the conformation of the enzyme and making it inactive. Still, others target upstream regulators of protein kinases or interfere with their ability to form functional complexes.

Examples of protein kinase inhibitors include imatinib (Gleevec), which targets the BCR-ABL kinase in chronic myeloid leukemia, and gefitinib (Iressa), which inhibits the EGFR kinase in non-small cell lung cancer. These drugs have shown significant clinical benefits in treating these diseases and have become important components of modern cancer therapy.

Calcium-calmodulin-dependent protein kinases (CAMKs) are a family of enzymes that play a crucial role in intracellular signaling pathways. They are activated by the binding of calcium ions and calmodulin, a ubiquitous calcium-binding protein, to their regulatory domain.

Once activated, CAMKs phosphorylate specific serine or threonine residues on target proteins, thereby modulating their activity, localization, or stability. This post-translational modification is essential for various cellular processes, including synaptic plasticity, gene expression, metabolism, and cell cycle regulation.

There are several subfamilies of CAMKs, including CaMKI, CaMKII, CaMKIII (also known as CaMKIV), and CaMK kinase (CaMKK). Each subfamily has distinct structural features, substrate specificity, and regulatory mechanisms. Dysregulation of CAMK signaling has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and cardiovascular disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.

Protein Kinase C (PKC) is a family of serine-threonine kinases that play crucial roles in various cellular signaling pathways. These enzymes are activated by second messengers such as diacylglycerol (DAG) and calcium ions (Ca2+), which result from the activation of cell surface receptors like G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs).

Once activated, PKC proteins phosphorylate downstream target proteins, thereby modulating their activities. This regulation is involved in numerous cellular processes, including cell growth, differentiation, apoptosis, and membrane trafficking. There are at least 10 isoforms of PKC, classified into three subfamilies based on their second messenger requirements and structural features: conventional (cPKC; α, βI, βII, and γ), novel (nPKC; δ, ε, η, and θ), and atypical (aPKC; ζ and ι/λ). Dysregulation of PKC signaling has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

SRC-family kinases (SFKs) are a group of non-receptor tyrosine kinases that play important roles in various cellular processes, including cell proliferation, differentiation, survival, and migration. They are named after the founding member, SRC, which was first identified as an oncogene in Rous sarcoma virus.

SFKs share a common structure, consisting of an N-terminal unique domain, a SH3 domain, a SH2 domain, a catalytic kinase domain, and a C-terminal regulatory tail with a negative regulatory tyrosine residue (Y527 in human SRC). In their inactive state, SFKs are maintained in a closed conformation through intramolecular interactions between the SH3 domain, SH2 domain, and the phosphorylated C-terminal tyrosine.

Upon activation by various signals, such as growth factors, cytokines, or integrin engagement, SFKs are activated through a series of events that involve dephosphorylation of the regulatory tyrosine residue, recruitment to membrane receptors via their SH2 and SH3 domains, and trans-autophosphorylation of the activation loop in the kinase domain.

Once activated, SFKs can phosphorylate a wide range of downstream substrates, including other protein kinases, adaptor proteins, and cytoskeletal components, thereby regulating various signaling pathways that control cell behavior. Dysregulation of SFK activity has been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Cyclic AMP (cAMP)-dependent protein kinases, also known as protein kinase A (PKA), are a family of enzymes that play a crucial role in intracellular signaling pathways. These enzymes are responsible for the regulation of various cellular processes, including metabolism, gene expression, and cell growth and differentiation.

PKA is composed of two regulatory subunits and two catalytic subunits. When cAMP binds to the regulatory subunits, it causes a conformational change that leads to the dissociation of the catalytic subunits. The freed catalytic subunits then phosphorylate specific serine and threonine residues on target proteins, thereby modulating their activity.

The cAMP-dependent protein kinases are activated in response to a variety of extracellular signals, such as hormones and neurotransmitters, that bind to G protein-coupled receptors (GPCRs) or receptor tyrosine kinases (RTKs). These signals lead to the activation of adenylyl cyclase, which catalyzes the conversion of ATP to cAMP. The resulting increase in intracellular cAMP levels triggers the activation of PKA and the downstream phosphorylation of target proteins.

Overall, cAMP-dependent protein kinases are essential regulators of many fundamental cellular processes and play a critical role in maintaining normal physiology and homeostasis. Dysregulation of these enzymes has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

p38 Mitogen-Activated Protein Kinases (p38 MAPKs) are a family of conserved serine-threonine protein kinases that play crucial roles in various cellular processes, including inflammation, immune response, differentiation, apoptosis, and stress responses. They are activated by diverse stimuli such as cytokines, ultraviolet radiation, heat shock, osmotic stress, and lipopolysaccharides (LPS).

Once activated, p38 MAPKs phosphorylate and regulate several downstream targets, including transcription factors and other protein kinases. This regulation leads to the expression of genes involved in inflammation, cell cycle arrest, and apoptosis. Dysregulation of p38 MAPK signaling has been implicated in various diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. Therefore, p38 MAPKs are considered promising targets for developing new therapeutic strategies to treat these conditions.

Phosphoproteins are proteins that have been post-translationally modified by the addition of a phosphate group (-PO3H2) onto specific amino acid residues, most commonly serine, threonine, or tyrosine. This process is known as phosphorylation and is mediated by enzymes called kinases. Phosphoproteins play crucial roles in various cellular processes such as signal transduction, cell cycle regulation, metabolism, and gene expression. The addition or removal of a phosphate group can activate or inhibit the function of a protein, thereby serving as a switch to control its activity. Phosphoproteins can be detected and quantified using techniques such as Western blotting, mass spectrometry, and immunofluorescence.

Peptide mapping is a technique used in proteomics and analytical chemistry to analyze and identify the sequence and structure of peptides or proteins. This method involves breaking down a protein into smaller peptide fragments using enzymatic or chemical digestion, followed by separation and identification of these fragments through various analytical techniques such as liquid chromatography (LC) and mass spectrometry (MS).

The resulting peptide map serves as a "fingerprint" of the protein, providing information about its sequence, modifications, and structure. Peptide mapping can be used for a variety of applications, including protein identification, characterization of post-translational modifications, and monitoring of protein degradation or cleavage.

In summary, peptide mapping is a powerful tool in proteomics that enables the analysis and identification of proteins and their modifications at the peptide level.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Mitogen-Activated Protein Kinase 1 (MAPK1), also known as Extracellular Signal-Regulated Kinase 2 (ERK2), is a protein kinase that plays a crucial role in intracellular signal transduction pathways. It is a member of the MAPK family, which regulates various cellular processes such as proliferation, differentiation, apoptosis, and stress response.

MAPK1 is activated by a cascade of phosphorylation events initiated by upstream activators like MAPKK (Mitogen-Activated Protein Kinase Kinase) in response to various extracellular signals such as growth factors, hormones, and mitogens. Once activated, MAPK1 phosphorylates downstream targets, including transcription factors and other protein kinases, thereby modulating their activities and ultimately influencing gene expression and cellular responses.

MAPK1 is widely expressed in various tissues and cells, and its dysregulation has been implicated in several pathological conditions, including cancer, inflammation, and neurodegenerative diseases. Therefore, understanding the regulation and function of MAPK1 signaling pathways has important implications for developing therapeutic strategies to treat these disorders.

CDC2 protein kinase, also known as cell division cycle 2 or CDK1, is a type of enzyme that plays a crucial role in the regulation of the cell cycle. The cell cycle is the series of events that cells undergo as they grow, replicate their DNA, and divide into two daughter cells.

CDC2 protein kinase is a member of the cyclin-dependent kinase (CDK) family, which are serine/threonine protein kinases that are activated by binding to regulatory subunits called cyclins. CDC2 protein kinase is primarily associated with the regulation of the G2 phase and the entry into mitosis, the stage of the cell cycle where nuclear and cytoplasmic division occur.

CDC2 protein kinase functions by phosphorylating various target proteins, which alters their activity and contributes to the coordination of the different events that occur during the cell cycle. The activity of CDC2 protein kinase is tightly regulated through a variety of mechanisms, including phosphorylation and dephosphorylation, as well as the binding and destruction of cyclin subunits.

Dysregulation of CDC2 protein kinase has been implicated in various human diseases, including cancer, where uncontrolled cell division can lead to the formation of tumors. Therefore, understanding the regulation and function of CDC2 protein kinase is an important area of research in molecular biology and medicine.

JNK (c-Jun N-terminal kinase) Mitogen-Activated Protein Kinases are a subgroup of the Ser/Thr protein kinases that are activated by stress stimuli and play important roles in various cellular processes, including inflammation, apoptosis, and differentiation. They are involved in the regulation of gene expression through phosphorylation of transcription factors such as c-Jun. JNKs are activated by a variety of upstream kinases, including MAP2Ks (MKK4/SEK1 and MKK7), which are in turn activated by MAP3Ks (such as ASK1, MEKK1, MLKs, and TAK1). JNK signaling pathways have been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases.

Dichlororibofuranosylbenzimidazole is not a medical term, but it is a chemical compound with the formula C6H5Cl2N2O4. It is also known as tribuzole or 1-(2'-deoxy-2'-fluoro-β-D-erythro-pentofuranosyl)-2,2-dichlorobenzimidazole.

Tribuzole is an antiviral drug that has been studied for the treatment of HIV infection. It works by inhibiting the reverse transcriptase enzyme of the virus, which is necessary for the replication of the viral RNA into DNA. However, tribuzole has not been approved for clinical use due to its limited efficacy and unfavorable side effects profile.

Therefore, there is no medical definition for 'dichlororibofuranosylbenzimidazole' as it is not a term used in medical practice or literature.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

P21-activated kinases (PAKs) are a family of serine/threonine protein kinases that play crucial roles in various cellular processes, including cytoskeletal reorganization, cell motility, and gene transcription. They are activated by binding to small GTPases of the Rho family, such as Cdc42 and Rac, which become active upon stimulation of various extracellular signals. Once activated, PAKs phosphorylate a range of downstream targets, leading to changes in cell behavior and function. Aberrant regulation of PAKs has been implicated in several human diseases, including cancer and neurological disorders.

Protein-Tyrosine Kinases (PTKs) are a type of enzyme that plays a crucial role in various cellular functions, including signal transduction, cell growth, differentiation, and metabolism. They catalyze the transfer of a phosphate group from ATP to the tyrosine residues of proteins, thereby modifying their activity, localization, or interaction with other molecules.

PTKs can be divided into two main categories: receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases (NRTKs). RTKs are transmembrane proteins that become activated upon binding to specific ligands, such as growth factors or hormones. NRTKs, on the other hand, are intracellular enzymes that can be activated by various signals, including receptor-mediated signaling and intracellular messengers.

Dysregulation of PTK activity has been implicated in several diseases, such as cancer, diabetes, and inflammatory disorders. Therefore, PTKs are important targets for drug development and therapy.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Mitogen-Activated Protein Kinase Kinases (MAP2K or MEK) are a group of protein kinases that play a crucial role in intracellular signal transduction pathways. They are so named because they are activated by mitogens, which are substances that stimulate cell division, and other extracellular signals.

MAP2Ks are positioned upstream of the Mitogen-Activated Protein Kinases (MAPK) in a three-tiered kinase cascade. Once activated, MAP2Ks phosphorylate and activate MAPKs, which then go on to regulate various cellular processes such as proliferation, differentiation, survival, and apoptosis.

There are several subfamilies of MAP2Ks, including MEK1/2, MEK3/6 (also known as MKK3/6), MEK4/7 (also known as MKK4/7), and MEK5. Each MAP2K is specific to activating a particular MAPK, and they are activated by different MAP3Ks (MAP kinase kinase kinases) in response to various extracellular signals.

Dysregulation of the MAPK/MAP2K signaling pathways has been implicated in numerous diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, targeting these pathways with therapeutic agents has emerged as a promising strategy for treating various diseases.

Cyclin-dependent kinases (CDKs) are a family of serine/threonine protein kinases that play crucial roles in regulating the cell cycle, transcription, and other cellular processes. They are activated by binding to cyclin proteins, which accumulate and degrade at specific stages of the cell cycle. The activation of CDKs leads to phosphorylation of various downstream target proteins, resulting in the promotion or inhibition of different cell cycle events. Dysregulation of CDKs has been implicated in several human diseases, including cancer, and they are considered important targets for drug development.

Mitogen-Activated Protein Kinase 3 (MAPK3), also known as extracellular signal-regulated kinase 1 (ERK1), is a serine/threonine protein kinase that plays a crucial role in intracellular signal transduction pathways. It is involved in the regulation of various cellular processes, including proliferation, differentiation, and survival, in response to extracellular stimuli such as growth factors, hormones, and stress.

MAPK3 is activated through a phosphorylation cascade that involves the activation of upstream MAPK kinases (MKK or MEK). Once activated, MAPK3 can phosphorylate and activate various downstream targets, including transcription factors, to regulate gene expression. Dysregulation of MAPK3 signaling has been implicated in several diseases, including cancer and neurological disorders.

Phosphoserine is not a medical term per se, but rather a biochemical term. It refers to a post-translationally modified amino acid called serine that has a phosphate group attached to its side chain. This modification plays a crucial role in various cellular processes, including signal transduction and regulation of protein function. In medical contexts, abnormalities in the regulation of phosphorylation (the addition of a phosphate group) and dephosphorylation (the removal of a phosphate group) have been implicated in several diseases, such as cancer and neurological disorders.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Glycogen Synthase Kinase 3 (GSK-3) is a serine/threonine protein kinase that plays a crucial role in the regulation of several cellular processes, including glycogen metabolism, cell signaling, gene transcription, and apoptosis. It was initially discovered as a key enzyme involved in glycogen metabolism due to its ability to phosphorylate and inhibit glycogen synthase, an enzyme responsible for the synthesis of glycogen from glucose.

GSK-3 exists in two isoforms, GSK-3α and GSK-3β, which share a high degree of sequence similarity and are widely expressed in various tissues. Both isoforms are constitutively active under normal conditions and are regulated through inhibitory phosphorylation by several upstream signaling pathways, such as insulin, Wnt, and Hedgehog signaling.

Dysregulation of GSK-3 has been implicated in the pathogenesis of various diseases, including diabetes, neurodegenerative disorders, and cancer. In recent years, GSK-3 has emerged as an attractive therapeutic target for the development of novel drugs to treat these conditions.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Phosphopeptides are short peptide sequences that contain one or more phosphorylated amino acid residues, most commonly serine, threonine, or tyrosine. Phosphorylation is a post-translational modification that plays a crucial role in regulating various cellular processes such as signal transduction, protein-protein interactions, enzyme activity, and protein degradation. The addition of a phosphate group to a peptide can alter its charge, conformation, stability, and interaction with other molecules, thereby modulating its function in the cell. Phosphopeptides are often generated by proteolytic digestion of phosphorylated proteins and are used as biomarkers or probes to study protein phosphorylation and signaling pathways in various biological systems.

Creatine kinase (CK) is a muscle enzyme that is normally present in small amounts in the blood. It is primarily found in tissues that require a lot of energy, such as the heart, brain, and skeletal muscles. When these tissues are damaged or injured, CK is released into the bloodstream, causing the levels to rise.

Creatine kinase exists in several forms, known as isoenzymes, which can be measured in the blood to help identify the location of tissue damage. The three main isoenzymes are:

1. CK-MM: Found primarily in skeletal muscle
2. CK-MB: Found primarily in heart muscle
3. CK-BB: Found primarily in the brain

Elevated levels of creatine kinase, particularly CK-MB, can indicate damage to the heart muscle, such as occurs with a heart attack. Similarly, elevated levels of CK-BB may suggest brain injury or disease. Overall, measuring creatine kinase levels is a useful diagnostic tool for assessing tissue damage and determining the severity of injuries or illnesses.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

MAP (Mitogen-Activated Protein) Kinase Kinase Kinases (MAP3K or MAPKKK) are a group of protein kinases that play a crucial role in intracellular signal transduction pathways, which regulate various cellular processes such as proliferation, differentiation, survival, and apoptosis. They are called "kinases" because they catalyze the transfer of a phosphate group from ATP to specific serine or threonine residues on their target proteins.

MAP3Ks function upstream of MAP Kinase Kinases (MKKs or MAP2K) and MAP Kinases (MPKs or MAPK) in the MAP kinase cascade. Upon activation by various extracellular signals, such as growth factors, cytokines, stress, and hormones, MAP3Ks phosphorylate and activate MKKs, which subsequently phosphorylate and activate MPKs. Activated MPKs then regulate the activity of downstream transcription factors and other target proteins to elicit appropriate cellular responses.

There are several subfamilies of MAP3Ks, including ASK, DLK, TAK, MEKK, MLK, and ZAK, among others. Each subfamily has distinct structural features and functions in different signaling pathways. Dysregulation of MAP kinase cascades, including MAP3Ks, has been implicated in various human diseases, such as cancer, inflammation, and neurodegenerative disorders.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

eIF-2 kinase is a type of protein kinase that phosphorylates the alpha subunit of eukaryotic initiation factor-2 (eIF-2) at serine 51. This phosphorylation event inhibits the guanine nucleotide exchange factor eIF-2B, thereby preventing the recycling of eIF-2 and reducing global protein synthesis.

There are four main subtypes of eIF-2 kinases:

1. HRI (heme-regulated inhibitor) - responds to heme deficiency and oxidative stress
2. PERK (PKR-like endoplasmic reticulum kinase) - activated by ER stress and misfolded proteins in the ER
3. GCN2 (general control non-derepressible 2) - responds to amino acid starvation
4. PKR (double-stranded RNA-activated protein kinase) - activated by double-stranded RNA during viral infections

These eIF-2 kinases play crucial roles in regulating cellular responses to various stress conditions, such as the integrated stress response (ISR), which helps maintain cellular homeostasis and promote survival under adverse conditions.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Ribosomal Protein S6 Kinases (RSKs) are a family of serine/threonine protein kinases that play a crucial role in the regulation of cell growth, proliferation, and survival. They are so named because they phosphorylate and regulate the function of the ribosomal protein S6, which is a component of the 40S ribosomal subunit involved in protein synthesis.

RSKs are activated by various signals, including growth factors, hormones, and mitogens, through a cascade of phosphorylation events involving several upstream kinases such as MAPK/ERK kinase (MEK) and extracellular signal-regulated kinase (ERK). Once activated, RSKs phosphorylate a wide range of downstream targets, including transcription factors, regulators of translation, and cytoskeletal proteins, thereby modulating their activities and functions.

There are four isoforms of RSKs in humans, namely RSK1, RSK2, RSK3, and RSK4, which share a common structural organization and functional domains, including an N-terminal kinase domain, a C-terminal kinase domain, and a linker region that contains several regulatory motifs. Dysregulation of RSKs has been implicated in various pathological conditions, including cancer, cardiovascular diseases, neurological disorders, and diabetes, making them attractive targets for therapeutic intervention.

Threonine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is HO2CCH(NH2)CH(OH)CH3. Threonine plays a crucial role in various biological processes, including protein synthesis, immune function, and fat metabolism. It is particularly important for maintaining the structural integrity of proteins, as it is often found in their hydroxyl-containing regions. Foods rich in threonine include animal proteins such as meat, dairy products, and eggs, as well as plant-based sources like lentils and soybeans.

Phosvitin is not a medical term, but it is a protein found in egg yolk. It is a highly phosphorylated protein, meaning that many of its amino acids are bound to phosphate groups. This gives phosvitin a high negative charge and makes it an excellent chelator of positively charged ions such as calcium and iron.

Phosvitin is known for its ability to bind and store minerals, particularly iron, in the egg yolk. It plays a role in the development and nutrition of growing embryos in birds. In addition to its nutritional role, phosvitin has been studied for its potential health benefits due to its antioxidant properties and ability to bind heavy metals.

While not a medical term itself, phosvitin may be relevant to certain medical fields such as nutrition, biochemistry, and food science.

Phosphothreonine is not a medical term per se, but rather a biochemical term that refers to a specific post-translational modification of the amino acid threonine. In this modification, a phosphate group is added to the hydroxyl side chain of threonine, which can affect the function and regulation of proteins in which it occurs.

In medical or clinical contexts, phosphothreonine may be mentioned in relation to various disease processes or signaling pathways that involve protein kinases, enzymes that add phosphate groups to specific amino acids (including threonine) in proteins. For example, abnormal regulation of protein kinases and phosphatases (enzymes that remove phosphate groups) can contribute to the development of cancer, neurological disorders, and other diseases.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Pyruvate kinase is an enzyme that plays a crucial role in the final step of glycolysis, a process by which glucose is broken down to produce energy in the form of ATP (adenosine triphosphate). Specifically, pyruvate kinase catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), resulting in the formation of pyruvate and ATP.

There are several isoforms of pyruvate kinase found in different tissues, including the liver, muscle, and brain. The type found in red blood cells is known as PK-RBC or PK-M2. Deficiencies in pyruvate kinase can lead to a genetic disorder called pyruvate kinase deficiency, which can result in hemolytic anemia due to the premature destruction of red blood cells.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Mitogen-Activated Protein Kinases (MAPKs) are a family of serine/threonine protein kinases that play crucial roles in various cellular processes, including proliferation, differentiation, transformation, and apoptosis, in response to diverse stimuli such as mitogens, growth factors, hormones, cytokines, and environmental stresses. They are highly conserved across eukaryotes and consist of a three-tiered kinase module composed of MAPK kinase kinases (MAP3Ks), MAPK kinases (MKKs or MAP2Ks), and MAPKs.

Activation of MAPKs occurs through a sequential phosphorylation and activation cascade, where MAP3Ks phosphorylate and activate MKKs, which in turn phosphorylate and activate MAPKs at specific residues (Thr-X-Tyr or Ser-Pro motifs). Once activated, MAPKs can further phosphorylate and regulate various downstream targets, including transcription factors and other protein kinases.

There are four major groups of MAPKs in mammals: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5/BMK1. Each group of MAPKs has distinct upstream activators, downstream targets, and cellular functions, allowing for a high degree of specificity in signal transduction and cellular responses. Dysregulation of MAPK signaling pathways has been implicated in various human diseases, including cancer, diabetes, neurodegenerative disorders, and inflammatory diseases.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

MAPKKK1 or Mitogen-Activated Protein Kinase Kinase Kinase 1 is a serine/threonine protein kinase that belongs to the MAP3K family. It plays a crucial role in intracellular signal transduction pathways, particularly in the MAPK/ERK cascade, which is involved in various cellular processes such as proliferation, differentiation, and survival.

MAPKKK1 activates MAPKKs (Mitogen-Activated Protein Kinase Kinases) through phosphorylation of specific serine and threonine residues. In turn, activated MAPKKs phosphorylate and activate MAPKs (Mitogen-Activated Protein Kinases), which then regulate the activity of various transcription factors and other downstream targets to elicit appropriate cellular responses.

Mutations in MAPKKK1 have been implicated in several human diseases, including cancer and developmental disorders. Therefore, understanding its function and regulation is essential for developing novel therapeutic strategies to treat these conditions.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Proto-oncogene proteins are normal cellular proteins that play crucial roles in various cellular processes, such as signal transduction, cell cycle regulation, and apoptosis (programmed cell death). They are involved in the regulation of cell growth, differentiation, and survival under physiological conditions.

When proto-oncogene proteins undergo mutations or aberrations in their expression levels, they can transform into oncogenic forms, leading to uncontrolled cell growth and division. These altered proteins are then referred to as oncogene products or oncoproteins. Oncogenic mutations can occur due to various factors, including genetic predisposition, environmental exposures, and aging.

Examples of proto-oncogene proteins include:

1. Ras proteins: Involved in signal transduction pathways that regulate cell growth and differentiation. Activating mutations in Ras genes are found in various human cancers.
2. Myc proteins: Regulate gene expression related to cell cycle progression, apoptosis, and metabolism. Overexpression of Myc proteins is associated with several types of cancer.
3. EGFR (Epidermal Growth Factor Receptor): A transmembrane receptor tyrosine kinase that regulates cell proliferation, survival, and differentiation. Mutations or overexpression of EGFR are linked to various malignancies, such as lung cancer and glioblastoma.
4. Src family kinases: Intracellular tyrosine kinases that regulate signal transduction pathways involved in cell proliferation, survival, and migration. Dysregulation of Src family kinases is implicated in several types of cancer.
5. Abl kinases: Cytoplasmic tyrosine kinases that regulate various cellular processes, including cell growth, differentiation, and stress responses. Aberrant activation of Abl kinases, as seen in chronic myelogenous leukemia (CML), leads to uncontrolled cell proliferation.

Understanding the roles of proto-oncogene proteins and their dysregulation in cancer development is essential for developing targeted cancer therapies that aim to inhibit or modulate these aberrant signaling pathways.

Receptor Protein-Tyrosine Kinases (RTKs) are a type of transmembrane receptors found on the cell surface that play a crucial role in signal transduction and regulation of various cellular processes, including cell growth, differentiation, metabolism, and survival. They are called "tyrosine kinases" because they possess an intrinsic enzymatic activity that catalyzes the transfer of a phosphate group from ATP to tyrosine residues on target proteins, thereby modulating their function.

RTKs are composed of three main domains: an extracellular domain that binds to specific ligands (growth factors, hormones, or cytokines), a transmembrane domain that spans the cell membrane, and an intracellular domain with tyrosine kinase activity. Upon ligand binding, RTKs undergo conformational changes that lead to their dimerization or oligomerization, which in turn activates their tyrosine kinase activity. Activated RTKs then phosphorylate specific tyrosine residues on downstream signaling proteins, initiating a cascade of intracellular signaling events that ultimately result in the appropriate cellular response.

Dysregulation of RTK signaling has been implicated in various human diseases, including cancer, diabetes, and developmental disorders. As such, RTKs are important targets for therapeutic intervention in these conditions.

Thymidine kinase (TK) is an enzyme that plays a crucial role in the synthesis of thymidine triphosphate (dTMP), a nucleotide required for DNA replication and repair. It catalyzes the phosphorylation of thymidine to thymidine monophosphate (dTMP) by transferring a phosphate group from adenosine triphosphate (ATP).

There are two major isoforms of thymidine kinase in humans: TK1 and TK2. TK1 is primarily found in the cytoplasm of proliferating cells, such as those involved in the cell cycle, while TK2 is located mainly in the mitochondria and is responsible for maintaining the dNTP pool required for mtDNA replication and repair.

Thymidine kinase activity has been used as a marker for cell proliferation, particularly in cancer cells, which often exhibit elevated levels of TK1 due to their high turnover rates. Additionally, measuring TK1 levels can help monitor the effectiveness of certain anticancer therapies that target DNA replication.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Phosphoprotein phosphatases (PPPs) are a family of enzymes that play a crucial role in the regulation of various cellular processes by removing phosphate groups from serine, threonine, and tyrosine residues on proteins. Phosphorylation is a post-translational modification that regulates protein function, localization, and stability, and dephosphorylation by PPPs is essential for maintaining the balance of this regulation.

The PPP family includes several subfamilies, such as PP1, PP2A, PP2B (also known as calcineurin), PP4, PP5, and PP6. Each subfamily has distinct substrate specificities and regulatory mechanisms. For example, PP1 and PP2A are involved in the regulation of metabolism, signal transduction, and cell cycle progression, while PP2B is involved in immune response and calcium signaling.

Dysregulation of PPPs has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, understanding the function and regulation of PPPs is important for developing therapeutic strategies to target these diseases.

I-kappa B kinase (IKK) is a protein complex that plays a crucial role in the activation of NF-kB (nuclear factor kappa-light-chain-enhancer of activated B cells), a transcription factor involved in the regulation of immune response, inflammation, cell survival, and proliferation.

The IKK complex is composed of two catalytic subunits, IKKα and IKKβ, and a regulatory subunit, IKKγ (also known as NEMO). Upon stimulation by various signals such as cytokines, pathogens, or stress, the IKK complex becomes activated and phosphorylates I-kappa B (IkB), an inhibitor protein that keeps NF-kB in an inactive state in the cytoplasm.

Once IkB is phosphorylated by the IKK complex, it undergoes ubiquitination and degradation, leading to the release and nuclear translocation of NF-kB, where it can bind to specific DNA sequences and regulate gene expression. Dysregulation of IKK activity has been implicated in various pathological conditions, including chronic inflammation, autoimmune diseases, and cancer.

Extracellular signal-regulated mitogen-activated protein kinases (ERKs or Extracellular signal-regulated kinases) are a subfamily of the MAPK (mitogen-activated protein kinase) family, which are serine/threonine protein kinases that regulate various cellular processes such as proliferation, differentiation, migration, and survival in response to extracellular signals.

ERKs are activated by a cascade of phosphorylation events initiated by the binding of growth factors, hormones, or other extracellular molecules to their respective receptors. This activation results in the formation of a complex signaling pathway that involves the sequential activation of several protein kinases, including Ras, Raf, MEK (MAPK/ERK kinase), and ERK.

Once activated, ERKs translocate to the nucleus where they phosphorylate and activate various transcription factors, leading to changes in gene expression that ultimately result in the appropriate cellular response. Dysregulation of the ERK signaling pathway has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

MAP Kinase Kinase 4 (MAP2K4 or MKK4) is a serine/threonine protein kinase that plays a crucial role in intracellular signal transduction pathways, particularly the mitogen-activated protein kinase (MAPK) cascades. These cascades are involved in various cellular processes such as proliferation, differentiation, survival, and apoptosis in response to extracellular stimuli like cytokines, growth factors, and stress signals.

MAP2K4 specifically activates the c-Jun N-terminal kinase (JNK) pathway by phosphorylating and activating JNK proteins. The activation of JNK leads to the phosphorylation and regulation of various transcription factors, ultimately influencing gene expression and cellular responses. Dysregulation of MAP2K4 has been implicated in several diseases, including cancer and inflammatory disorders.

A precipitin test is a type of immunodiagnostic test used to detect and measure the presence of specific antibodies or antigens in a patient's serum. The test is based on the principle of antigen-antibody interaction, where the addition of an antigen to a solution containing its corresponding antibody results in the formation of an insoluble immune complex known as a precipitin.

In this test, a small amount of the patient's serum is added to a solution containing a known antigen or antibody. If the patient has antibodies or antigens that correspond to the added reagent, they will bind and form a visible precipitate. The size and density of the precipitate can be used to quantify the amount of antibody or antigen present in the sample.

Precipitin tests are commonly used in the diagnosis of various infectious diseases, autoimmune disorders, and allergies. They can also be used in forensic science to identify biological samples. However, they have largely been replaced by more modern immunological techniques such as enzyme-linked immunosorbent assays (ELISAs) and radioimmunoassays (RIAs).

The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.

The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).

The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

1-Phosphatidylinositol 4-Kinase (PI4K) is a type of enzyme that belongs to the family of kinases, which are enzymes that transfer phosphate groups from high-energy donor molecules to specific target proteins or lipids in the cell. PI4K specifically phosphorylates the 4th position on the inositol ring of phosphatidylinositol (PI), a type of phospholipid found in the cell membrane, converting it to phosphatidylinositol 4-phosphate (PI4P).

PI4K has several isoforms, including PI4K alpha, beta, gamma, and delta, which are located in different cellular compartments and play distinct roles. For example, PI4K alpha and beta are primarily involved in vesicle trafficking and Golgi function, while PI4K gamma and delta are associated with the plasma membrane and regulate ion channels and other signaling pathways.

PI4P, the product of PI4K activity, is an important signaling molecule that regulates various cellular processes, including membrane trafficking, cytoskeleton organization, and protein sorting. Dysregulation of PI4K and its downstream pathways has been implicated in several human diseases, such as cancer, neurodegeneration, and viral infection.

HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.

HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.

It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

CDC2 and CDC28 are members of the Serine/Threonine protein kinase family, which play crucial roles in the regulation of the cell cycle. These kinases were originally identified in yeast (CDC28) and humans (CDC2), but they are highly conserved across eukaryotes.

CDC2-CDC28 Kinases function as a part of larger complexes, often associated with cyclins, to control different phases of the cell cycle by phosphorylating specific substrates at key regulatory points. The activity of CDC2-CDC28 Kinases is tightly regulated through various mechanisms, including phosphorylation, dephosphorylation, and protein binding interactions.

During the G2 phase of the cell cycle, CDC2-CDC28 Kinases are inactivated by phosphorylation at specific residues (Tyr15 and Thr14). As the cell approaches mitosis, a family of phosphatases called Cdc25 removes these inhibitory phosphates, leading to activation of the kinase. Activated CDC2-CDC28 Kinases then initiate mitotic processes such as chromosome condensation and nuclear envelope breakdown.

In summary, CDC2-CDC28 Kinases are essential regulators of the eukaryotic cell cycle, controlling various aspects of cell division through phosphorylation of specific substrates. Their activity is tightly regulated to ensure proper progression through the cell cycle and prevent uncontrolled cell growth, which can lead to diseases such as cancer.

Aurora kinases are a family of serine/threonine protein kinases that play crucial roles in the regulation of cell division. There are three members of the Aurora kinase family, designated as Aurora A, Aurora B, and Aurora C. These kinases are involved in the proper separation of chromosomes during mitosis and meiosis, and their dysregulation has been implicated in various types of cancer.

Aurora A is primarily located at the centrosomes and spindle poles during cell division, where it regulates centrosome maturation, bipolar spindle formation, and chromosome segregation. Aurora B, on the other hand, is a component of the chromosomal passenger complex (CPC) that localizes to the centromeres during prophase and moves to the spindle midzone during anaphase. It plays essential roles in kinetochore-microtubule attachment, chromosome alignment, and cytokinesis. Aurora C is most similar to Aurora B and appears to have overlapping functions with it, although its specific roles are less well understood.

Dysregulation of Aurora kinases has been associated with various types of cancer, including breast, ovarian, colon, and lung cancers. Overexpression or amplification of Aurora A is observed in many cancers, leading to chromosomal instability and aneuploidy. Inhibition of Aurora kinases has emerged as a potential therapeutic strategy for cancer treatment, with several small molecule inhibitors currently under investigation in clinical trials.

Rho-associated kinases (ROCKs) are serine/threonine kinases that are involved in the regulation of various cellular processes, including actin cytoskeleton organization, cell migration, and gene expression. They are named after their association with the small GTPase RhoA, which activates them upon binding.

ROCKs exist as two isoforms, ROCK1 and ROCK2, which share a high degree of sequence homology and have similar functions. They contain several functional domains, including a kinase domain, a coiled-coil region that mediates protein-protein interactions, and a Rho-binding domain (RBD) that binds to active RhoA.

Once activated by RhoA, ROCKs phosphorylate a variety of downstream targets, including myosin light chain (MLC), LIM kinase (LIMK), and moesin, leading to the regulation of actomyosin contractility, stress fiber formation, and focal adhesion turnover. Dysregulation of ROCK signaling has been implicated in various pathological conditions, such as cancer, cardiovascular diseases, neurological disorders, and fibrosis. Therefore, ROCKs have emerged as promising therapeutic targets for the treatment of these diseases.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.

The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.

After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.

Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.

Protein Kinase C-delta (PKC-δ) is a specific isoform of the Protein Kinase C (PKC) family, which are serine/threonine protein kinases that play crucial roles in various cellular signaling pathways. PKC-δ is involved in several cellular processes such as proliferation, differentiation, apoptosis, and motility. It is activated by second messengers like diacylglycerol (DAG) and calcium ions (Ca2+), and its activation leads to the phosphorylation of specific target proteins, thereby modulating their functions. Aberrant regulation of PKC-δ has been implicated in various diseases, including cancer and neurodegenerative disorders.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Protein Kinase C-alpha (PKC-α) is a specific isoform of the Protein Kinase C (PKC) family, which are serine/threonine protein kinases that play crucial roles in various cellular processes such as proliferation, differentiation, and apoptosis. PKC-α is activated by diacylglycerol (DAG) and calcium ions (Ca2+). It is involved in signal transduction pathways related to cell growth, differentiation, and oncogenic transformation. Mutations or dysregulation of PKC-alpha have been implicated in several diseases including cancer, diabetes, and neurological disorders.

Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.

Intracellular signaling peptides and proteins are molecules that play a crucial role in transmitting signals within cells, which ultimately lead to changes in cell behavior or function. These signals can originate from outside the cell (extracellular) or within the cell itself. Intracellular signaling molecules include various types of peptides and proteins, such as:

1. G-protein coupled receptors (GPCRs): These are seven-transmembrane domain receptors that bind to extracellular signaling molecules like hormones, neurotransmitters, or chemokines. Upon activation, they initiate a cascade of intracellular signals through G proteins and secondary messengers.
2. Receptor tyrosine kinases (RTKs): These are transmembrane receptors that bind to growth factors, cytokines, or hormones. Activation of RTKs leads to autophosphorylation of specific tyrosine residues, creating binding sites for intracellular signaling proteins such as adapter proteins, phosphatases, and enzymes like Ras, PI3K, and Src family kinases.
3. Second messenger systems: Intracellular second messengers are small molecules that amplify and propagate signals within the cell. Examples include cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), diacylglycerol (DAG), inositol triphosphate (IP3), calcium ions (Ca2+), and nitric oxide (NO). These second messengers activate or inhibit various downstream effectors, leading to changes in cellular responses.
4. Signal transduction cascades: Intracellular signaling proteins often form complex networks of interacting molecules that relay signals from the plasma membrane to the nucleus. These cascades involve kinases (protein kinases A, B, C, etc.), phosphatases, and adapter proteins, which ultimately regulate gene expression, cell cycle progression, metabolism, and other cellular processes.
5. Ubiquitination and proteasome degradation: Intracellular signaling pathways can also control protein stability by modulating ubiquitin-proteasome degradation. E3 ubiquitin ligases recognize specific substrates and conjugate them with ubiquitin molecules, targeting them for proteasomal degradation. This process regulates the abundance of key signaling proteins and contributes to signal termination or amplification.

In summary, intracellular signaling pathways involve a complex network of interacting proteins that relay signals from the plasma membrane to various cellular compartments, ultimately regulating gene expression, metabolism, and other cellular processes. Dysregulation of these pathways can contribute to disease development and progression, making them attractive targets for therapeutic intervention.

Glycogen synthase kinases (GSKs) are a family of enzymes that play a crucial role in the regulation of glycogen metabolism. Glycogen is a complex carbohydrate that serves as a primary energy storage form in animals, fungi, and bacteria.

GSKs function as serine/threonine protein kinases, which means they add phosphate groups to specific serine or threonine residues on their target proteins. In the case of glycogen synthase kinases, their primary target is glycogen synthase, an enzyme responsible for synthesizing glycogen from glucose-1-phosphate during the process of glycogenesis (glycogen synthesis).

There are several isoforms of GSKs identified in humans, including GSK3α and GSK3β. These kinases are involved in various cellular processes, such as:

1. Regulation of glycogen metabolism: By phosphorylating and inhibiting glycogen synthase, GSKs help control the balance between glycogen storage and glucose utilization.
2. Cell signaling pathways: GSKs participate in several intracellular signaling cascades, including the Wnt signaling pathway, insulin signaling pathway, and the PI3K/AKT pathway, which regulate various cellular functions such as proliferation, differentiation, survival, and metabolism.
3. Regulation of gene expression: GSKs can modulate transcription factors' activity, thereby influencing gene expression and contributing to various cellular responses.
4. Neuronal function: In the brain, GSKs are involved in regulating synaptic plasticity, learning, and memory processes.
5. Disease pathogenesis: Dysregulation of GSKs has been implicated in several diseases, such as diabetes, neurodegenerative disorders (e.g., Alzheimer's disease), and cancer.

In summary, glycogen synthase kinases are a family of protein kinases that regulate glycogen metabolism and participate in various cell signaling pathways, influencing numerous cellular functions and being implicated in several diseases.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

Protein-kinase B, also known as AKT, is a group of intracellular proteins that play a crucial role in various cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration. The AKT family includes three isoforms: AKT1, AKT2, and AKT3, which are encoded by the genes PKBalpha, PKBbeta, and PKBgamma, respectively.

Proto-oncogene proteins c-AKT refer to the normal, non-mutated forms of these proteins that are involved in the regulation of cell growth and survival under physiological conditions. However, when these genes are mutated or overexpressed, they can become oncogenes, leading to uncontrolled cell growth and cancer development.

Activation of c-AKT occurs through a signaling cascade that begins with the binding of extracellular ligands such as insulin-like growth factor 1 (IGF-1) or epidermal growth factor (EGF) to their respective receptors on the cell surface. This triggers a series of phosphorylation events that ultimately lead to the activation of c-AKT, which then phosphorylates downstream targets involved in various cellular processes.

In summary, proto-oncogene proteins c-AKT are normal intracellular proteins that play essential roles in regulating cell growth and survival under physiological conditions. However, their dysregulation can contribute to cancer development and progression.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Period (PER) circadian proteins are a group of proteins that play a crucial role in the regulation of circadian rhythms, which are physical, mental, and behavioral changes that follow a daily cycle. They are named after the PERIOD gene, whose protein product is one of the key components of the molecular circadian clock mechanism.

The molecular clock is a self-sustaining oscillator present in most organisms, from cyanobacteria to humans. In mammals, the molecular clock consists of two interlocking transcriptional-translational feedback loops that generate rhythmic expression of clock genes and their protein products with a period of approximately 24 hours.

The primary loop involves the positive regulators CLOCK and BMAL1, which heterodimerize and bind to E-box elements in the promoter regions of target genes, including PERIOD (PER) and CRYPTOCHROME (CRY) genes. Upon transcription and translation, PER and CRY proteins form a complex that translocates back into the nucleus, where it inhibits CLOCK-BMAL1-mediated transcription, thereby suppressing its own expression. After a certain period, the repressive complex dissociates, allowing for another cycle of transcription and translation to occur.

The second loop involves the regulation of additional clock genes such as REV-ERBα and RORα, which compete for binding to ROR response elements (ROREs) in the BMAL1 promoter, thereby modulating its expression level. REV-ERBα also represses PER and CRY transcription by recruiting histone deacetylases (HDACs) and nuclear receptor corepressor 1 (NCOR1).

Overall, Period circadian proteins are essential for the proper functioning of the molecular clock and the regulation of various physiological processes, including sleep-wake cycles, metabolism, hormone secretion, and cellular homeostasis. Dysregulation of these proteins has been implicated in several diseases, such as sleep disorders, metabolic syndromes, and cancer.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

Diacylglycerol kinase (DGK) is an enzyme that plays a role in regulating cell signaling pathways. It catalyzes the conversion of diacylglycerol (DAG), a lipid second messenger, to phosphatidic acid (PA). This reaction helps to terminate DAG-mediated signals and initiate PA-mediated signals, which are involved in various cellular processes such as proliferation, differentiation, and survival. There are several isoforms of DGK that differ in their regulation, subcellular localization, and substrate specificity. Inhibition or genetic deletion of DGK has been shown to affect a variety of physiological and pathological processes, including inflammation, immunity, cancer, and neurological disorders.

Cell cycle proteins are a group of regulatory proteins that control the progression of the cell cycle, which is the series of events that take place in a eukaryotic cell leading to its division and duplication. These proteins can be classified into several categories based on their functions during different stages of the cell cycle.

The major groups of cell cycle proteins include:

1. Cyclin-dependent kinases (CDKs): CDKs are serine/threonine protein kinases that regulate key transitions in the cell cycle. They require binding to a regulatory subunit called cyclin to become active. Different CDK-cyclin complexes are activated at different stages of the cell cycle.
2. Cyclins: Cyclins are a family of regulatory proteins that bind and activate CDKs. Their levels fluctuate throughout the cell cycle, with specific cyclins expressed during particular phases. For example, cyclin D is important for the G1 to S phase transition, while cyclin B is required for the G2 to M phase transition.
3. CDK inhibitors (CKIs): CKIs are regulatory proteins that bind to and inhibit CDKs, thereby preventing their activation. CKIs can be divided into two main families: the INK4 family and the Cip/Kip family. INK4 family members specifically inhibit CDK4 and CDK6, while Cip/Kip family members inhibit a broader range of CDKs.
4. Anaphase-promoting complex/cyclosome (APC/C): APC/C is an E3 ubiquitin ligase that targets specific proteins for degradation by the 26S proteasome. During the cell cycle, APC/C regulates the metaphase to anaphase transition and the exit from mitosis by targeting securin and cyclin B for degradation.
5. Other regulatory proteins: Several other proteins play crucial roles in regulating the cell cycle, such as p53, a transcription factor that responds to DNA damage and arrests the cell cycle, and the polo-like kinases (PLKs), which are involved in various aspects of mitosis.

Overall, cell cycle proteins work together to ensure the proper progression of the cell cycle, maintain genomic stability, and prevent uncontrolled cell growth, which can lead to cancer.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

Cyclin-Dependent Kinase 5 (CDK5) is a type of protein kinase that plays crucial roles in the regulation of various cellular processes, particularly in neurons. Unlike other cyclin-dependent kinases, CDK5 is activated by associating with regulatory subunits called cyclins, specifically cyclin I and cyclin D1, but not during the cell cycle.

CDK5 activity is primarily involved in the development and functioning of the nervous system, where it regulates neuronal migration, differentiation, and synaptic plasticity. It has been implicated in several neurological disorders, including Alzheimer's disease, Parkinson's disease, and various neurodevelopmental conditions.

CDK5 activity is tightly regulated by phosphorylation and interacting partners. Dysregulation of CDK5 can lead to abnormal neuronal function and contribute to the pathogenesis of neurological disorders.

Phloroglucinol is not strictly a medical term, but it is used in medicine and pharmacology. Phloroglucinol is an aromatic organic compound with the formula C6H6(OH)3. It is a white crystalline solid that is soluble in water and polar organic solvents.

In a medical context, phloroglucinol is most commonly used as a smooth muscle relaxant. It is often found in over-the-counter medications used to treat gastrointestinal symptoms such as abdominal cramps, spasms, and pain. Phloroglucinol works by relaxing the smooth muscles of the digestive tract, which can help to reduce spasms and relieve pain.

Phloroglucinol is also used in some countries as a treatment for kidney stones. It is believed to help to relax the ureter, the tube that connects the kidney to the bladder, making it easier to pass small kidney stones. However, its effectiveness for this use is not well established, and it is not approved by the U.S. Food and Drug Administration (FDA) for this purpose.

It's important to note that phloroglucinol should only be used under the guidance of a healthcare provider, as it can have side effects and interact with other medications.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

AMP-activated protein kinases (AMPK) are a group of heterotrimeric enzymes that play a crucial role in cellular energy homeostasis. They are composed of a catalytic subunit (α) and two regulatory subunits (β and γ). AMPK is activated under conditions of low energy charge, such as ATP depletion, hypoxia, or exercise, through an increase in the AMP:ATP ratio.

Once activated, AMPK phosphorylates and regulates various downstream targets involved in metabolic pathways, including glycolysis, fatty acid oxidation, and protein synthesis. This results in the inhibition of energy-consuming processes and the promotion of energy-producing processes, ultimately helping to restore cellular energy balance.

AMPK has been implicated in a variety of physiological processes, including glucose and lipid metabolism, autophagy, mitochondrial biogenesis, and inflammation. Dysregulation of AMPK activity has been linked to several diseases, such as diabetes, obesity, cancer, and neurodegenerative disorders. Therefore, AMPK is an attractive target for therapeutic interventions in these conditions.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Adaptor proteins are a type of protein that play a crucial role in intracellular signaling pathways by serving as a link between different components of the signaling complex. Specifically, "signal transducing adaptor proteins" refer to those adaptor proteins that are involved in signal transduction processes, where they help to transmit signals from the cell surface receptors to various intracellular effectors. These proteins typically contain modular domains that allow them to interact with multiple partners, thereby facilitating the formation of large signaling complexes and enabling the integration of signals from different pathways.

Signal transducing adaptor proteins can be classified into several families based on their structural features, including the Src homology 2 (SH2) domain, the Src homology 3 (SH3) domain, and the phosphotyrosine-binding (PTB) domain. These domains enable the adaptor proteins to recognize and bind to specific motifs on other signaling molecules, such as receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors.

One well-known example of a signal transducing adaptor protein is the growth factor receptor-bound protein 2 (Grb2), which contains an SH2 domain that binds to phosphotyrosine residues on activated receptor tyrosine kinases. Grb2 also contains an SH3 domain that interacts with proline-rich motifs on other signaling proteins, such as the guanine nucleotide exchange factor SOS. This interaction facilitates the activation of the Ras small GTPase and downstream signaling pathways involved in cell growth, differentiation, and survival.

Overall, signal transducing adaptor proteins play a critical role in regulating various cellular processes by modulating intracellular signaling pathways in response to extracellular stimuli. Dysregulation of these proteins has been implicated in various diseases, including cancer and inflammatory disorders.

Cyclic adenosine monophosphate (cAMP) is a key secondary messenger in many biological processes, including the regulation of metabolism, gene expression, and cellular excitability. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase and is degraded by the enzyme phosphodiesterase.

In the body, cAMP plays a crucial role in mediating the effects of hormones and neurotransmitters on target cells. For example, when a hormone binds to its receptor on the surface of a cell, it can activate a G protein, which in turn activates adenylyl cyclase to produce cAMP. The increased levels of cAMP then activate various effector proteins, such as protein kinases, which go on to regulate various cellular processes.

Overall, the regulation of cAMP levels is critical for maintaining proper cellular function and homeostasis, and abnormalities in cAMP signaling have been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Dietary proteins are sources of protein that come from the foods we eat. Protein is an essential nutrient for the human body, required for various bodily functions such as growth, repair, and immune function. Dietary proteins are broken down into amino acids during digestion, which are then absorbed and used to synthesize new proteins in the body.

Dietary proteins can be classified as complete or incomplete based on their essential amino acid content. Complete proteins contain all nine essential amino acids that cannot be produced by the human body and must be obtained through the diet. Examples of complete protein sources include meat, poultry, fish, eggs, dairy products, soy, and quinoa.

Incomplete proteins lack one or more essential amino acids and are typically found in plant-based foods such as grains, legumes, nuts, and seeds. However, by combining different incomplete protein sources, it is possible to obtain all the essential amino acids needed for a complete protein diet. This concept is known as complementary proteins.

It's important to note that while dietary proteins are essential for good health, excessive protein intake can have negative effects on the body, such as increased stress on the kidneys and bones. Therefore, it's recommended to consume protein in moderation as part of a balanced and varied diet.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Focal Adhesion Kinase 1 (FAK1), also known as Protein Tyrosine Kinase 2 (PTK2), is a cytoplasmic tyrosine kinase that plays a crucial role in cellular processes such as cell adhesion, migration, and survival. It is recruited to focal adhesions, which are specialized structures that form at the sites of integrin-mediated attachment of the cell to the extracellular matrix (ECM).

FAK1 becomes activated through autophosphorylation upon integrin clustering and ECM binding. Once activated, FAK1 can phosphorylate various downstream substrates, leading to the activation of several signaling pathways that regulate cell behavior. These pathways include the Ras/MAPK, PI3K/AKT, and JNK signaling cascades, which are involved in cell proliferation, survival, and motility.

FAK1 has been implicated in various physiological and pathological processes, including embryonic development, wound healing, angiogenesis, and tumorigenesis. Dysregulation of FAK1 signaling has been associated with several diseases, such as cancer, fibrosis, and neurological disorders. Therefore, FAK1 is considered a potential therapeutic target for the treatment of these conditions.

Polylysine is not a medical term per se, but it is a term used in biochemistry and medicine. Polylysine refers to a synthetic polymer of the amino acid lysine, which is linked together by peptide bonds to form a long, unbranched chain. It is often used in laboratory settings as a tool for scientific research, particularly in the study of protein-protein interactions and cellular uptake mechanisms.

In medicine, polylysine has been explored as a potential drug delivery vehicle, as it can be chemically modified to carry drugs or other therapeutic agents into cells. However, its use in clinical settings is not yet widespread. It's important to note that the term 'polylysine' itself does not have a specific medical definition, but rather refers to a class of biochemical compounds with certain properties.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

Heparin is defined as a highly sulfated glycosaminoglycan (a type of polysaccharide) that is widely present in many tissues, but is most commonly derived from the mucosal tissues of mammalian lungs or intestinal mucosa. It is an anticoagulant that acts as an inhibitor of several enzymes involved in the blood coagulation cascade, primarily by activating antithrombin III which then neutralizes thrombin and other clotting factors.

Heparin is used medically to prevent and treat thromboembolic disorders such as deep vein thrombosis, pulmonary embolism, and certain types of heart attacks. It can also be used during hemodialysis, cardiac bypass surgery, and other medical procedures to prevent the formation of blood clots.

It's important to note that while heparin is a powerful anticoagulant, it does not have any fibrinolytic activity, meaning it cannot dissolve existing blood clots. Instead, it prevents new clots from forming and stops existing clots from growing larger.

Saccharomyces cerevisiae proteins are the proteins that are produced by the budding yeast, Saccharomyces cerevisiae. This organism is a single-celled eukaryote that has been widely used as a model organism in scientific research for many years due to its relatively simple genetic makeup and its similarity to higher eukaryotic cells.

The genome of Saccharomyces cerevisiae has been fully sequenced, and it is estimated to contain approximately 6,000 genes that encode proteins. These proteins play a wide variety of roles in the cell, including catalyzing metabolic reactions, regulating gene expression, maintaining the structure of the cell, and responding to environmental stimuli.

Many Saccharomyces cerevisiae proteins have human homologs and are involved in similar biological processes, making this organism a valuable tool for studying human disease. For example, many of the proteins involved in DNA replication, repair, and recombination in yeast have human counterparts that are associated with cancer and other diseases. By studying these proteins in yeast, researchers can gain insights into their function and regulation in humans, which may lead to new treatments for disease.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Dopamine and cAMP-regulated phosphoprotein 32 (DARPP-32) is a protein that plays a crucial role in the regulation of signal transduction pathways in the brain. It is primarily expressed in neurons of the striatum, a region involved in movement control, motivation, and reward processing.

DARPP-32 acts as a molecular switch in response to various neurotransmitters, including dopamine and glutamate. When phosphorylated by protein kinase A (PKA), DARPP-32 inhibits protein phosphatase-1 (PP-1), thereby enhancing the effects of PKA and promoting long-term changes in synaptic plasticity. Conversely, when phosphorylated by other kinases such as cyclin-dependent kinase 5 (Cdk5) or protein kinase C (PKC), DARPP-32 inhibits PKA, counteracting its effects.

Dysregulation of DARPP-32 has been implicated in several neurological and psychiatric disorders, including drug addiction, Parkinson's disease, and schizophrenia. Therefore, understanding the molecular mechanisms underlying DARPP-32 function is essential for developing novel therapeutic strategies to treat these conditions.

Soybean proteins are the proteins derived from soybeans, a legume native to East Asia. Soybeans contain approximately 40% protein by weight, making them a significant source of plant-based protein. The two major types of soy protein are:

1. Soy protein isolate (SPI): This is a highly refined protein that contains at least 90% protein by weight. It is made by removing carbohydrates and fiber from defatted soy flour, leaving behind a protein-rich powder. SPI is often used as an ingredient in various food products, including meat alternatives, energy bars, and beverages.
2. Soy protein concentrate (SPC): This type of soy protein contains approximately 70% protein by weight. It is made by removing some of the carbohydrates from defatted soy flour, leaving behind a higher concentration of proteins. SPC has applications in food and industrial uses, such as in textured vegetable protein (TVP) for meat alternatives, baked goods, and functional foods.

Soy proteins are considered high-quality proteins due to their complete amino acid profile, containing all nine essential amino acids necessary for human nutrition. They also have various health benefits, such as lowering cholesterol levels, improving bone health, and promoting muscle growth and maintenance. However, it is important to note that soy protein consumption should be balanced with other protein sources to ensure a diverse intake of nutrients.

Myosin-Light-Chain Kinase (MLCK) is an enzyme that plays a crucial role in muscle contraction. It phosphorylates the regulatory light chains of myosin, a protein involved in muscle contraction, leading to the activation of myosin and the initiation of the contractile process. MLCK is activated by calcium ions and calmodulin, and its activity is essential for various cellular processes, including cytokinesis, cell motility, and maintenance of cell shape. In addition to its role in muscle contraction, MLCK has been implicated in several pathological conditions, such as hypertension, atherosclerosis, and cancer.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

The cell cycle is a series of events that take place in a cell leading to its division and duplication. It consists of four main phases: G1 phase, S phase, G2 phase, and M phase.

During the G1 phase, the cell grows in size and synthesizes mRNA and proteins in preparation for DNA replication. In the S phase, the cell's DNA is copied, resulting in two complete sets of chromosomes. During the G2 phase, the cell continues to grow and produces more proteins and organelles necessary for cell division.

The M phase is the final stage of the cell cycle and consists of mitosis (nuclear division) and cytokinesis (cytoplasmic division). Mitosis results in two genetically identical daughter nuclei, while cytokinesis divides the cytoplasm and creates two separate daughter cells.

The cell cycle is regulated by various checkpoints that ensure the proper completion of each phase before progressing to the next. These checkpoints help prevent errors in DNA replication and division, which can lead to mutations and cancer.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Tetradecanoylphorbol acetate (TPA) is defined as a pharmacological agent that is a derivative of the phorbol ester family. It is a potent tumor promoter and activator of protein kinase C (PKC), a group of enzymes that play a role in various cellular processes such as signal transduction, proliferation, and differentiation. TPA has been widely used in research to study PKC-mediated signaling pathways and its role in cancer development and progression. It is also used in topical treatments for skin conditions such as psoriasis.

Janus Kinase 2 (JAK2) is a tyrosine kinase enzyme that plays a crucial role in intracellular signal transduction. It is named after the Roman god Janus, who is depicted with two faces, as JAK2 has two similar phosphate-transferring domains. JAK2 is involved in various cytokine receptor-mediated signaling pathways and contributes to hematopoiesis, immune function, and cell growth.

Mutations in the JAK2 gene have been associated with several myeloproliferative neoplasms (MPNs), including polycythemia vera, essential thrombocythemia, and primary myelofibrosis. The most common mutation is JAK2 V617F, which results in a constitutively active enzyme that promotes uncontrolled cell proliferation and survival, contributing to the development of these MPNs.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

3T3 cells are a type of cell line that is commonly used in scientific research. The name "3T3" is derived from the fact that these cells were developed by treating mouse embryo cells with a chemical called trypsin and then culturing them in a flask at a temperature of 37 degrees Celsius.

Specifically, 3T3 cells are a type of fibroblast, which is a type of cell that is responsible for producing connective tissue in the body. They are often used in studies involving cell growth and proliferation, as well as in toxicity tests and drug screening assays.

One particularly well-known use of 3T3 cells is in the 3T3-L1 cell line, which is a subtype of 3T3 cells that can be differentiated into adipocytes (fat cells) under certain conditions. These cells are often used in studies of adipose tissue biology and obesity.

It's important to note that because 3T3 cells are a type of immortalized cell line, they do not always behave exactly the same way as primary cells (cells that are taken directly from a living organism). As such, researchers must be careful when interpreting results obtained using 3T3 cells and consider any potential limitations or artifacts that may arise due to their use.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Focal adhesion protein-tyrosine kinases (FAKs) are a group of non-receptor tyrosine kinases that play crucial roles in the regulation of various cellular processes, including cell adhesion, migration, proliferation, and survival. They are primarily localized at focal adhesions, which are specialized structures formed at the sites of integrin-mediated attachment of cells to the extracellular matrix (ECM).

FAKs consist of two major domains: an N-terminal FERM (4.1 protein, ezrin, radixin, moesin) domain and a C-terminal kinase domain. The FERM domain is responsible for the interaction with various proteins, including integrins, growth factor receptors, and cytoskeletal components, while the kinase domain possesses enzymatic activity that phosphorylates tyrosine residues on target proteins.

FAKs are activated in response to various extracellular signals, such as ECM stiffness, growth factors, and integrin engagement. Once activated, FAKs initiate a cascade of intracellular signaling events that ultimately regulate cell behavior. Dysregulation of FAK signaling has been implicated in several pathological conditions, including cancer, fibrosis, and cardiovascular diseases.

In summary, focal adhesion protein-tyrosine kinases are essential regulators of cellular processes that localize to focal adhesions and modulate intracellular signaling pathways in response to extracellular cues.

Cell division is the process by which a single eukaryotic cell (a cell with a true nucleus) divides into two identical daughter cells. This complex process involves several stages, including replication of DNA, separation of chromosomes, and division of the cytoplasm. There are two main types of cell division: mitosis and meiosis.

Mitosis is the type of cell division that results in two genetically identical daughter cells. It is a fundamental process for growth, development, and tissue repair in multicellular organisms. The stages of mitosis include prophase, prometaphase, metaphase, anaphase, and telophase, followed by cytokinesis, which divides the cytoplasm.

Meiosis, on the other hand, is a type of cell division that occurs in the gonads (ovaries and testes) during the production of gametes (sex cells). Meiosis results in four genetically unique daughter cells, each with half the number of chromosomes as the parent cell. This process is essential for sexual reproduction and genetic diversity. The stages of meiosis include meiosis I and meiosis II, which are further divided into prophase, prometaphase, metaphase, anaphase, and telophase.

In summary, cell division is the process by which a single cell divides into two daughter cells, either through mitosis or meiosis. This process is critical for growth, development, tissue repair, and sexual reproduction in multicellular organisms.

Vegetable proteins, also known as plant-based proteins, are nitrogenous organic compounds derived from plants. These proteins are composed of amino acid chains that are essential for the growth, repair, and maintenance of body tissues. Vegetable proteins can be found in a wide variety of plant sources such as legumes (e.g., beans, lentils, peas), grains (e.g., rice, wheat, corn), nuts, seeds, and vegetables.

It is important to note that while vegetable proteins are often considered "incomplete" because they may lack one or more of the essential amino acids found in animal-based proteins, consuming a variety of plant-based protein sources throughout the day can provide all the necessary amino acids for a healthy diet. Vegetarian and vegan diets that are well-planned can meet protein needs without the use of animal products.

Mammary glands are specialized exocrine glands found in mammals, including humans and other animals. These glands are responsible for producing milk, which is used to nurse offspring after birth. The mammary glands are located in the breast region of female mammals and are usually rudimentary or absent in males.

In animals, mammary glands can vary in number and location depending on the species. For example, humans and other primates have two mammary glands, one in each breast. Cows, goats, and sheep, on the other hand, have multiple pairs of mammary glands located in their lower abdominal region.

Mammary glands are made up of several structures, including lobules, ducts, and connective tissue. The lobules contain clusters of milk-secreting cells called alveoli, which produce and store milk. The ducts transport the milk from the lobules to the nipple, where it is released during lactation.

Mammary glands are an essential feature of mammals, as they provide a source of nutrition for newborn offspring. They also play a role in the development and maintenance of the mother-infant bond, as nursing provides opportunities for physical contact and bonding between the mother and her young.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Isoquinolines are not a medical term per se, but a chemical classification. They refer to a class of organic compounds that consist of a benzene ring fused to a piperidine ring. This structure is similar to that of quinoline, but with the nitrogen atom located at a different position in the ring.

Isoquinolines have various biological activities and can be found in some natural products, including certain alkaloids. Some isoquinoline derivatives have been developed as drugs for the treatment of various conditions, such as cardiovascular diseases, neurological disorders, and cancer. However, specific medical definitions related to isoquinolines typically refer to the use or effects of these specific drugs rather than the broader class of compounds.

Ribosomal Protein S6 Kinases, 90-kDa (RSKs) are a group of serine/threonine protein kinases that play a crucial role in signal transduction pathways linked to cell growth, proliferation, and survival. They are so named because they were initially discovered as protein kinases that phosphorylate the 40S ribosomal protein S6, a component of the ribosome involved in translation regulation.

RSKs consist of four isoforms (RSK1-4) encoded by separate genes but sharing similar structures and functions. They have an N-terminal kinase domain, a C-terminal kinase domain, and a linker region containing several regulatory phosphorylation sites. RSKs are activated through the Ras/MAPK (Mitogen-Activated Protein Kinase) signaling cascade, where Ras activates Raf, which in turn activates MEK, ultimately leading to the activation of ERK. Activated ERK then phosphorylates and activates RSKs by promoting a conformational change that allows for autophosphorylation and full kinase activity.

Once activated, RSKs can phosphorylate various substrates involved in transcriptional regulation, cytoskeletal reorganization, protein synthesis, and cell cycle progression. Dysregulation of RSK signaling has been implicated in several diseases, including cancer, where they contribute to tumor growth, metastasis, and drug resistance. Therefore, RSKs are considered potential therapeutic targets for cancer treatment.

Protein Kinase C-epsilon (PKCε) is a serine-threonine protein kinase that belongs to the family of Protein Kinase C (PKC) enzymes. These enzymes play crucial roles in various cellular processes, including signal transduction, cell survival, differentiation, and apoptosis.

PKCε is specifically involved in regulating several signaling pathways related to inflammation, proliferation, and carcinogenesis. It can be activated by different stimuli such as diacylglycerol (DAG) and phorbol esters, which lead to its translocation from the cytosol to the plasma membrane, where it phosphorylates and modulates the activity of various target proteins.

Abnormal regulation or expression of PKCε has been implicated in several diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders. Therefore, PKCε is considered a potential therapeutic target for these conditions, and inhibitors of this enzyme are being developed and tested in preclinical and clinical studies.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Cytoplasm is the material within a eukaryotic cell (a cell with a true nucleus) that lies between the nuclear membrane and the cell membrane. It is composed of an aqueous solution called cytosol, in which various organelles such as mitochondria, ribosomes, endoplasmic reticulum, Golgi apparatus, lysosomes, and vacuoles are suspended. Cytoplasm also contains a variety of dissolved nutrients, metabolites, ions, and enzymes that are involved in various cellular processes such as metabolism, signaling, and transport. It is where most of the cell's metabolic activities take place, and it plays a crucial role in maintaining the structure and function of the cell.

MAP Kinase Kinase Kinase 1 (MAP3K1) is a serine/threonine protein kinase that belongs to the MAPKKK family. It plays a crucial role in intracellular signaling pathways, particularly the mitogen-activated protein kinase (MAPK) cascades. These cascades are involved in various cellular processes such as proliferation, differentiation, and apoptosis.

MAP3K1 activates MAPKKs (MAP Kinase Kinases) by phosphorylating them on specific serine and threonine residues. In turn, activated MAPKKs phosphorylate and activate MAPKs, which then regulate the activity of various transcription factors and other downstream targets.

Mutations in MAP3K1 have been implicated in several human diseases, including cancer and developmental disorders. For example, gain-of-function mutations in MAP3K1 can lead to aberrant activation of MAPK signaling pathways, promoting tumor growth and progression. On the other hand, loss-of-function mutations in MAP3K1 have been associated with developmental defects such as craniofacial anomalies and skeletal malformations.

Calcium-calmodulin-dependent protein kinase type 2 (CAMK2) is a type of serine/threonine protein kinase that plays a crucial role in signal transduction pathways related to synaptic plasticity, learning, and memory. It is composed of four subunits, each with a catalytic domain and a regulatory domain that contains an autoinhibitory region and a calmodulin-binding site.

The activation of CAMK2 requires the binding of calcium ions (Ca^2+^) to calmodulin, which then binds to the regulatory domain of CAMK2, relieving the autoinhibition and allowing the kinase to phosphorylate its substrates. Once activated, CAMK2 can also undergo a process called autophosphorylation, which results in a persistent activation state that can last for hours or even days.

CAMK2 has many downstream targets, including ion channels, transcription factors, and other protein kinases. Dysregulation of CAMK2 signaling has been implicated in various neurological disorders, such as Alzheimer's disease, Parkinson's disease, and epilepsy.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Axin protein is a type of intracellular protein that plays a crucial role in regulating the Wnt signaling pathway, which is essential for various developmental processes and tissue homeostasis. Axin serves as a scaffold protein that facilitates the formation of a complex with other proteins involved in the degradation of β-catenin, a key component of the Wnt signalling cascade. By promoting the phosphorylation and subsequent degradation of β-catenin, Axin helps to maintain its levels in the cell and ensures proper regulation of gene transcription. Mutations in the AXIN gene can lead to abnormal Wnt signaling and have been associated with various diseases, including cancer.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Protein Kinase C beta (PKCβ) is a serine-threonine protein kinase that belongs to the family of Protein Kinase C (PKC) enzymes. It plays a crucial role in various cellular processes, including signal transduction, cell survival, differentiation, and apoptosis. PKCβ is activated by diacylglycerol (DAG) and calcium ions (Ca2+), which results in its translocation from the cytosol to the plasma membrane, where it phosphorylates downstream target proteins.

There are two isoforms of PKCβ, PKCβI and PKCβII, which differ in their regulatory domains but have similar catalytic domains. PKCβ has been implicated in several diseases, including cancer, diabetes, and inflammatory disorders, making it a potential therapeutic target for drug development.

A dose-response relationship in the context of drugs refers to the changes in the effects or symptoms that occur as the dose of a drug is increased or decreased. Generally, as the dose of a drug is increased, the severity or intensity of its effects also increases. Conversely, as the dose is decreased, the effects of the drug become less severe or may disappear altogether.

The dose-response relationship is an important concept in pharmacology and toxicology because it helps to establish the safe and effective dosage range for a drug. By understanding how changes in the dose of a drug affect its therapeutic and adverse effects, healthcare providers can optimize treatment plans for their patients while minimizing the risk of harm.

The dose-response relationship is typically depicted as a curve that shows the relationship between the dose of a drug and its effect. The shape of the curve may vary depending on the drug and the specific effect being measured. Some drugs may have a steep dose-response curve, meaning that small changes in the dose can result in large differences in the effect. Other drugs may have a more gradual dose-response curve, where larger changes in the dose are needed to produce significant effects.

In addition to helping establish safe and effective dosages, the dose-response relationship is also used to evaluate the potential therapeutic benefits and risks of new drugs during clinical trials. By systematically testing different doses of a drug in controlled studies, researchers can identify the optimal dosage range for the drug and assess its safety and efficacy.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

I'm sorry for any confusion, but "Pyrvinium compounds" is not a widely recognized medical term or category. Pyrvinium is an antiparasitic medication that is used to treat certain types of intestinal worm infections. The most common compound is Pyrvinium pamoate, which is the active ingredient in the branded medication "Vanquin."

Pyrvinium works by inhibiting the metabolism of the parasites, leading to their death and elimination from the body. It'… Read more

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

MAP Kinase Kinase 2 (MKK2 or MAP2K2) is a serine/threonine protein kinase that plays a crucial role in the mitogen-activated protein kinase (MAPK) signal transduction pathways. These pathways are involved in various cellular processes, including proliferation, differentiation, and stress responses. MKK2 is specifically a part of the JNK (c-Jun N-terminal kinase) signaling module, where it acts as an upstream kinase that activates JNK by phosphorylating its activation loop at threonine and tyrosine residues.

MKK2 is activated in response to various stimuli such as cytokines, growth factors, and environmental stresses. Once activated, MKK2 phosphorylates and activates JNK, which then regulates the activity of several transcription factors leading to changes in gene expression and ultimately modulating cellular responses.

In summary, MAP Kinase Kinase 2 is a protein kinase involved in the activation of the JNK signaling pathway, which plays essential roles in regulating various cellular processes, including stress response, inflammation, and programmed cell death (apoptosis).

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Cyclin-Dependent Kinase 2 (CDK2) is a type of enzyme that plays a crucial role in the regulation of the cell cycle, which is the process by which cells grow and divide. CDK2 is activated when it binds to a regulatory subunit called a cyclin.

During the cell cycle, CDK2 helps to control the progression from the G1 phase to the S phase, where DNA replication occurs. Specifically, CDK2 phosphorylates various target proteins that are involved in the regulation of DNA replication and the initiation of mitosis, which is the process of cell division.

CDK2 activity is tightly regulated through a variety of mechanisms, including phosphorylation, dephosphorylation, and protein degradation. Dysregulation of CDK2 activity has been implicated in various human diseases, including cancer. Therefore, CDK2 is an important target for the development of therapies aimed at treating these diseases.

Protein Phosphatase 2 (PP2A) is a type of serine/threonine protein phosphatase that plays a crucial role in the regulation of various cellular processes, including signal transduction, cell cycle progression, and metabolism. PP2A is a heterotrimeric enzyme composed of a catalytic subunit (C), a regulatory subunit A (A), and a variable regulatory subunit B (B). The different combinations of the B subunits confer specificity to PP2A, allowing it to regulate a diverse array of cellular targets.

PP2A is responsible for dephosphorylating many proteins that have been previously phosphorylated by protein kinases. This function is essential for maintaining the balance of phosphorylation and dephosphorylation in cells, which is necessary for proper protein function and cell signaling. Dysregulation of PP2A has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Cyclic guanosine monophosphate (cGMP)-dependent protein kinases (PKGs) are a type of enzyme that add phosphate groups to other proteins, thereby modifying their function. These kinases are activated by cGMP, which is a second messenger molecule that helps transmit signals within cells. PKGs play important roles in various cellular processes, including smooth muscle relaxation, platelet aggregation, and cardiac contractility. They have been implicated in the regulation of a number of physiological functions, such as blood flow, inflammation, and learning and memory. There are two main isoforms of cGMP-dependent protein kinases, PKG I and PKG II, which differ in their tissue distribution, regulatory properties, and substrate specificity.

Androstadienes are a class of steroid hormones that are derived from androstenedione, which is a weak male sex hormone. Androstadienes include various compounds such as androstadiene-3,17-dione and androstanedione, which are intermediate products in the biosynthesis of more potent androgens like testosterone and dihydrotestosterone.

Androstadienes are present in both males and females but are found in higher concentrations in men. They can be detected in various bodily fluids, including blood, urine, sweat, and semen. In addition to their role in steroid hormone synthesis, androstadienes have been studied for their potential use as biomarkers of physiological processes and disease states.

It's worth noting that androstadienes are sometimes referred to as "androstenes" in the literature, although this term can also refer to other related compounds.

Flavonoids are a type of plant compounds with antioxidant properties that are beneficial to health. They are found in various fruits, vegetables, grains, and wine. Flavonoids have been studied for their potential to prevent chronic diseases such as heart disease and cancer due to their ability to reduce inflammation and oxidative stress.

There are several subclasses of flavonoids, including:

1. Flavanols: Found in tea, chocolate, grapes, and berries. They have been shown to improve blood flow and lower blood pressure.
2. Flavones: Found in parsley, celery, and citrus fruits. They have anti-inflammatory and antioxidant properties.
3. Flavanonols: Found in citrus fruits, onions, and tea. They have been shown to improve blood flow and reduce inflammation.
4. Isoflavones: Found in soybeans and legumes. They have estrogen-like effects and may help prevent hormone-related cancers.
5. Anthocyanidins: Found in berries, grapes, and other fruits. They have antioxidant properties and may help improve vision and memory.

It is important to note that while flavonoids have potential health benefits, they should not be used as a substitute for medical treatment or a healthy lifestyle. It is always best to consult with a healthcare professional before starting any new supplement regimen.

Calmodulin is a small, ubiquitous calcium-binding protein that plays a critical role in various intracellular signaling pathways. It functions as a calcium sensor, binding to and regulating the activity of numerous target proteins upon calcium ion (Ca^2+^) binding. Calmodulin is expressed in all eukaryotic cells and participates in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, metabolism, and cell cycle progression.

The protein contains four EF-hand motifs that can bind Ca^2+^ ions. Upon calcium binding, conformational changes occur in the calmodulin structure, exposing hydrophobic surfaces that facilitate its interaction with target proteins. Calmodulin's targets include enzymes (such as protein kinases and phosphatases), ion channels, transporters, and cytoskeletal components. By modulating the activity of these proteins, calmodulin helps regulate essential cellular functions in response to changes in intracellular Ca^2+^ concentrations.

Calmodulin's molecular weight is approximately 17 kDa, and it consists of a single polypeptide chain with 148-150 amino acid residues. The protein can be found in both the cytoplasm and the nucleus of cells. In addition to its role as a calcium sensor, calmodulin has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders.

Indole is not strictly a medical term, but it is a chemical compound that can be found in the human body and has relevance to medical and biological research. Indoles are organic compounds that contain a bicyclic structure consisting of a six-membered benzene ring fused to a five-membered pyrrole ring.

In the context of medicine, indoles are particularly relevant due to their presence in certain hormones and other biologically active molecules. For example, the neurotransmitter serotonin contains an indole ring, as does the hormone melatonin. Indoles can also be found in various plant-based foods, such as cruciferous vegetables (e.g., broccoli, kale), and have been studied for their potential health benefits.

Some indoles, like indole-3-carbinol and diindolylmethane, are found in these vegetables and can have anti-cancer properties by modulating estrogen metabolism, reducing inflammation, and promoting cell death (apoptosis) in cancer cells. However, it is essential to note that further research is needed to fully understand the potential health benefits and risks associated with indoles.

Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.

The process typically involves the following steps:

1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.

Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.

Phosphorylase Kinase (PhK) is a key enzyme in the regulation of glycogen metabolism, primarily involved in the breakdown of glycogen to glucose-1-phosphate. It is a serine/threonine protein kinase that catalyzes the phosphorylation of glycogen phosphorylase b, an isoform of glycogen phosphorylase, converting it into its active form, glycogen phosphorylase a.

PhK is composed of four different subunits: α, β, γ, and δ. The γ subunit contains the catalytic site, while the other subunits play regulatory roles. PhK itself can be activated by calcium ions (Ca2+) and protein kinase A (PKA)-mediated phosphorylation.

Phosphorylase Kinase is primarily located in the sarcoplasmic reticulum of muscle cells, where it plays a crucial role in regulating energy production during muscle contraction and relaxation. Dysregulation or mutations in PhK have been implicated in several genetic disorders, such as Debré-akaki syndrome, which is characterized by muscle weakness and cardiac abnormalities.

Trypsin is a proteolytic enzyme, specifically a serine protease, that is secreted by the pancreas as an inactive precursor, trypsinogen. Trypsinogen is converted into its active form, trypsin, in the small intestine by enterokinase, which is produced by the intestinal mucosa.

Trypsin plays a crucial role in digestion by cleaving proteins into smaller peptides at specific arginine and lysine residues. This enzyme helps to break down dietary proteins into amino acids, allowing for their absorption and utilization by the body. Additionally, trypsin can activate other zymogenic pancreatic enzymes, such as chymotrypsinogen and procarboxypeptidases, thereby contributing to overall protein digestion.

TOR (Target Of Rapamycin) Serine-Threonine Kinases are a family of conserved protein kinases that play crucial roles in the regulation of cell growth, proliferation, and metabolism in response to various environmental cues such as nutrients, growth factors, and energy status. They are named after their ability to phosphorylate serine and threonine residues on target proteins.

Mammalian cells express two distinct TOR kinases, mTORC1 and mTORC2, which have different protein compositions and functions. mTORC1 is rapamycin-sensitive and regulates cell growth, proliferation, and metabolism by phosphorylating downstream targets such as p70S6 kinase and 4E-BP1, thereby controlling protein synthesis, autophagy, and lysosome biogenesis. mTORC2 is rapamycin-insensitive and regulates cell survival, cytoskeleton organization, and metabolism by phosphorylating AGC kinases such as AKT and PKCα.

Dysregulation of TOR Serine-Threonine Kinases has been implicated in various human diseases, including cancer, diabetes, and neurological disorders. Therefore, targeting TOR kinases has emerged as a promising therapeutic strategy for the treatment of these diseases.

Phosphorus radioisotopes are radioactive isotopes or variants of the element phosphorus that emit radiation. Phosphorus has several radioisotopes, with the most common ones being phosphorus-32 (^32P) and phosphorus-33 (^33P). These radioisotopes are used in various medical applications such as cancer treatment and diagnostic procedures.

Phosphorus-32 has a half-life of approximately 14.3 days and emits beta particles, making it useful for treating certain types of cancer, such as leukemia and lymphoma. It can also be used in brachytherapy, a type of radiation therapy that involves placing a radioactive source close to the tumor.

Phosphorus-33 has a shorter half-life of approximately 25.4 days and emits both beta particles and gamma rays. This makes it useful for diagnostic procedures, such as positron emission tomography (PET) scans, where the gamma rays can be detected and used to create images of the body's internal structures.

It is important to note that handling and using radioisotopes requires specialized training and equipment to ensure safety and prevent radiation exposure.

Protein hydrolysates are defined as proteins that have been broken down into smaller peptide chains or individual amino acids through a process called hydrolysis. This process involves the use of water, enzymes, or acids to break the bonds between the amino acids in the protein molecule.

Protein hydrolysates are often used in medical and nutritional applications because they are easier to digest and absorb than intact proteins. They are also less likely to cause allergic reactions or digestive discomfort in individuals who have difficulty tolerating whole proteins. Protein hydrolysates can be derived from a variety of sources, including animal proteins such as collagen and casein, as well as plant proteins such as soy and wheat.

In addition to their use in medical and nutritional applications, protein hydrolysates are also used in the food industry as flavor enhancers, emulsifiers, and texturizers. They are commonly found in products such as infant formula, sports drinks, and clinical nutrition formulas.

Small interfering RNA (siRNA) is a type of short, double-stranded RNA molecule that plays a role in the RNA interference (RNAi) pathway. The RNAi pathway is a natural cellular process that regulates gene expression by targeting and destroying specific messenger RNA (mRNA) molecules, thereby preventing the translation of those mRNAs into proteins.

SiRNAs are typically 20-25 base pairs in length and are generated from longer double-stranded RNA precursors called hairpin RNAs or dsRNAs by an enzyme called Dicer. Once generated, siRNAs associate with a protein complex called the RNA-induced silencing complex (RISC), which uses one strand of the siRNA (the guide strand) to recognize and bind to complementary sequences in the target mRNA. The RISC then cleaves the target mRNA, leading to its degradation and the inhibition of protein synthesis.

SiRNAs have emerged as a powerful tool for studying gene function and have shown promise as therapeutic agents for a variety of diseases, including viral infections, cancer, and genetic disorders. However, their use as therapeutics is still in the early stages of development, and there are challenges associated with delivering siRNAs to specific cells and tissues in the body.

Phosphoglycerate Kinase (PGK) is an enzyme that plays a crucial role in the glycolytic pathway, which is a series of reactions that convert glucose into pyruvate, producing ATP and NADH as energy-rich compounds. PGK catalyzes the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3-PG), concomitantly transferring a phosphate group to ADP to form ATP. This reaction is the fourth step in the glycolytic pathway and is reversible under certain conditions.

In humans, there are two isoforms of PGK: PGK1 and PGK2. PGK1 is widely expressed in various tissues, while PGK2 is primarily found in sperm cells. Deficiencies or mutations in the PGK1 gene can lead to a rare metabolic disorder called Phosphoglycerate Kinase Deficiency (PGKD), which can present with hemolytic anemia and neurological symptoms.

Wnt proteins are a family of secreted signaling molecules that play crucial roles in the regulation of fundamental biological processes, including cell proliferation, differentiation, migration, and survival. They were first discovered in 1982 through genetic studies in Drosophila melanogaster (fruit flies) and have since been found to be highly conserved across various species, from invertebrates to humans.

Wnt proteins exert their effects by binding to specific receptors on the target cell surface, leading to the activation of several intracellular signaling pathways:

1. Canonical Wnt/β-catenin pathway: In the absence of Wnt ligands, β-catenin is continuously degraded by a destruction complex consisting of Axin, APC (Adenomatous polyposis coli), and GSK3β (Glycogen synthase kinase 3 beta). When Wnt proteins bind to their receptors Frizzled and LRP5/6, the formation of a "signalosome" complex leads to the inhibition of the destruction complex, allowing β-catenin to accumulate in the cytoplasm and translocate into the nucleus. Here, it interacts with TCF/LEF (T-cell factor/lymphoid enhancer-binding factor) transcription factors to regulate the expression of target genes involved in cell proliferation, differentiation, and survival.
2. Non-canonical Wnt pathways: These include the Wnt/Ca^2+^ pathway and the planar cell polarity (PCP) pathway. In the Wnt/Ca^2+^ pathway, Wnt ligands bind to Frizzled receptors and activate heterotrimeric G proteins, leading to an increase in intracellular Ca^2+^ levels and activation of downstream targets such as protein kinase C (PKC) and calcium/calmodulin-dependent protein kinase II (CAMKII). These signaling events ultimately regulate cell movement, adhesion, and gene expression. In the PCP pathway, Wnt ligands bind to Frizzled receptors and coreceptor complexes containing Ror2 or Ryk, leading to activation of small GTPases such as RhoA and Rac1, which control cytoskeletal organization and cell polarity.

Dysregulation of Wnt signaling has been implicated in various human diseases, including cancer, developmental disorders, and degenerative conditions. In cancer, aberrant activation of the canonical Wnt/β-catenin pathway contributes to tumor initiation, progression, and metastasis by promoting cell proliferation, survival, and epithelial-mesenchymal transition (EMT). Inhibitors targeting different components of the Wnt signaling pathway are currently being developed as potential therapeutic strategies for cancer treatment.

Chromones are a type of chemical compound that contain a benzopyran ring, which is a structural component made up of a benzene ring fused to a pyran ring. They can be found in various plants and have been used in medicine for their anti-inflammatory, antimicrobial, and antitussive (cough suppressant) properties. Some chromones are also known to have estrogenic activity and have been studied for their potential use in hormone replacement therapy. Additionally, some synthetic chromones have been developed as drugs for the treatment of asthma and other respiratory disorders.

Protein Phosphatase 1 (PP1) is a type of serine/threonine protein phosphatase that plays a crucial role in the regulation of various cellular processes, including metabolism, signal transduction, and cell cycle progression. PP1 functions by removing phosphate groups from specific serine and threonine residues on target proteins, thereby reversing the effects of protein kinases and controlling protein activity, localization, and stability.

PP1 is a highly conserved enzyme found in eukaryotic cells and is composed of a catalytic subunit associated with one or more regulatory subunits that determine its substrate specificity, subcellular localization, and regulation. The human genome encodes several isoforms of the PP1 catalytic subunit, including PP1α, PP1β/δ, and PP1γ, which share a high degree of sequence similarity and functional redundancy.

PP1 has been implicated in various physiological processes, such as muscle contraction, glycogen metabolism, DNA replication, transcription, and RNA processing. Dysregulation of PP1 activity has been associated with several pathological conditions, including neurodegenerative diseases, cancer, and diabetes. Therefore, understanding the molecular mechanisms that regulate PP1 function is essential for developing novel therapeutic strategies to treat these disorders.

Mitosis is a type of cell division in which the genetic material of a single cell, called the mother cell, is equally distributed into two identical daughter cells. It's a fundamental process that occurs in multicellular organisms for growth, maintenance, and repair, as well as in unicellular organisms for reproduction.

The process of mitosis can be broken down into several stages: prophase, prometaphase, metaphase, anaphase, and telophase. During prophase, the chromosomes condense and become visible, and the nuclear envelope breaks down. In prometaphase, the nuclear membrane is completely disassembled, and the mitotic spindle fibers attach to the chromosomes at their centromeres.

During metaphase, the chromosomes align at the metaphase plate, an imaginary line equidistant from the two spindle poles. In anaphase, sister chromatids are pulled apart by the spindle fibers and move toward opposite poles of the cell. Finally, in telophase, new nuclear envelopes form around each set of chromosomes, and the chromosomes decondense and become less visible.

Mitosis is followed by cytokinesis, a process that divides the cytoplasm of the mother cell into two separate daughter cells. The result of mitosis and cytokinesis is two genetically identical cells, each with the same number and kind of chromosomes as the original parent cell.

Reticulocytes are immature red blood cells that still contain remnants of organelles, such as ribosomes and mitochondria, which are typically found in developing cells. These organelles are involved in the process of protein synthesis and energy production, respectively. Reticulocytes are released from the bone marrow into the bloodstream, where they continue to mature into fully developed red blood cells called erythrocytes.

Reticulocytes can be identified under a microscope by their staining characteristics, which reveal a network of fine filaments or granules known as the reticular apparatus. This apparatus is composed of residual ribosomal RNA and other proteins that have not yet been completely eliminated during the maturation process.

The percentage of reticulocytes in the blood can be used as a measure of bone marrow function and erythropoiesis, or red blood cell production. An increased reticulocyte count may indicate an appropriate response to blood loss, hemolysis, or other conditions that cause anemia, while a decreased count may suggest impaired bone marrow function or a deficiency in erythropoietin, the hormone responsible for stimulating red blood cell production.

Glutathione transferases (GSTs) are a group of enzymes involved in the detoxification of xenobiotics and endogenous compounds. They facilitate the conjugation of these compounds with glutathione, a tripeptide consisting of cysteine, glutamic acid, and glycine, which results in more water-soluble products that can be easily excreted from the body.

GSTs play a crucial role in protecting cells against oxidative stress and chemical injury by neutralizing reactive electrophilic species and peroxides. They are found in various tissues, including the liver, kidneys, lungs, and intestines, and are classified into several families based on their structure and function.

Abnormalities in GST activity have been associated with increased susceptibility to certain diseases, such as cancer, neurological disorders, and respiratory diseases. Therefore, GSTs have become a subject of interest in toxicology, pharmacology, and clinical research.

Arginine kinase is an enzyme that catalyzes the phosphorylation of arginine, a basic amino acid, to form phosphoarginine. This reaction plays a crucial role in energy metabolism in various organisms, including invertebrates and microorganisms. Phosphoarginine serves as an energy storage molecule, similar to how phosphocreatine is used in vertebrate muscle tissue. Arginine kinase is not typically found in mammals, but it is present in other animals such as insects, crustaceans, and mollusks. The enzyme helps facilitate rapid energy transfer during high-intensity activities, supporting the organism's physiological functions.

Okadaic acid is a type of toxin that is produced by certain species of marine algae, including Dinophysis and Prorocentrum. It is a potent inhibitor of protein phosphatases 1 and 2A, which are important enzymes that help regulate cellular processes in the body.

Okadaic acid can accumulate in shellfish that feed on these algae, and consumption of contaminated seafood can lead to a serious illness known as diarrhetic shellfish poisoning (DSP). Symptoms of DSP include nausea, vomiting, diarrhea, and abdominal cramps. In severe cases, it can also cause neurological symptoms such as dizziness, disorientation, and tingling or numbness in the lips, tongue, and fingers.

It is important to note that okadaic acid is not only a marine toxin but also used in scientific research as a tool to study the role of protein phosphatases in cellular processes. However, exposure to this compound should be avoided due to its toxic effects.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Nucleoside-phosphate kinase (NPK) is an enzyme that plays a crucial role in the synthesis and metabolism of nucleotides, which are the building blocks of DNA and RNA. NPK catalyzes the transfer of a phosphate group from a donor molecule, typically ATP, to a nucleoside or deoxynucleoside, forming a nucleoside monophosphate (NMP) or deoxynucleoside monophosphate (dNMP).

There are several isoforms of NPK found in different cellular compartments and tissues, each with distinct substrate specificities. These enzymes play essential roles in maintaining the balance of nucleotides required for various cellular processes, including DNA replication, repair, and transcription, as well as RNA synthesis and metabolism.

Abnormalities in NPK activity or expression have been implicated in several human diseases, such as cancer, viral infections, and neurological disorders. Therefore, understanding the function and regulation of NPK is crucial for developing novel therapeutic strategies to target these conditions.

MAP Kinase Kinase 6 (MAP2K6) is a serine/threonine protein kinase that plays a crucial role in intracellular signaling transduction pathways. It is also known as MKK6 or MITogen-Activated Protein Kinase Kinase 6. This enzyme is a member of the MAPK kinase family, which activates mitogen-activated protein kinases (MAPKs) by phosphorylating their activation loop residues.

MAP2K6 specifically activates p38 MAPK, another serine/threonine protein kinase involved in various cellular responses to stress stimuli, cytokines, and hormones. The MAP2K6-p38 MAPK signaling pathway is essential for regulating processes such as inflammation, differentiation, apoptosis, and autophagy. Dysregulation of this pathway has been implicated in several diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.

Milk proteins are a complex mixture of proteins that are naturally present in milk, consisting of casein and whey proteins. Casein makes up about 80% of the total milk protein and is divided into several types including alpha-, beta-, gamma- and kappa-casein. Whey proteins account for the remaining 20% and include beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin, and immunoglobulins. These proteins are important sources of essential amino acids and play a crucial role in the nutrition of infants and young children. Additionally, milk proteins have various functional properties that are widely used in the food industry for their gelling, emulsifying, and foaming abilities.

I'm sorry for any confusion, but "Morpholines" is not a medical term. It is a chemical term that refers to a class of heterocyclic organic compounds containing one nitrogen atom and one oxygen atom in the ring. They are widely used as intermediates in the synthesis of various pharmaceuticals, agrochemicals, and dyes. If you have any questions about a medical issue or term, I'd be happy to try to help answer those for you!

'Drosophila proteins' refer to the proteins that are expressed in the fruit fly, Drosophila melanogaster. This organism is a widely used model system in genetics, developmental biology, and molecular biology research. The study of Drosophila proteins has contributed significantly to our understanding of various biological processes, including gene regulation, cell signaling, development, and aging.

Some examples of well-studied Drosophila proteins include:

1. HSP70 (Heat Shock Protein 70): A chaperone protein involved in protein folding and protection from stress conditions.
2. TUBULIN: A structural protein that forms microtubules, important for cell division and intracellular transport.
3. ACTIN: A cytoskeletal protein involved in muscle contraction, cell motility, and maintenance of cell shape.
4. BETA-GALACTOSIDASE (LACZ): A reporter protein often used to monitor gene expression patterns in transgenic flies.
5. ENDOGLIN: A protein involved in the development of blood vessels during embryogenesis.
6. P53: A tumor suppressor protein that plays a crucial role in preventing cancer by regulating cell growth and division.
7. JUN-KINASE (JNK): A signaling protein involved in stress response, apoptosis, and developmental processes.
8. DECAPENTAPLEGIC (DPP): A member of the TGF-β (Transforming Growth Factor Beta) superfamily, playing essential roles in embryonic development and tissue homeostasis.

These proteins are often studied using various techniques such as biochemistry, genetics, molecular biology, and structural biology to understand their functions, interactions, and regulation within the cell.

MAP Kinase Kinase 3 (MKK3) is a serine/threonine protein kinase that plays a crucial role in intracellular signaling pathways, particularly in the mitogen-activated protein kinase (MAPK) cascades. MAPK cascades are evolutionarily conserved signal transduction modules that regulate various cellular processes, including proliferation, differentiation, survival, and stress responses.

MKK3 is specifically involved in the p38 MAPK signaling pathway, which responds to diverse stimuli such as cytokines, environmental stresses, and inflammatory mediators. Upon activation, MKK3 phosphorylates and activates p38 MAPK, leading to the regulation of downstream targets that mediate various cellular responses.

In summary, MAP Kinase Kinase 3 (MKK3) is a protein kinase involved in the p38 MAPK signaling pathway, which regulates essential cellular processes in response to extracellular signals and stresses.

Mitogen-Activated Protein Kinase 8 (MAPK8), also known as JNK1 (c-Jun N-terminal kinase 1), is a serine/threonine protein kinase that plays a crucial role in signal transduction pathways involved in various cellular processes, including inflammation, differentiation, apoptosis, and stress response. It is activated by dual phosphorylation on its threonine and tyrosine residues in the activation loop by upstream MAP2Ks (MKK4/SEK1 and MKK7). Once activated, MAPK8 can phosphorylate and regulate the activity of various transcription factors, such as c-Jun, ATF-2, and ELK1, thereby modulating gene expression. Dysregulation of this kinase has been implicated in several pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders.

Aurora Kinase A is a type of serine/threonine kinase that plays a crucial role in the regulation of cell division and mitosis. It is encoded by the AURKA gene in humans. This enzyme is responsible for proper chromosome alignment and segregation during mitosis, and its dysregulation has been implicated in various types of cancer. Aurora Kinase A is often overexpressed in cancer cells, leading to chromosomal instability and aneuploidy, which contribute to tumor growth and progression. Inhibitors of Aurora Kinase A are being investigated as potential cancer therapeutics.

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, such as protein synthesis, signal transduction, and regulation of enzymatic activities. It serves as an energy currency, similar to adenosine triphosphate (ATP), and undergoes hydrolysis to guanosine diphosphate (GDP) or guanosine monophosphate (GMP) to release energy required for these processes. GTP is also a precursor for the synthesis of other essential molecules, including RNA and certain signaling proteins. Additionally, it acts as a molecular switch in many intracellular signaling pathways by binding and activating specific GTPase proteins.

3-Phosphoinositide-Dependent Protein Kinases (PDPKs) are a family of serine/threonine protein kinases that play crucial roles in regulating various cellular processes, including cell survival, proliferation, and metabolism. They are named after their ability to phosphorylate and activate downstream targets in response to the binding of 3-phosphoinositides, which are lipid second messengers generated by the activation of phosphatidylinositol 3-kinases (PI3Ks).

PDPKs consist of two main isoforms: PDPK1 and PDK2. PDPK1 is also known as the mammalian target of rapamycin complex 2 (mTORC2) associated protein, mSin1 kinase, or Rictor-binding protein. It primarily phosphorylates and activates AGC kinases, such as Akt/PKB, p70 S6 kinase, and protein kinase C (PKC). PDK2, on the other hand, is also known as ILK-associated kinase (ILKAP) or PDPK2. It primarily phosphorylates and activates PKC isoforms.

PDPKs are often deregulated in various human diseases, including cancer, diabetes, and neurological disorders. Therefore, they represent potential therapeutic targets for the development of novel drugs to treat these conditions.

Focal Adhesion Kinase 2 (FAK2), also known as Protein Tyrosine Kinase 2 beta (PTK2B), is a cytoplasmic tyrosine kinase that plays a crucial role in various cellular processes, including cell adhesion, migration, proliferation, and survival. FAK2 is structurally similar to Focal Adhesion Kinase 1 (FAK1 or PTK2A) but has distinct functions and expression patterns.

FAK2 contains several functional domains, such as an N-terminal FERM domain, a central kinase domain, a C-terminal focal adhesion targeting (FAT) domain, and proline-rich regions that interact with various signaling proteins. FAK2 is activated by autophosphorylation at the Y397 residue upon integrin clustering or growth factor receptor activation, which leads to the recruitment of downstream effectors and the initiation of intracellular signaling cascades.

FAK2 has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and cardiovascular disorders. In cancer, FAK2 overexpression or hyperactivation promotes tumor cell survival, invasion, and metastasis, making it an attractive therapeutic target for anticancer therapy. However, the role of FAK2 in physiological processes is still not fully understood and requires further investigation.

2,3-Diphosphoglycerate (2,3-DPG) is a molecule found in red blood cells that plays a crucial role in regulating the affinity of hemoglobin for oxygen. It is a byproduct of the glycolytic pathway, which is a series of biochemical reactions that convert glucose into energy.

In the tissues where oxygen demand is high, such as muscles and organs, 2,3-DPG concentrations are typically elevated. This molecule binds to deoxygenated hemoglobin at specific sites on the beta chains, reducing its affinity for oxygen and promoting the release of oxygen to the tissues.

Conversely, in the lungs where oxygen is abundant, 2,3-DPG concentrations are lower, allowing hemoglobin to bind more readily to oxygen and load up with oxygen for delivery to the tissues. Therefore, 2,3-DPG helps optimize the matching of oxygen supply and demand in the body.

Calmodulin-binding proteins are a diverse group of proteins that have the ability to bind to calmodulin, a ubiquitous calcium-binding protein found in eukaryotic cells. Calmodulin plays a critical role in various cellular processes by regulating the activity of its target proteins in a calcium-dependent manner.

Calmodulin-binding proteins contain specific domains or motifs that enable them to interact with calmodulin. These domains can be classified into two main categories: IQ motifs and CaM motifs. The IQ motif is a short amino acid sequence that contains the consensus sequence IQXXXRGXXR, where X represents any amino acid. This motif binds to the C-lobe of calmodulin in a calcium-dependent manner. On the other hand, CaM motifs are longer sequences that can bind to both lobes of calmodulin with high affinity and in a calcium-dependent manner.

Calmodulin-binding proteins play crucial roles in various cellular functions, including signal transduction, gene regulation, cytoskeleton organization, and ion channel regulation. For example, calmodulin-binding proteins such as calcineurin and CaM kinases are involved in the regulation of immune responses, learning, and memory. Similarly, myosin regulatory light chains, which contain IQ motifs, play a critical role in muscle contraction by regulating the interaction between actin and myosin filaments.

In summary, calmodulin-binding proteins are a diverse group of proteins that interact with calmodulin to regulate various cellular processes. They contain specific domains or motifs that enable them to bind to calmodulin in a calcium-dependent manner, thereby modulating the activity of their target proteins.

Beta-catenin is a protein that plays a crucial role in gene transcription and cell-cell adhesion. It is a key component of the Wnt signaling pathway, which regulates various processes such as cell proliferation, differentiation, and migration during embryonic development and tissue homeostasis in adults.

In the absence of Wnt signals, beta-catenin forms a complex with other proteins, including adenomatous polyposis coli (APC) and axin, which targets it for degradation by the proteasome. When Wnt ligands bind to their receptors, this complex is disrupted, allowing beta-catenin to accumulate in the cytoplasm and translocate to the nucleus. In the nucleus, beta-catenin interacts with T cell factor/lymphoid enhancer-binding factor (TCF/LEF) transcription factors to activate the transcription of target genes involved in cell fate determination, survival, and proliferation.

Mutations in the genes encoding components of the Wnt signaling pathway, including beta-catenin, have been implicated in various human diseases, such as cancer, developmental disorders, and degenerative conditions.

Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.

Subcellular fractions refer to the separation and collection of specific parts or components of a cell, including organelles, membranes, and other structures, through various laboratory techniques such as centrifugation and ultracentrifugation. These fractions can be used in further biochemical and molecular analyses to study the structure, function, and interactions of individual cellular components. Examples of subcellular fractions include nuclear extracts, mitochondrial fractions, microsomal fractions (membrane vesicles), and cytosolic fractions (cytoplasmic extracts).

Protein isoforms are different forms or variants of a protein that are produced from a single gene through the process of alternative splicing, where different exons (or parts of exons) are included in the mature mRNA molecule. This results in the production of multiple, slightly different proteins that share a common core structure but have distinct sequences and functions. Protein isoforms can also arise from genetic variations such as single nucleotide polymorphisms or mutations that alter the protein-coding sequence of a gene. These differences in protein sequence can affect the stability, localization, activity, or interaction partners of the protein isoform, leading to functional diversity and specialization within cells and organisms.

Spermine is a polyamine compound that is involved in various biological processes, including cell growth and differentiation, DNA packaging, and gene expression. It is synthesized from the amino acid ornithine through a series of enzymatic reactions and is found in high concentrations in tissues such as the prostate gland, liver, and brain. Spermine has been shown to have antioxidant properties and may play a role in protecting cells against oxidative stress. In addition, spermine has been implicated in the regulation of ion channels and receptors, and may be involved in the modulation of neuronal excitability.

Phosphatidylinositol 3-Kinase (PI3K) is an intracellular lipid kinase that phosphorylates the 3-hydroxyl group of the inositol ring of phosphatidylinositol and its phosphorylated derivatives, converting PIP2 (phosphatidylinositol 4,5-bisphosphate) to PIP3 (phosphatidylinositol 3,4,5-trisphosphate). This enzyme plays a crucial role in various cellular functions such as cell growth, proliferation, differentiation, motility, survival, and intracellular trafficking. PI3Ks are classified into three classes (I, II, and III) based on their structure, regulation, and substrate specificity. Class I PI3Ks are further divided into two subclasses (IA and IB), which are involved in signal transduction downstream of receptor tyrosine kinases and G protein-coupled receptors. Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders.

Insulin is a hormone produced by the beta cells of the pancreatic islets, primarily in response to elevated levels of glucose in the circulating blood. It plays a crucial role in regulating blood glucose levels and facilitating the uptake and utilization of glucose by peripheral tissues, such as muscle and adipose tissue, for energy production and storage. Insulin also inhibits glucose production in the liver and promotes the storage of excess glucose as glycogen or triglycerides.

Deficiency in insulin secretion or action leads to impaired glucose regulation and can result in conditions such as diabetes mellitus, characterized by chronic hyperglycemia and associated complications. Exogenous insulin is used as a replacement therapy in individuals with diabetes to help manage their blood glucose levels and prevent long-term complications.

Pyrimidines are heterocyclic aromatic organic compounds similar to benzene and pyridine, containing two nitrogen atoms at positions 1 and 3 of the six-member ring. They are one of the two types of nucleobases found in nucleic acids, the other being purines. The pyrimidine bases include cytosine (C) and thymine (T) in DNA, and uracil (U) in RNA, which pair with guanine (G) and adenine (A), respectively, through hydrogen bonding to form the double helix structure of nucleic acids. Pyrimidines are also found in many other biomolecules and have various roles in cellular metabolism and genetic regulation.

NF-κB (Nuclear Factor kappa-light-chain-enhancer of activated B cells) is a protein complex that plays a crucial role in regulating the immune response to infection and inflammation, as well as in cell survival, differentiation, and proliferation. It is composed of several subunits, including p50, p52, p65 (RelA), c-Rel, and RelB, which can form homodimers or heterodimers that bind to specific DNA sequences called κB sites in the promoter regions of target genes.

Under normal conditions, NF-κB is sequestered in the cytoplasm by inhibitory proteins known as IκBs (inhibitors of κB). However, upon stimulation by various signals such as cytokines, bacterial or viral products, and stress, IκBs are phosphorylated, ubiquitinated, and degraded, leading to the release and activation of NF-κB. Activated NF-κB then translocates to the nucleus, where it binds to κB sites and regulates the expression of target genes involved in inflammation, immunity, cell survival, and proliferation.

Dysregulation of NF-κB signaling has been implicated in various pathological conditions such as cancer, chronic inflammation, autoimmune diseases, and neurodegenerative disorders. Therefore, targeting NF-κB signaling has emerged as a potential therapeutic strategy for the treatment of these diseases.

Adenosine kinase (ADK) is an enzyme that plays a crucial role in the regulation of adenosine levels in cells. The medical definition of adenosine kinase is:

"An enzyme (EC 2.7.1.20) that catalyzes the phosphorylation of adenosine to form adenosine monophosphate (AMP) using ATP as the phosphate donor. This reaction helps maintain the balance between adenosine and its corresponding nucleotides in cells, and it plays a significant role in purine metabolism, cell signaling, and energy homeostasis."

Adenosine kinase is widely distributed in various tissues, including the brain, heart, liver, and muscles. Dysregulation of adenosine kinase activity has been implicated in several pathological conditions, such as ischemia-reperfusion injury, neurodegenerative disorders, and cancer. Therefore, modulating adenosine kinase activity has emerged as a potential therapeutic strategy for treating these diseases.

The brain is the central organ of the nervous system, responsible for receiving and processing sensory information, regulating vital functions, and controlling behavior, movement, and cognition. It is divided into several distinct regions, each with specific functions:

1. Cerebrum: The largest part of the brain, responsible for higher cognitive functions such as thinking, learning, memory, language, and perception. It is divided into two hemispheres, each controlling the opposite side of the body.
2. Cerebellum: Located at the back of the brain, it is responsible for coordinating muscle movements, maintaining balance, and fine-tuning motor skills.
3. Brainstem: Connects the cerebrum and cerebellum to the spinal cord, controlling vital functions such as breathing, heart rate, and blood pressure. It also serves as a relay center for sensory information and motor commands between the brain and the rest of the body.
4. Diencephalon: A region that includes the thalamus (a major sensory relay station) and hypothalamus (regulates hormones, temperature, hunger, thirst, and sleep).
5. Limbic system: A group of structures involved in emotional processing, memory formation, and motivation, including the hippocampus, amygdala, and cingulate gyrus.

The brain is composed of billions of interconnected neurons that communicate through electrical and chemical signals. It is protected by the skull and surrounded by three layers of membranes called meninges, as well as cerebrospinal fluid that provides cushioning and nutrients.

A circadian rhythm is a roughly 24-hour biological cycle that regulates various physiological and behavioral processes in living organisms. It is driven by the body's internal clock, which is primarily located in the suprachiasmatic nucleus (SCN) of the hypothalamus in the brain.

The circadian rhythm controls many aspects of human physiology, including sleep-wake cycles, hormone secretion, body temperature, and metabolism. It helps to synchronize these processes with the external environment, particularly the day-night cycle caused by the rotation of the Earth.

Disruptions to the circadian rhythm can have negative effects on health, leading to conditions such as insomnia, sleep disorders, depression, bipolar disorder, and even increased risk of chronic diseases like cancer, diabetes, and cardiovascular disease. Factors that can disrupt the circadian rhythm include shift work, jet lag, irregular sleep schedules, and exposure to artificial light at night.

Amino acid motifs are recurring patterns or sequences of amino acids in a protein molecule. These motifs can be identified through various sequence analysis techniques and often have functional or structural significance. They can be as short as two amino acids in length, but typically contain at least three to five residues.

Some common examples of amino acid motifs include:

1. Active site motifs: These are specific sequences of amino acids that form the active site of an enzyme and participate in catalyzing chemical reactions. For example, the catalytic triad in serine proteases consists of three residues (serine, histidine, and aspartate) that work together to hydrolyze peptide bonds.
2. Signal peptide motifs: These are sequences of amino acids that target proteins for secretion or localization to specific organelles within the cell. For example, a typical signal peptide consists of a positively charged n-region, a hydrophobic h-region, and a polar c-region that directs the protein to the endoplasmic reticulum membrane for translocation.
3. Zinc finger motifs: These are structural domains that contain conserved sequences of amino acids that bind zinc ions and play important roles in DNA recognition and regulation of gene expression.
4. Transmembrane motifs: These are sequences of hydrophobic amino acids that span the lipid bilayer of cell membranes and anchor transmembrane proteins in place.
5. Phosphorylation sites: These are specific serine, threonine, or tyrosine residues that can be phosphorylated by protein kinases to regulate protein function.

Understanding amino acid motifs is important for predicting protein structure and function, as well as for identifying potential drug targets in disease-associated proteins.

LIM kinases are a group of serine/threonine protein kinases that play important roles in various cellular processes, including actin dynamics, microtubule organization, and cell motility. They are named after their conserved N-terminal LIM domains, which are zinc-finger domains involved in protein-protein interactions.

LIM kinase 1 (LIMK1) and LIM kinase 2 (LIMK2) are the two main isoforms found in mammals. They are activated by upstream regulators such as Rho GTPases, PAK kinases, and ROCK kinases, which bind to and activate the LIM kinases in response to various cellular signals.

Once activated, LIM kinases phosphorylate and regulate the activity of cofilin, an actin-binding protein that severs and depolymerizes actin filaments. By inhibiting cofilin's activity, LIM kinases promote the stabilization and bundling of actin filaments, which is important for various cellular functions such as cell migration, cytokinesis, and neurite outgrowth.

Dysregulation of LIM kinases has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the regulation and function of LIM kinases is an important area of research with potential therapeutic implications.

Down-regulation is a process that occurs in response to various stimuli, where the number or sensitivity of cell surface receptors or the expression of specific genes is decreased. This process helps maintain homeostasis within cells and tissues by reducing the ability of cells to respond to certain signals or molecules.

In the context of cell surface receptors, down-regulation can occur through several mechanisms:

1. Receptor internalization: After binding to their ligands, receptors can be internalized into the cell through endocytosis. Once inside the cell, these receptors may be degraded or recycled back to the cell surface in smaller numbers.
2. Reduced receptor synthesis: Down-regulation can also occur at the transcriptional level, where the expression of genes encoding for specific receptors is decreased, leading to fewer receptors being produced.
3. Receptor desensitization: Prolonged exposure to a ligand can lead to a decrease in receptor sensitivity or affinity, making it more difficult for the cell to respond to the signal.

In the context of gene expression, down-regulation refers to the decreased transcription and/or stability of specific mRNAs, leading to reduced protein levels. This process can be induced by various factors, including microRNA (miRNA)-mediated regulation, histone modification, or DNA methylation.

Down-regulation is an essential mechanism in many physiological processes and can also contribute to the development of several diseases, such as cancer and neurodegenerative disorders.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Nerve tissue proteins are specialized proteins found in the nervous system that provide structural and functional support to nerve cells, also known as neurons. These proteins include:

1. Neurofilaments: These are type IV intermediate filaments that provide structural support to neurons and help maintain their shape and size. They are composed of three subunits - NFL (light), NFM (medium), and NFH (heavy).

2. Neuronal Cytoskeletal Proteins: These include tubulins, actins, and spectrins that provide structural support to the neuronal cytoskeleton and help maintain its integrity.

3. Neurotransmitter Receptors: These are specialized proteins located on the postsynaptic membrane of neurons that bind neurotransmitters released by presynaptic neurons, triggering a response in the target cell.

4. Ion Channels: These are transmembrane proteins that regulate the flow of ions across the neuronal membrane and play a crucial role in generating and transmitting electrical signals in neurons.

5. Signaling Proteins: These include enzymes, receptors, and adaptor proteins that mediate intracellular signaling pathways involved in neuronal development, differentiation, survival, and death.

6. Adhesion Proteins: These are cell surface proteins that mediate cell-cell and cell-matrix interactions, playing a crucial role in the formation and maintenance of neural circuits.

7. Extracellular Matrix Proteins: These include proteoglycans, laminins, and collagens that provide structural support to nerve tissue and regulate neuronal migration, differentiation, and survival.

Cell proliferation is the process by which cells increase in number, typically through the process of cell division. In the context of biology and medicine, it refers to the reproduction of cells that makes up living tissue, allowing growth, maintenance, and repair. It involves several stages including the transition from a phase of quiescence (G0 phase) to an active phase (G1 phase), DNA replication in the S phase, and mitosis or M phase, where the cell divides into two daughter cells.

Abnormal or uncontrolled cell proliferation is a characteristic feature of many diseases, including cancer, where deregulated cell cycle control leads to excessive and unregulated growth of cells, forming tumors that can invade surrounding tissues and metastasize to distant sites in the body.

RNA interference (RNAi) is a biological process in which RNA molecules inhibit the expression of specific genes. This process is mediated by small RNA molecules, including microRNAs (miRNAs) and small interfering RNAs (siRNAs), that bind to complementary sequences on messenger RNA (mRNA) molecules, leading to their degradation or translation inhibition.

RNAi plays a crucial role in regulating gene expression and defending against foreign genetic elements, such as viruses and transposons. It has also emerged as an important tool for studying gene function and developing therapeutic strategies for various diseases, including cancer and viral infections.

HEK293 cells, also known as human embryonic kidney 293 cells, are a line of cells used in scientific research. They were originally derived from human embryonic kidney cells and have been adapted to grow in a lab setting. HEK293 cells are widely used in molecular biology and biochemistry because they can be easily transfected (a process by which DNA is introduced into cells) and highly express foreign genes. As a result, they are often used to produce proteins for structural and functional studies. It's important to note that while HEK293 cells are derived from human tissue, they have been grown in the lab for many generations and do not retain the characteristics of the original embryonic kidney cells.

'Cercopithecus aethiops' is the scientific name for the monkey species more commonly known as the green monkey. It belongs to the family Cercopithecidae and is native to western Africa. The green monkey is omnivorous, with a diet that includes fruits, nuts, seeds, insects, and small vertebrates. They are known for their distinctive greenish-brown fur and long tail. Green monkeys are also important animal models in biomedical research due to their susceptibility to certain diseases, such as SIV (simian immunodeficiency virus), which is closely related to HIV.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Cell survival refers to the ability of a cell to continue living and functioning normally, despite being exposed to potentially harmful conditions or treatments. This can include exposure to toxins, radiation, chemotherapeutic drugs, or other stressors that can damage cells or interfere with their normal processes.

In scientific research, measures of cell survival are often used to evaluate the effectiveness of various therapies or treatments. For example, researchers may expose cells to a particular drug or treatment and then measure the percentage of cells that survive to assess its potential therapeutic value. Similarly, in toxicology studies, measures of cell survival can help to determine the safety of various chemicals or substances.

It's important to note that cell survival is not the same as cell proliferation, which refers to the ability of cells to divide and multiply. While some treatments may promote cell survival, they may also inhibit cell proliferation, making them useful for treating diseases such as cancer. Conversely, other treatments may be designed to specifically target and kill cancer cells, even if it means sacrificing some healthy cells in the process.

Nucleoside-diphosphate kinase (NDK) is an enzyme that plays a crucial role in the regulation of intracellular levels of nucleoside triphosphates and diphosphates. These nucleotides are essential for various cellular processes, including DNA replication, transcription, translation, and energy metabolism.

NDK catalyzes the transfer of a phosphate group from a nucleoside triphosphate (most commonly ATP or GTP) to a nucleoside diphosphate (NDP), converting it into a nucleoside triphosphate (NTP). The reaction can be summarized as follows:

NTP + NDP ↔ NDP + NTP

The enzyme has several isoforms, which are differentially expressed in various tissues and cellular compartments. In humans, there are nine known isoforms of NDK, classified into three subfamilies: NM23-H (NME1), NM23-H2 (NME2), and NME4-8. These isoforms share a conserved catalytic core but differ in their regulatory domains and cellular localization.

NDK has been implicated in several physiological processes, such as cell proliferation, differentiation, and survival. Dysregulation of NDK activity has been associated with various pathological conditions, including cancer, neurodegenerative diseases, and viral infections.

Choline kinase is an enzyme that plays a role in the synthesis of phosphatidylcholine, a major component of cell membranes. It catalyzes the phosphorylation of choline to form phosphocholine, which is then used in the synthesis of phosphatidylcholine. Choline kinase exists as multiple isoforms, and its activity has been found to be elevated in some types of cancer cells, making it a potential target for cancer therapy.

Ribosomal Protein S6 Kinases, 70-kDa (p70S6K or RPS6KB1) are serine/threonine protein kinases that play a crucial role in the regulation of cell growth and metabolism. They are so named because they phosphorylate the 40S ribosomal protein S6, which is a component of the small ribosomal subunit. This phosphorylation event is believed to contribute to the control of protein synthesis rates in response to various cellular signals, including growth factors and nutrients.

p70S6K is activated by the PI3K/AKT/mTOR signaling pathway, which is a critical regulator of cell growth, proliferation, and survival. The activation of p70S6K involves a series of phosphorylation events, primarily by mTORC1 (mammalian target of rapamycin complex 1). Once activated, p70S6K promotes several processes related to cell growth, such as:

1. Translation initiation and elongation: Phosphorylation of ribosomal protein S6 and other translation factors enhances the translation of specific mRNAs involved in cell cycle progression, ribosome biogenesis, and metabolic enzymes.
2. Nucleolar formation and rRNA transcription: p70S6K promotes nucleolar formation and increases rRNA transcription by phosphorylating upstream binding factor (UBF), a critical transcriptional regulator of rDNA.
3. mRNA stability: Phosphorylation of certain RNA-binding proteins, such as 4E-BP1, by p70S6K can lead to increased mRNA stability and translation efficiency.

Abnormal regulation of p70S6K has been implicated in various diseases, including cancer, diabetes, and cardiovascular disorders. Therefore, understanding the function and regulation of p70S6K is essential for developing novel therapeutic strategies targeting these conditions.

Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.

In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.

Phosphotyrosine is not a medical term per se, but rather a biochemical term used in the field of medicine and life sciences.

Phosphotyrosine is a post-translational modification of tyrosine residues in proteins, where a phosphate group is added to the hydroxyl side chain of tyrosine by protein kinases. This modification plays a crucial role in intracellular signaling pathways and regulates various cellular processes such as cell growth, differentiation, and apoptosis. Abnormalities in phosphotyrosine-mediated signaling have been implicated in several diseases, including cancer and diabetes.

A consensus sequence in genetics refers to the most common nucleotide (DNA or RNA) or amino acid at each position in a multiple sequence alignment. It is derived by comparing and analyzing several sequences of the same gene or protein from different individuals or organisms. The consensus sequence provides a general pattern or motif that is shared among these sequences and can be useful in identifying functional regions, conserved domains, or evolutionary relationships. However, it's important to note that not every sequence will exactly match the consensus sequence, as variations can occur naturally due to mutations or genetic differences among individuals.

Elongation Factor 2 Kinase (eEF2K) is a type of protein kinase that phosphorylates and inactivates elongation factor 2 (eEF2), a crucial player in protein synthesis. Specifically, eEF2 is responsible for translocating the ribosome along the mRNA during translation, and its phosphorylation by eEF2K leads to a decrease in protein synthesis rates.

eEF2K is activated under conditions of cellular stress, such as nutrient deprivation or hypoxia, and functions to conserve energy by reducing protein synthesis. The kinase is also involved in various cellular processes, including autophagy, apoptosis, and cancer progression. Inhibition of eEF2K has been proposed as a potential therapeutic strategy for treating various diseases, including neurodegenerative disorders and cancer.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.

The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.

The main components of a two-hybrid system include:

1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)

The two-hybrid system technique has several advantages, including:

1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis

However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.

"Xenopus laevis" is not a medical term itself, but it refers to a specific species of African clawed frog that is often used in scientific research, including biomedical and developmental studies. Therefore, its relevance to medicine comes from its role as a model organism in laboratories.

In a broader sense, Xenopus laevis has contributed significantly to various medical discoveries, such as the understanding of embryonic development, cell cycle regulation, and genetic research. For instance, the Nobel Prize in Physiology or Medicine was awarded in 1963 to John R. B. Gurdon and Sir Michael J. Bishop for their discoveries concerning the genetic mechanisms of organism development using Xenopus laevis as a model system.

I'm sorry for any confusion, but "Pyridines" is not a medical term. It is a chemical term that refers to a class of organic compounds with the chemical structure of a six-membered ring containing one nitrogen atom and five carbon atoms (heterocyclic aromatic compound).

In a biological or medical context, pyridine derivatives can be found in various natural and synthetic substances. For example, some medications contain pyridine rings as part of their chemical structure. However, "Pyridines" itself is not a medical term or condition.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

RAF kinases are a family of serine/threonine protein kinases that play crucial roles in intracellular signal transduction pathways, most notably the RAS-RAF-MEK-ERK signaling cascade. This pathway is essential for regulating various cellular processes such as proliferation, differentiation, and survival. There are three main isoforms of RAF kinases in humans: RAF-1 (CRAF), A-RAF, and B-RAF. These kinases become activated through a series of phosphorylation events, ultimately leading to the activation of MEK and ERK kinases, which then regulate various transcription factors and other downstream targets. Dysregulation of RAF kinases has been implicated in several diseases, particularly cancers.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Epidermal Growth Factor (EGF) is a small polypeptide that plays a significant role in various biological processes, including cell growth, proliferation, differentiation, and survival. It primarily binds to the Epidermal Growth Factor Receptor (EGFR) on the surface of target cells, leading to the activation of intracellular signaling pathways that regulate these functions.

EGF is naturally produced in various tissues, such as the skin, and is involved in wound healing, tissue regeneration, and maintaining the integrity of epithelial tissues. In addition to its physiological roles, EGF has been implicated in several pathological conditions, including cancer, where it can contribute to tumor growth and progression by promoting cell proliferation and survival.

As a result, EGF and its signaling pathways have become targets for therapeutic interventions in various diseases, particularly cancer. Inhibitors of EGFR or downstream signaling components are used in the treatment of several types of malignancies, such as non-small cell lung cancer, colorectal cancer, and head and neck cancer.

Transcriptional activation is the process by which a cell increases the rate of transcription of specific genes from DNA to RNA. This process is tightly regulated and plays a crucial role in various biological processes, including development, differentiation, and response to environmental stimuli.

Transcriptional activation occurs when transcription factors (proteins that bind to specific DNA sequences) interact with the promoter region of a gene and recruit co-activator proteins. These co-activators help to remodel the chromatin structure around the gene, making it more accessible for the transcription machinery to bind and initiate transcription.

Transcriptional activation can be regulated at multiple levels, including the availability and activity of transcription factors, the modification of histone proteins, and the recruitment of co-activators or co-repressors. Dysregulation of transcriptional activation has been implicated in various diseases, including cancer and genetic disorders.

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

MAPK kinase 7 (MKK7) is a serine/threonine protein kinase that is also known as MAP2K7 or Mitogen-activated protein kinase kinase 7. It is a member of the MAPK kinase family, which are protein kinases that activate MAPKs (mitogen-activated protein kinases) by phosphorylating them on specific serine and threonine residues.

MKK7 specifically activates c-Jun N-terminal kinase (JNK), a subgroup of the MAPK family, by phosphorylating it on threonine and tyrosine residues. JNK plays important roles in various cellular processes such as proliferation, differentiation, survival, and apoptosis, and its activity is regulated by upstream kinases including MKK7.

MKK7 has been implicated in several signaling pathways that are activated in response to stress signals, inflammatory cytokines, and growth factors. Dysregulation of the MKK7-JNK signaling pathway has been associated with various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

"Drosophila" is a genus of small flies, also known as fruit flies. The most common species used in scientific research is "Drosophila melanogaster," which has been a valuable model organism for many areas of biological and medical research, including genetics, developmental biology, neurobiology, and aging.

The use of Drosophila as a model organism has led to numerous important discoveries in genetics and molecular biology, such as the identification of genes that are associated with human diseases like cancer, Parkinson's disease, and obesity. The short reproductive cycle, large number of offspring, and ease of genetic manipulation make Drosophila a powerful tool for studying complex biological processes.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Glycogen synthase is an enzyme (EC 2.4.1.11) that plays a crucial role in the synthesis of glycogen, a polysaccharide that serves as the primary storage form of glucose in animals, fungi, and bacteria. This enzyme catalyzes the transfer of glucosyl residues from uridine diphosphate glucose (UDP-glucose) to the non-reducing end of an growing glycogen chain, thereby elongating it.

Glycogen synthase is regulated by several mechanisms, including allosteric regulation and covalent modification. The activity of this enzyme is inhibited by high levels of intracellular glucose-6-phosphate (G6P) and activated by the binding of glycogen or proteins that bind to glycogen, such as glycogenin. Phosphorylation of glycogen synthase by protein kinases, like glycogen synthase kinase-3 (GSK3), also reduces its activity, while dephosphorylation by protein phosphatases enhances it.

The regulation of glycogen synthase is critical for maintaining glucose homeostasis and energy balance in the body. Dysregulation of this enzyme has been implicated in several metabolic disorders, including type 2 diabetes and non-alcoholic fatty liver disease (NAFLD).

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

Fungal proteins are a type of protein that is specifically produced and present in fungi, which are a group of eukaryotic organisms that include microorganisms such as yeasts and molds. These proteins play various roles in the growth, development, and survival of fungi. They can be involved in the structure and function of fungal cells, metabolism, pathogenesis, and other cellular processes. Some fungal proteins can also have important implications for human health, both in terms of their potential use as therapeutic targets and as allergens or toxins that can cause disease.

Fungal proteins can be classified into different categories based on their functions, such as enzymes, structural proteins, signaling proteins, and toxins. Enzymes are proteins that catalyze chemical reactions in fungal cells, while structural proteins provide support and protection for the cell. Signaling proteins are involved in communication between cells and regulation of various cellular processes, and toxins are proteins that can cause harm to other organisms, including humans.

Understanding the structure and function of fungal proteins is important for developing new treatments for fungal infections, as well as for understanding the basic biology of fungi. Research on fungal proteins has led to the development of several antifungal drugs that target specific fungal enzymes or other proteins, providing effective treatment options for a range of fungal diseases. Additionally, further study of fungal proteins may reveal new targets for drug development and help improve our ability to diagnose and treat fungal infections.

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

Wnt3A is a type of Wnt protein, which is a secreted signaling molecule that plays crucial roles in the regulation of cell-to-cell communication during embryonic development and tissue homeostasis in adults. Specifically, Wnt3A is a member of the Wnt family that binds to Frizzled receptors and activates the canonical Wnt/β-catenin signaling pathway.

In this pathway, Wnt3A binding to its receptor leads to the inhibition of the β-catenin destruction complex, resulting in the stabilization and accumulation of β-catenin in the cytoplasm. β-catenin then translocates to the nucleus, where it interacts with TCF/LEF transcription factors to regulate the expression of target genes involved in cell proliferation, differentiation, and survival.

Wnt3A has been extensively studied in various biological contexts, including developmental biology, cancer research, and stem cell biology. In particular, Wnt3A has been shown to play important roles in the regulation of embryonic axis formation, neural crest development, and adult tissue regeneration. Dysregulation of Wnt/β-catenin signaling, including aberrant activation by Wnt3A, has been implicated in various human diseases, such as cancer, degenerative disorders, and fibrotic diseases.

An oocyte, also known as an egg cell or female gamete, is a large specialized cell found in the ovary of female organisms. It contains half the number of chromosomes as a normal diploid cell, as it is the product of meiotic division. Oocytes are surrounded by follicle cells and are responsible for the production of female offspring upon fertilization with sperm. The term "oocyte" specifically refers to the immature egg cell before it reaches full maturity and is ready for fertilization, at which point it is referred to as an ovum or egg.

Aurora Kinase B is a type of enzyme that plays a crucial role in the regulation of cell division and mitosis. It is a member of the Aurora kinase family, which includes three different isoforms (Aurora A, B, and C). Among these, Aurora Kinase B is specifically involved in the proper alignment and separation of chromosomes during cell division.

During mitosis, Aurora Kinase B forms a complex with other proteins to form the chromosomal passenger complex (CPC), which plays a critical role in ensuring accurate chromosome segregation. The CPC is responsible for regulating various events during mitosis, including the attachment of microtubules to kinetochores (protein structures that connect chromosomes to spindle fibers), the correction of erroneous kinetochore-microtubule attachments, and the regulation of the anaphase promoting complex/cyclosome (APC/C), which targets specific proteins for degradation during mitosis.

Dysregulation of Aurora Kinase B has been implicated in various human diseases, including cancer. Overexpression or amplification of this kinase can lead to chromosomal instability and aneuploidy, contributing to tumorigenesis and cancer progression. As a result, Aurora Kinase B is considered a promising target for the development of anti-cancer therapies, with several inhibitors currently being investigated in preclinical and clinical studies.

Cyclin-Dependent Kinase 4 (CDK4) is a type of enzyme, specifically a serine/threonine protein kinase, that plays a crucial role in the regulation of the cell cycle. The cell cycle is the series of events that take place in a cell leading to its division and duplication. CDK4, when activated by binding to cyclin D, helps to promote the transition from the G1 phase to the S phase of the cell cycle. This transition is a critical point in the regulation of cell growth and division, and dysregulation of this process can lead to uncontrolled cell growth and cancer. CDK4 inhibitors are used in the treatment of certain types of cancer, such as breast and lung cancer, to block the activity of CDK4 and prevent tumor cell proliferation.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

I apologize for any confusion, but "Paramecium tetraurelia" is not a medical term. It is the scientific name of a species of ciliate protists, which are single-celled organisms commonly found in freshwater environments. These organisms are often studied in biology and microbiology as models for cellular and molecular processes. If you have any questions related to medical terminology or definitions, I would be happy to help with those instead.

A "knockout" mouse is a genetically engineered mouse in which one or more genes have been deleted or "knocked out" using molecular biology techniques. This allows researchers to study the function of specific genes and their role in various biological processes, as well as potential associations with human diseases. The mice are generated by introducing targeted DNA modifications into embryonic stem cells, which are then used to create a live animal. Knockout mice have been widely used in biomedical research to investigate gene function, disease mechanisms, and potential therapeutic targets.

Janus Kinase 1 (JAK1) is not a medical condition, but rather a protein involved in intracellular signal transduction. It is a member of the Janus kinase family, which are cytoplasmic tyrosine kinases that play a critical role in signal transduction of cytokines and growth factors. JAK1 is involved in the signaling of several cytokines and hormones, including interleukin-6 (IL-6), interferons (IFNs), and various growth factors. Mutations in JAK1 can lead to abnormal signal transduction and have been implicated in certain diseases such as autoimmune disorders and cancer.

Therefore, a medical definition of 'Janus Kinase 1' would be: "A cytoplasmic tyrosine kinase that is involved in the intracellular signaling of several cytokines and hormones, including IL-6, IFNs, and various growth factors. JAK1 mutations have been associated with certain diseases such as autoimmune disorders and cancer."

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

Wnt3 protein is a member of the Wnt family of signaling proteins, which are secreted signaling molecules that play crucial roles in embryonic development and tissue homeostasis in adults. Specifically, Wnt3 is involved in the regulation of cell fate decisions, proliferation, and differentiation during embryogenesis. It binds to receptors on the target cells and activates a signaling pathway known as the canonical Wnt pathway, leading to the stabilization and nuclear accumulation of β-catenin, which then interacts with transcription factors to regulate gene expression. Defects in Wnt3 have been implicated in various developmental disorders, including some forms of congenital scoliosis and spina bifida.

Phosphoric monoester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric monoesters into alcohol and phosphate. This class of enzymes includes several specific enzymes, such as phosphatases and nucleotidases, which play important roles in various biological processes, including metabolism, signal transduction, and regulation of cellular processes.

Phosphoric monoester hydrolases are classified under the EC number 3.1.3 by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The enzymes in this class share a common mechanism of action, which involves the nucleophilic attack on the phosphorus atom of the substrate by a serine or cysteine residue in the active site of the enzyme. This results in the formation of a covalent intermediate, which is then hydrolyzed to release the products.

Phosphoric monoester hydrolases are important therapeutic targets for the development of drugs that can modulate their activity. For example, inhibitors of phosphoric monoester hydrolases have been developed as potential treatments for various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

'Drosophila melanogaster' is the scientific name for a species of fruit fly that is commonly used as a model organism in various fields of biological research, including genetics, developmental biology, and evolutionary biology. Its small size, short generation time, large number of offspring, and ease of cultivation make it an ideal subject for laboratory studies. The fruit fly's genome has been fully sequenced, and many of its genes have counterparts in the human genome, which facilitates the understanding of genetic mechanisms and their role in human health and disease.

Here is a brief medical definition:

Drosophila melanogaster (droh-suh-fih-luh meh-lon-guh-ster): A species of fruit fly used extensively as a model organism in genetic, developmental, and evolutionary research. Its genome has been sequenced, revealing many genes with human counterparts, making it valuable for understanding genetic mechanisms and their role in human health and disease.

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

"Xenopus proteins" refer to the proteins that are expressed or isolated from the Xenopus species, which are primarily used as model organisms in biological and biomedical research. The most commonly used Xenopus species for research are the African clawed frogs, Xenopus laevis and Xenopus tropicalis. These proteins play crucial roles in various cellular processes and functions, and they serve as valuable tools to study different aspects of molecular biology, developmental biology, genetics, and biochemistry.

Some examples of Xenopus proteins that are widely studied include:

1. Xenopus Histones: These are the proteins that package DNA into nucleosomes, which are the fundamental units of chromatin in eukaryotic cells. They play a significant role in gene regulation and epigenetic modifications.
2. Xenopus Cyclins and Cyclin-dependent kinases (CDKs): These proteins regulate the cell cycle and control cell division, differentiation, and apoptosis.
3. Xenopus Transcription factors: These proteins bind to specific DNA sequences and regulate gene expression during development and in response to various stimuli.
4. Xenopus Signaling molecules: These proteins are involved in intracellular signaling pathways that control various cellular processes, such as cell growth, differentiation, migration, and survival.
5. Xenopus Cytoskeletal proteins: These proteins provide structural support to the cells and regulate their shape, motility, and organization.
6. Xenopus Enzymes: These proteins catalyze various biochemical reactions in the cell, such as metabolic pathways, DNA replication, transcription, and translation.

Overall, Xenopus proteins are essential tools for understanding fundamental biological processes and have contributed significantly to our current knowledge of molecular biology, genetics, and developmental biology.

Two-dimensional (2D) gel electrophoresis is a type of electrophoretic technique used in the separation and analysis of complex protein mixtures. This method combines two types of electrophoresis – isoelectric focusing (IEF) and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) – to separate proteins based on their unique physical and chemical properties in two dimensions.

In the first dimension, IEF separates proteins according to their isoelectric points (pI), which is the pH at which a protein carries no net electrical charge. The proteins are focused into narrow zones along a pH gradient established within a gel strip. In the second dimension, SDS-PAGE separates the proteins based on their molecular weights by applying an electric field perpendicular to the first dimension.

The separated proteins form distinct spots on the 2D gel, which can be visualized using various staining techniques. The resulting protein pattern provides valuable information about the composition and modifications of the protein mixture, enabling researchers to identify and compare different proteins in various samples. Two-dimensional gel electrophoresis is widely used in proteomics research, biomarker discovery, and quality control in protein production.

Cyclin-Dependent Kinase Inhibitor p27, also known as CDKN1B or p27Kip1, is a protein that regulates the cell cycle. It inhibits the activity of certain cyclin-dependent kinases (CDKs), which are enzymes that play key roles in regulating the progression of the cell cycle.

The cell cycle is a series of events that cells undergo as they grow and divide. Cyclins and CDKs help to control the different stages of the cell cycle by activating and deactivating various proteins at specific times. The p27 protein acts as a brake on the cell cycle, preventing cells from dividing too quickly or abnormally.

When p27 binds to a CDK-cyclin complex, it prevents the complex from phosphorylating its target proteins, which are necessary for the progression of the cell cycle. By inhibiting CDK activity, p27 helps to ensure that cells divide only when the proper conditions are met.

Mutations in the CDKN1B gene, which encodes p27, have been associated with several types of cancer, including breast, lung, and prostate cancer. These mutations can lead to decreased levels of p27 or impaired function, allowing cells to divide uncontrollably and form tumors.

I'm sorry for any confusion, but "Active Transport, Cell Nucleus" is not a widely recognized or established medical term. Active transport typically refers to the energy-dependent process by which cells move molecules across their membranes against their concentration gradient. This process is facilitated by transport proteins and requires ATP as an energy source. However, this process primarily occurs in the cell membrane and not in the cell nucleus.

The cell nucleus, on the other hand, contains genetic material (DNA) and is responsible for controlling various cellular activities such as gene expression, replication, and repair. While there are transport processes that occur within the nucleus, they do not typically involve active transport in the same way that it occurs at the cell membrane.

Therefore, a medical definition of "Active Transport, Cell Nucleus" would not be applicable or informative in this context.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

Staurosporine is an alkaloid compound that is derived from the bacterium Streptomyces staurosporeus. It is a potent and broad-spectrum protein kinase inhibitor, which means it can bind to and inhibit various types of protein kinases, including protein kinase C (PKC), cyclin-dependent kinases (CDKs), and tyrosine kinases.

Protein kinases are enzymes that play a crucial role in cell signaling by adding phosphate groups to other proteins, thereby modulating their activity. The inhibition of protein kinases by staurosporine can disrupt these signaling pathways and lead to various biological effects, such as the induction of apoptosis (programmed cell death) and the inhibition of cell proliferation.

Staurosporine has been widely used in research as a tool to study the roles of protein kinases in various cellular processes and diseases, including cancer, neurodegenerative disorders, and inflammation. However, its use as a therapeutic agent is limited due to its lack of specificity and high toxicity.

Chromatography, agarose is a type of chromatography technique that utilizes agarose gel as the stationary phase in the separation and analysis of biological molecules, such as DNA, RNA, and proteins. This method is commonly used in molecular biology for various applications, including DNA fragment separation, protein purification, and detection of specific nucleic acid sequences or proteins.

Agarose gel is a matrix made from agarose, a polysaccharide derived from seaweed. It has a porous structure with uniform pore size that allows for the size-based separation of molecules based on their ability to migrate through the gel under an electric field (in the case of electrophoresis) or by capillary action (in the case of capillary electrophoresis).

The charged molecules, such as DNA or proteins, interact with the agarose matrix and move through the gel at different rates depending on their size, charge, and shape. Smaller molecules can migrate more quickly through the pores of the gel, while larger molecules are retarded due to their inability to easily pass through the pores. This results in a separation of the molecules based on their physical properties, allowing for their analysis and characterization.

In summary, chromatography, agarose refers to the use of agarose gel as the stationary phase in the separation and analysis of biological molecules using various chromatography techniques, such as electrophoresis or capillary electrophoresis.

An insulin receptor is a transmembrane protein found on the surface of cells, primarily in the liver, muscle, and adipose tissue. It plays a crucial role in regulating glucose metabolism in the body. When insulin binds to its receptor, it triggers a series of intracellular signaling events that promote the uptake and utilization of glucose by cells, as well as the storage of excess glucose as glycogen or fat.

Insulin receptors are composed of two extracellular alpha subunits and two transmembrane beta subunits, which are linked together by disulfide bonds. The binding of insulin to the alpha subunits activates the tyrosine kinase activity of the beta subunits, leading to the phosphorylation of intracellular proteins and the initiation of downstream signaling pathways.

Abnormalities in insulin receptor function or number can contribute to the development of insulin resistance and type 2 diabetes.

Repressor proteins are a type of regulatory protein in molecular biology that suppress the transcription of specific genes into messenger RNA (mRNA) by binding to DNA. They function as part of gene regulation processes, often working in conjunction with an operator region and a promoter region within the DNA molecule. Repressor proteins can be activated or deactivated by various signals, allowing for precise control over gene expression in response to changing cellular conditions.

There are two main types of repressor proteins:

1. DNA-binding repressors: These directly bind to specific DNA sequences (operator regions) near the target gene and prevent RNA polymerase from transcribing the gene into mRNA.
2. Allosteric repressors: These bind to effector molecules, which then cause a conformational change in the repressor protein, enabling it to bind to DNA and inhibit transcription.

Repressor proteins play crucial roles in various biological processes, such as development, metabolism, and stress response, by controlling gene expression patterns in cells.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Lactation is the process by which milk is produced and secreted from the mammary glands of female mammals, including humans, for the nourishment of their young. This physiological function is initiated during pregnancy and continues until it is deliberately stopped or weaned off. The primary purpose of lactation is to provide essential nutrients, antibodies, and other bioactive components that support the growth, development, and immune system of newborns and infants.

The process of lactation involves several hormonal and physiological changes in a woman's body. During pregnancy, the hormones estrogen and progesterone stimulate the growth and development of the mammary glands. After childbirth, the levels of these hormones drop significantly, allowing another hormone called prolactin to take over. Prolactin is responsible for triggering the production of milk in the alveoli, which are tiny sacs within the breast tissue.

Another hormone, oxytocin, plays a crucial role in the release or "let-down" of milk from the alveoli to the nipple during lactation. This reflex is initiated by suckling or thinking about the baby, which sends signals to the brain to release oxytocin. The released oxytocin then binds to receptors in the mammary glands, causing the smooth muscles around the alveoli to contract and push out the milk through the ducts and into the nipple.

Lactation is a complex and highly regulated process that ensures the optimal growth and development of newborns and infants. It provides not only essential nutrients but also various bioactive components, such as immunoglobulins, enzymes, and growth factors, which protect the infant from infections and support their immune system.

In summary, lactation is the physiological process by which milk is produced and secreted from the mammary glands of female mammals for the nourishment of their young. It involves hormonal changes, including the actions of prolactin, oxytocin, estrogen, and progesterone, to regulate the production, storage, and release of milk.

CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.

CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.

In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.

It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.

PC12 cells are a type of rat pheochromocytoma cell line, which are commonly used in scientific research. Pheochromocytomas are tumors that develop from the chromaffin cells of the adrenal gland, and PC12 cells are a subtype of these cells.

PC12 cells have several characteristics that make them useful for research purposes. They can be grown in culture and can be differentiated into a neuron-like phenotype when treated with nerve growth factor (NGF). This makes them a popular choice for studies involving neuroscience, neurotoxicity, and neurodegenerative disorders.

PC12 cells are also known to express various neurotransmitter receptors, ion channels, and other proteins that are relevant to neuronal function, making them useful for studying the mechanisms of drug action and toxicity. Additionally, PC12 cells can be used to study the regulation of cell growth and differentiation, as well as the molecular basis of cancer.

Cytoskeletal proteins are a type of structural proteins that form the cytoskeleton, which is the internal framework of cells. The cytoskeleton provides shape, support, and structure to the cell, and plays important roles in cell division, intracellular transport, and maintenance of cell shape and integrity.

There are three main types of cytoskeletal proteins: actin filaments, intermediate filaments, and microtubules. Actin filaments are thin, rod-like structures that are involved in muscle contraction, cell motility, and cell division. Intermediate filaments are thicker than actin filaments and provide structural support to the cell. Microtubules are hollow tubes that are involved in intracellular transport, cell division, and maintenance of cell shape.

Cytoskeletal proteins are composed of different subunits that polymerize to form filamentous structures. These proteins can be dynamically assembled and disassembled, allowing cells to change their shape and move. Mutations in cytoskeletal proteins have been linked to various human diseases, including cancer, neurological disorders, and muscular dystrophies.

MAP Kinase Kinase Kinase 5 (MAP3K5) is a protein kinase that belongs to the serine/threonine family of kinases. It is also known as MEKK5 or apoptosis signal-regulating kinase 1 (ASK1). This enzyme plays a crucial role in intracellular signaling pathways, particularly those involved in stress responses, inflammation, and programmed cell death (apoptosis). MAP3K5 activates downstream MAP kinases such as p38 and JNK by phosphorylating them, which subsequently regulate various cellular processes like gene expression, proliferation, differentiation, and survival. Mutations in the MAP3K5 gene have been associated with several diseases, including neurodegenerative disorders, cardiovascular diseases, and cancer.

"Xenopus" is not a medical term, but it is a genus of highly invasive aquatic frogs native to sub-Saharan Africa. They are often used in scientific research, particularly in developmental biology and genetics. The most commonly studied species is Xenopus laevis, also known as the African clawed frog.

In a medical context, Xenopus might be mentioned when discussing their use in research or as a model organism to study various biological processes or diseases.

I believe you may be mistakenly using the term "starfish" to refer to a medical condition. If so, the correct term is likely " asterixis," which is a medical sign characterized by rapid, rhythmic flapping or tremulous movements of the hands when they are extended and the wrist is dorsiflexed (held with the back of the hand facing upwards). This is often seen in people with certain neurological conditions such as liver failure or certain types of poisoning.

However, if you are indeed referring to the marine animal commonly known as a "starfish," there isn't a specific medical definition for it. Starfish, also known as sea stars, are marine animals belonging to the class Asteroidea in the phylum Echinodermata. They have a distinctive shape with five or more arms radiating from a central disc, and they move slowly along the ocean floor using their tube feet. Some species of starfish have the ability to regenerate lost body parts, including entire limbs or even their central disc.

A muscle is a soft tissue in our body that contracts to produce force and motion. It is composed mainly of specialized cells called muscle fibers, which are bound together by connective tissue. There are three types of muscles: skeletal (voluntary), smooth (involuntary), and cardiac. Skeletal muscles attach to bones and help in movement, while smooth muscles are found within the walls of organs and blood vessels, helping with functions like digestion and circulation. Cardiac muscle is the specific type that makes up the heart, allowing it to pump blood throughout the body.

Up-regulation is a term used in molecular biology and medicine to describe an increase in the expression or activity of a gene, protein, or receptor in response to a stimulus. This can occur through various mechanisms such as increased transcription, translation, or reduced degradation of the molecule. Up-regulation can have important functional consequences, for example, enhancing the sensitivity or response of a cell to a hormone, neurotransmitter, or drug. It is a normal physiological process that can also be induced by disease or pharmacological interventions.

A sequence deletion in a genetic context refers to the removal or absence of one or more nucleotides (the building blocks of DNA or RNA) from a specific region in a DNA or RNA molecule. This type of mutation can lead to the loss of genetic information, potentially resulting in changes in the function or expression of a gene. If the deletion involves a critical portion of the gene, it can cause diseases, depending on the role of that gene in the body. The size of the deleted sequence can vary, ranging from a single nucleotide to a large segment of DNA.

Mitogen-Activated Protein Kinase 9 (MAPK9), also known as c-Jun N-terminal kinase 1 (JNK1), is a serine/threonine protein kinase that plays a crucial role in signal transduction pathways involved in various cellular processes, including inflammation, differentiation, apoptosis, and stress response. It is a member of the MAPK family and is activated by dual phosphorylation on threonine and tyrosine residues within its activation loop by upstream MAPK kinases (MKKs). Once activated, MAPK9/JNK1 translocates to the nucleus where it phosphorylates and regulates the activity of various transcription factors, such as c-Jun, ATF2, and Elk-1, thereby modulating gene expression. Its activation is primarily triggered by stress signals, inflammatory cytokines, and mitogens, making it a key player in the integration and interpretation of extracellular signals to regulate cellular responses.

Deoxycytidine kinase (dCK) is an enzyme that plays a crucial role in the phosphorylation of deoxycytidine and its analogs, which are important components in the intracellular metabolism of DNA precursors. The enzyme catalyzes the transfer of a phosphate group from adenosine triphosphate (ATP) to the hydroxyl group at the 5' carbon atom of deoxycytidine, forming deoxycytidine monophosphate (dCMP).

Deoxycytidine kinase is a key enzyme in the salvage pathway of pyrimidine nucleotide synthesis and is also involved in the activation of many antiviral and anticancer drugs that are analogs of deoxycytidine. The activity of dCK is tightly regulated, and its expression levels can vary depending on the cell type and physiological conditions.

In addition to its role in nucleotide metabolism, dCK has been implicated in various biological processes, including DNA damage response, cell cycle regulation, and apoptosis. Abnormalities in dCK activity or expression have been associated with several human diseases, including cancer and viral infections. Therefore, modulation of dCK activity has emerged as a potential therapeutic strategy for the treatment of these conditions.

Janus Kinase 3 (JAK3) is a tyrosine kinase enzyme that plays a crucial role in the signaling of cytokines, which are substances secreted by certain cells of the immune system to influence the behavior of other cells. JAK3 is primarily expressed in hematopoietic cells, which are blood-forming cells. It is involved in the activation of the signal transducer and activator of transcription (STAT) proteins, which regulate gene expression in response to cytokine stimulation.

JAK3 is unique among the JAK family members because it is predominantly associated with the interleukin-2 receptor complex, which includes the common gamma chain (γc), and is essential for the development and function of T and B lymphocytes, which are crucial components of the adaptive immune system.

Mutations in JAK3 can lead to severe combined immunodeficiency (SCID) disorders, characterized by profound defects in T and B cell development and function. Conversely, inhibition of JAK3 has been explored as a therapeutic strategy for the treatment of autoimmune diseases and certain types of cancer.

Diphosphoglycerates (also known as 2,3-diphosphoglycerates or 2,3-DPG) are organic molecules found in red blood cells. They play a crucial role in regulating the affinity of hemoglobin for oxygen. Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to the body's tissues.

When the concentration of diphosphoglycerates in red blood cells increases, it reduces the ability of hemoglobin to bind with oxygen, which allows more oxygen to be released into the tissues. This is particularly important in conditions where there is low oxygen availability, such as at high altitudes or in diseases that cause poor oxygen delivery to the tissues, like heart failure and chronic obstructive pulmonary disease (COPD).

In summary, diphosphoglycerates are essential molecules that help regulate hemoglobin's affinity for oxygen, ensuring optimal oxygen delivery to the body's tissues.

TYK2 (Tyrosine Kinase 2) is a member of the Janus kinase (JAK) family of intracellular non-receptor protein tyrosine kinases. It plays a crucial role in the signaling of various cytokines and growth factors, including interferons, interleukin-6, -10, -12, and -23, by associating with their receptors and mediating downstream signal transduction.

The activation of TYK2 leads to the phosphorylation of signal transducers and activators of transcription (STAT) proteins, which then dimerize and translocate to the nucleus, where they regulate gene expression involved in various cellular processes such as immune responses, hematopoiesis, and cell growth. Dysregulation of TYK2 has been implicated in several autoimmune diseases and cancer, making it an attractive target for therapeutic intervention.

The Epidermal Growth Factor Receptor (EGFR) is a type of receptor found on the surface of many cells in the body, including those of the epidermis or outer layer of the skin. It is a transmembrane protein that has an extracellular ligand-binding domain and an intracellular tyrosine kinase domain.

EGFR plays a crucial role in various cellular processes such as proliferation, differentiation, migration, and survival. When EGF (Epidermal Growth Factor) or other ligands bind to the extracellular domain of EGFR, it causes the receptor to dimerize and activate its intrinsic tyrosine kinase activity. This leads to the autophosphorylation of specific tyrosine residues on the receptor, which in turn recruits and activates various downstream signaling molecules, resulting in a cascade of intracellular signaling events that ultimately regulate gene expression and cell behavior.

Abnormal activation of EGFR has been implicated in several human diseases, including cancer. Overexpression or mutation of EGFR can lead to uncontrolled cell growth and division, angiogenesis, and metastasis, making it an important target for cancer therapy.

Northern blotting is a laboratory technique used in molecular biology to detect and analyze specific RNA molecules (such as mRNA) in a mixture of total RNA extracted from cells or tissues. This technique is called "Northern" blotting because it is analogous to the Southern blotting method, which is used for DNA detection.

The Northern blotting procedure involves several steps:

1. Electrophoresis: The total RNA mixture is first separated based on size by running it through an agarose gel using electrical current. This separates the RNA molecules according to their length, with smaller RNA fragments migrating faster than larger ones.

2. Transfer: After electrophoresis, the RNA bands are denatured (made single-stranded) and transferred from the gel onto a nitrocellulose or nylon membrane using a technique called capillary transfer or vacuum blotting. This step ensures that the order and relative positions of the RNA fragments are preserved on the membrane, similar to how they appear in the gel.

3. Cross-linking: The RNA is then chemically cross-linked to the membrane using UV light or heat treatment, which helps to immobilize the RNA onto the membrane and prevent it from washing off during subsequent steps.

4. Prehybridization: Before adding the labeled probe, the membrane is prehybridized in a solution containing blocking agents (such as salmon sperm DNA or yeast tRNA) to minimize non-specific binding of the probe to the membrane.

5. Hybridization: A labeled nucleic acid probe, specific to the RNA of interest, is added to the prehybridization solution and allowed to hybridize (form base pairs) with its complementary RNA sequence on the membrane. The probe can be either a DNA or an RNA molecule, and it is typically labeled with a radioactive isotope (such as ³²P) or a non-radioactive label (such as digoxigenin).

6. Washing: After hybridization, the membrane is washed to remove unbound probe and reduce background noise. The washing conditions (temperature, salt concentration, and detergent concentration) are optimized based on the stringency required for specific hybridization.

7. Detection: The presence of the labeled probe is then detected using an appropriate method, depending on the type of label used. For radioactive probes, this typically involves exposing the membrane to X-ray film or a phosphorimager screen and analyzing the resulting image. For non-radioactive probes, detection can be performed using colorimetric, chemiluminescent, or fluorescent methods.

8. Data analysis: The intensity of the signal is quantified and compared to controls (such as housekeeping genes) to determine the relative expression level of the RNA of interest. This information can be used for various purposes, such as identifying differentially expressed genes in response to a specific treatment or comparing gene expression levels across different samples or conditions.

DEAE-cellulose chromatography is a method of purification and separation of biological molecules such as proteins, nucleic acids, and enzymes. DEAE stands for diethylaminoethyl, which is a type of charged functional group that is covalently bound to cellulose, creating a matrix with positive charges.

In this method, the mixture of biological molecules is applied to a column packed with DEAE-cellulose. The positively charged DEAE groups attract and bind negatively charged molecules in the mixture, such as nucleic acids and proteins, while allowing uncharged or neutrally charged molecules to pass through.

By adjusting the pH, ionic strength, or concentration of salt in the buffer solution used to elute the bound molecules from the column, it is possible to selectively elute specific molecules based on their charge and binding affinity to the DEAE-cellulose matrix. This makes DEAE-cellulose chromatography a powerful tool for purifying and separating biological molecules with high resolution and efficiency.

NIH 3T3 cells are a type of mouse fibroblast cell line that was developed by the National Institutes of Health (NIH). The "3T3" designation refers to the fact that these cells were derived from embryonic Swiss mouse tissue and were able to be passaged (i.e., subcultured) more than three times in tissue culture.

NIH 3T3 cells are widely used in scientific research, particularly in studies involving cell growth and differentiation, signal transduction, and gene expression. They have also been used as a model system for studying the effects of various chemicals and drugs on cell behavior. NIH 3T3 cells are known to be relatively easy to culture and maintain, and they have a stable, flat morphology that makes them well-suited for use in microscopy studies.

It is important to note that, as with any cell line, it is essential to verify the identity and authenticity of NIH 3T3 cells before using them in research, as contamination or misidentification can lead to erroneous results.

A phenotype is the physical or biochemical expression of an organism's genes, or the observable traits and characteristics resulting from the interaction of its genetic constitution (genotype) with environmental factors. These characteristics can include appearance, development, behavior, and resistance to disease, among others. Phenotypes can vary widely, even among individuals with identical genotypes, due to differences in environmental influences, gene expression, and genetic interactions.

Jurkat cells are a type of human immortalized T lymphocyte (a type of white blood cell) cell line that is commonly used in scientific research. They were originally isolated from the peripheral blood of a patient with acute T-cell leukemia. Jurkat cells are widely used as a model system to study T-cell activation, signal transduction, and apoptosis (programmed cell death). They are also used in the study of HIV infection and replication, as they can be infected with the virus and used to investigate viral replication and host cell responses.

Magnesium is an essential mineral that plays a crucial role in various biological processes in the human body. It is the fourth most abundant cation in the body and is involved in over 300 enzymatic reactions, including protein synthesis, muscle and nerve function, blood glucose control, and blood pressure regulation. Magnesium also contributes to the structural development of bones and teeth.

In medical terms, magnesium deficiency can lead to several health issues, such as muscle cramps, weakness, heart arrhythmias, and seizures. On the other hand, excessive magnesium levels can cause symptoms like diarrhea, nausea, and muscle weakness. Magnesium supplements or magnesium-rich foods are often recommended to maintain optimal magnesium levels in the body.

Some common dietary sources of magnesium include leafy green vegetables, nuts, seeds, legumes, whole grains, and dairy products. Magnesium is also available in various forms as a dietary supplement, including magnesium oxide, magnesium citrate, magnesium chloride, and magnesium glycinate.

Imidazoles are a class of heterocyclic organic compounds that contain a double-bonded nitrogen atom and two additional nitrogen atoms in the ring. They have the chemical formula C3H4N2. In a medical context, imidazoles are commonly used as antifungal agents. Some examples of imidazole-derived antifungals include clotrimazole, miconazole, and ketoconazole. These medications work by inhibiting the synthesis of ergosterol, a key component of fungal cell membranes, leading to increased permeability and death of the fungal cells. Imidazoles may also have anti-inflammatory, antibacterial, and anticancer properties.

The abomasum is the fourth and final stomach chamber in ruminant animals, such as cows, sheep, and goats. It is often referred to as the "true" stomach because its structure and function are most similar to the stomachs of non-ruminant animals, including humans.

In the abomasum, gastric juices containing hydrochloric acid and digestive enzymes are secreted, which help to break down proteins and fats in the ingested feed. The abomasum also serves as a site for nutrient absorption and further mechanical breakdown of food particles before they enter the small intestine.

The term "abomasum" is derived from Latin, where "ab-" means "away from," and "omassum" refers to the "stomach." This name reflects its location away from the other three stomach chambers in ruminants.

A kinase anchor protein (AKAP) is a type of scaffolding protein that plays a role in organizing and targeting various signaling molecules within cells. AKAPs are so named because they can bind to and anchor protein kinases, enzymes that add phosphate groups to other proteins, thereby modulating their activity. This allows for the localized regulation of signaling pathways and helps ensure that specific cellular responses occur in the correct location and at the right time. AKAPs can also bind to other signaling molecules, such as phosphatases, ion channels, and second messenger systems, forming large complexes that facilitate efficient communication between different parts of the cell.

There are many different AKAPs identified in various organisms, and they play crucial roles in a wide range of cellular processes, including cell division, signal transduction, and gene expression. Mutations or dysregulation of AKAPs have been implicated in several diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the structure, function, and regulation of AKAPs is an important area of research with potential therapeutic implications.

"Swine" is a common term used to refer to even-toed ungulates of the family Suidae, including domestic pigs and wild boars. However, in a medical context, "swine" often appears in the phrase "swine flu," which is a strain of influenza virus that typically infects pigs but can also cause illness in humans. The 2009 H1N1 pandemic was caused by a new strain of swine-origin influenza A virus, which was commonly referred to as "swine flu." It's important to note that this virus is not transmitted through eating cooked pork products; it spreads from person to person, mainly through respiratory droplets produced when an infected person coughs or sneezes.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

Actin is a type of protein that forms part of the contractile apparatus in muscle cells, and is also found in various other cell types. It is a globular protein that polymerizes to form long filaments, which are important for many cellular processes such as cell division, cell motility, and the maintenance of cell shape. In muscle cells, actin filaments interact with another type of protein called myosin to enable muscle contraction. Actins can be further divided into different subtypes, including alpha-actin, beta-actin, and gamma-actin, which have distinct functions and expression patterns in the body.

Maleimides are a class of chemical compounds that contain a maleimide functional group, which is characterized by a five-membered ring containing two carbon atoms and three nitrogen atoms. The double bond in the maleimide ring makes it highly reactive towards nucleophiles, particularly thiol groups found in cysteine residues of proteins.

In medical and biological contexts, maleimides are often used as cross-linking agents to modify or label proteins, peptides, and other biomolecules. For example, maleimide-functionalized probes such as fluorescent dyes, biotin, or radioisotopes can be covalently attached to thiol groups in proteins for various applications, including protein detection, purification, and imaging.

However, it is important to note that maleimides can also react with other nucleophiles such as amines, although at a slower rate. Therefore, careful control of reaction conditions is necessary to ensure specificity towards thiol groups.

Restriction mapping is a technique used in molecular biology to identify the location and arrangement of specific restriction endonuclease recognition sites within a DNA molecule. Restriction endonucleases are enzymes that cut double-stranded DNA at specific sequences, producing fragments of various lengths. By digesting the DNA with different combinations of these enzymes and analyzing the resulting fragment sizes through techniques such as agarose gel electrophoresis, researchers can generate a restriction map - a visual representation of the locations and distances between recognition sites on the DNA molecule. This information is crucial for various applications, including cloning, genome analysis, and genetic engineering.

Antibodies are proteins produced by the immune system in response to the presence of a foreign substance, such as a bacterium or virus. They are capable of identifying and binding to specific antigens (foreign substances) on the surface of these invaders, marking them for destruction by other immune cells. Antibodies are also known as immunoglobulins and come in several different types, including IgA, IgD, IgE, IgG, and IgM, each with a unique function in the immune response. They are composed of four polypeptide chains, two heavy chains and two light chains, that are held together by disulfide bonds. The variable regions of the heavy and light chains form the antigen-binding site, which is specific to a particular antigen.

DNA topoisomerases are enzymes that regulate the topological state of DNA during various cellular processes such as replication, transcription, and repair. They do this by introducing temporary breaks in the DNA strands and allowing the strands to rotate around each other, thereby relieving torsional stress and supercoiling. Topoisomerases are classified into two types: type I and type II.

Type II topoisomerases are further divided into two subtypes: type IIA and type IIB. These enzymes function by forming a covalent bond with the DNA strands, cleaving them, and then passing another segment of DNA through the break before resealing the original strands. This process allows for the removal of both positive and negative supercoils from DNA as well as the separation of interlinked circular DNA molecules (catenanes) or knotted DNA structures.

Type II topoisomerases are essential for cell viability, and their dysfunction has been linked to various human diseases, including cancer and neurodegenerative disorders. They have also emerged as important targets for the development of anticancer drugs that inhibit their activity and induce DNA damage leading to cell death. Examples of type II topoisomerase inhibitors include etoposide, doxorubicin, and mitoxantrone.

Checkpoint Kinase 2 (Chk2) is a serine/threonine protein kinase that plays a crucial role in the DNA damage response and the regulation of the cell cycle. It is activated by various types of DNA damage, including double-strand breaks, and phosphorylates several downstream targets involved in cell cycle arrest, DNA repair, and apoptosis. Chk2 is a key player in the G2/M checkpoint, which prevents cells with damaged DNA from entering mitosis and dividing. Mutations in the Chk2 gene have been associated with increased risk of cancer.

Casein kinase I isoform alpha is an enzyme that in humans is encoded by the CSNK1A1 gene. Casein kinase 1, alpha 1 has been ... Zhang Y, Qiu WJ, Chan SC, Han J, He X, Lin SC (May 2002). "Casein kinase I and casein kinase II differentially regulate axin ... Casein kinase 1 GRCh38: Ensembl release 89: ENSG00000113712 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024576 ... Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ...
... , a type of kinase enzyme, may refer to: Casein kinase 1, serine/threonine-selective protein kinase family Casein ... kinase 2, a serine/threonine-selective protein kinase This article includes a list of related items that share the same name ( ... Protein kinases, All stub articles, Enzyme stubs). ...
... "casein kinase 1 alpha" and "casein kinase 1 epsilon". Casein kinase 1 epsilon has been suggested to play a role in ... Casein kinase 2 - a distinct protein kinase family Eide EJ, Virshup DM (May 2001). "Casein kinase I: another cog in the ... In humans there are three casein kinase 1 gamma enzymes. Xenopus casein kinase 1 gamma (CK1gamma) is associated with the cell ... "A noncanonical sequence phosphorylated by casein kinase 1 in beta-catenin may play a role in casein kinase 1 targeting of ...
... (EC 2.7.11.1)(CK2/CSNK2) is a serine/threonine-selective protein kinase that has been implicated in cell cycle ... CSNK2A1 CSNK2A2 Casein kinase 1 - a distinct protein kinase family Ahmad KA, Wang G, Unger G, Slaton J, Ahmed K (2008). " ... Schwein PA, Ge Y, Yang B, D'Souza A, Mody A, Shen D, Woo CM (May 2022). "Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha ... Casein kinase 2 activity has been reported to be activated following Wnt signaling pathway activation. A Pertussis toxin- ...
Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as ... Casein kinase 2, alpha 1 has been shown to interact with: APC, ATF1, ATF2, C-Fos, C-jun, CDC25B, CHEK1, CREBBP, CSNK2B, DDIT3, ... "Entrez Gene: CSNK2A1 casein kinase 2, alpha 1 polypeptide". Homma MK, Li D, Krebs EG, Yuasa Y, Homma Y (April 2002). " ... Casein kinase II subunit alpha is an enzyme that in humans is encoded by the CSNK2A1 gene. ...
The protein encoded by the casein kinase 1 epsilon gene is a serine/threonine protein kinase and a member of the casein kinase ... Casein kinase 1 epsilon, and related casein kinase 1 delta, is dephosphorylated in this pathway. Dephosphorylation of casein ... The current theory for how casein kinase 1 epsilon and/or casein kinase 1 delta function in this pathway is that both casein ... After priming through phosphorylation by the serine/threonine kinase LATS, both casein kinase 1 epsilon and casein kinase 1 ...
Phosphorylation by casein kinase II". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1264 (3): 303-11. ... Sheu GT, Traugh JA (Jan 1999). "A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII". ... Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII". The Journal of Biological Chemistry. ...
In vitro phosphorylation by casein kinase II". The Journal of Biological Chemistry. 269 (49): 31034-40. doi:10.1016/S0021-9258( ...
Casein kinase 1, alpha 1 Nucleolin, P110α, PRKCI, Protein kinase D1, and Protein kinase Mζ. Model organisms have been used in ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ... "Identification of casein kinase Ialpha interacting protein partners". FEBS Letters. 517 (1-3): 167-71. doi:10.1016/s0014-5793( ...
Kumar, R.; Tao, M. (1975-11-20). "Multiple forms of casein kinase from rabbit erythrocytes". Biochimica et Biophysica Acta (BBA ...
Dubois T, Howell S, Zemlickova E, Aitken A (April 2002). "Identification of casein kinase Ialpha interacting protein partners ... "Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation". ...
O'Brien KA, Lemke SJ, Cocke KS, Rao RN, Beckmann RP (July 1999). "Casein kinase 2 binds to and phosphorylates BRCA1". Biochem. ... "BRCA1 interacts with and is required for paclitaxel-induced activation of mitogen-activated protein kinase kinase kinase 3". ... kinase and ATM and Rad3 related kinase mediate phosphorylation of Brca1 at distinct and overlapping sites. In vivo assessment ... ATM/ATR are kinases activated by DNA damage. Mutation of serine residues may affect localization of BRCA1 to sites of DNA ...
Zemlickova E, Johannes FJ, Aitken A, Dubois T (March 2004). "Association of CPI-17 with protein kinase C and casein kinase I". ... Dubois T, Howell S, Zemlickova E, Aitken A (April 2002). "Identification of casein kinase Ialpha interacting protein partners ... Multiple kinases are identified to phosphorylate CPI-17, such as PKC, ROCK, PKN, ZIPK, ILK, and PAK. Agonist stimulation of ... Protein phosphatase 1 regulatory subunit 14A also known as CPI-17 (C-kinase potentiated Protein phosphatase-1 Inhibitor Mr = 17 ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological ... "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological ...
Kim YM, Barak LS, Caron MG, Benovic JL (May 2002). "Regulation of arrestin-3 phosphorylation by casein kinase II". The Journal ... Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ...
Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN (April 1989). "Myc oncoproteins are phosphorylated by casein kinase II". The EMBO ... "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase". Proceedings of the National ... Gupta S, Davis RJ (October 1994). "MAP kinase binds to the NH2-terminal activation domain of c-Myc". FEBS Letters. 353 (3): 281 ... Iijima S, Teraoka H, Date T, Tsukada K (June 1992). "DNA-activated protein kinase in Raji Burkitt's lymphoma cells. ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... "High mobility group proteins 1 and 2 can function as DNA-binding regulatory components for DNA-dependent protein kinase in ...
... down-regulation of Casein kinase 2 can promote tumorigenesis. Protein kinase C is a protein-regulator and is highly involved in ... Casein kinase 2 can play a role in cell cycle regulation, DNA repair, and necessary for cell survival; ...
1992). "Prothymosin alpha is phosphorylated by casein kinase-2". FEBS Lett. 312 (2-3): 152-6. doi:10.1016/0014-5793(92)80924-6 ...
The casein kinase 1 (CKI) family of kinases is a highly conserved group of proteins that are found in organisms from ... The casein kinase 1 (CK1) family of kinases comprises a highly conserved group of proteins found in organisms ranging from ... The mammalian homolog of DBT is casein kinase I epsilon, which plays a role in regulating the circadian rhythm in mammals. The ... Sekine T, Yamaguchi T, Hamano K, Young MW, Shimoda M, Saez L (February 2008). "Casein kinase I epsilon does not rescue double- ...
Li D, Dobrowolska G, Krebs EG (Jun 1996). "The physical association of casein kinase 2 with nucleolin". The Journal of ... Li D, Dobrowolska G, Krebs EG (Jun 1996). "The physical association of casein kinase 2 with nucleolin". The Journal of ... Jordan P, Heid H, Kinzel V, Kübler D (Dec 1994). "Major cell surface-located protein substrates of an ecto-protein kinase are ... Zhou G, Seibenhener ML, Wooten MW (Dec 1997). "Nucleolin is a protein kinase C-zeta substrate. Connection between cell surface ...
Apel ED, Litchfield DW, Clark RH, Krebs EG, Storm DR (Jun 1991). "Phosphorylation of neuromodulin (GAP-43) by casein kinase II ... It is a major protein kinase C (PKC) substrate and is considered to play a key role in neurite formation, regeneration, and ... However, F1 was not cAMP kinase dependent. B-50 was regulated by the pituitary peptide ACTH and was associated with grooming ... GAP-43 is also a protein kinase C (PKC) substrate. Phosphorylation of serine-41 on GAP-43 by PKC regulates neurite formation, ...
There is a possible Casein Kinase II phosphorylation site between amino acids 22-25. Casein Kinase II phosphorylation is ... its casein kinase II phosphorylation site, and its ubiquitous expression across tissues. The Hp53int1 gene expression is ... "GPS 5.0 - Kinase-specific Phosphorylation Site Prediction". gps.biocuckoo.cn. Retrieved 2022-12-16. "Motif Scan". myhits.sib. ... and protein-tyrosine kinase). There are two identified SNPS for Hp53int1. SNP 15 falls at position 32 in a sequence of 43 ...
Kim YM, Barak LS, Caron MG, Benovic JL (2002). "Regulation of arrestin-3 phosphorylation by casein kinase II". J. Biol. Chem. ...
Cooper CD, Lampe PD (Nov 2002). "Casein kinase 1 regulates connexin-43 gap junction assembly". The Journal of Biological ... factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase ...
"Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II". FEBS Letters. 257 (1): 101-4. doi: ... Nissen MS, Langan TA, Reeves R (Oct 1991). "Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility ...
Hino S, Michiue T, Asashima M, Kikuchi A (April 2003). "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is ... Swiatek W, Tsai IC, Klimowski L, Pepler A, Barnette J, Yost HJ, Virshup DM (March 2004). "Regulation of casein kinase I epsilon ...
Lussier G, Larose L (1997). "A casein kinase I activity is constitutively associated with Nck". J. Biol. Chem. 272 (5): 2688-94 ... "Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta". J ... Su YC, Han J, Xu S, Cobb M, Skolnik EY (March 1997). "NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates ... Su YC, Han J, Xu S, Cobb M, Skolnik EY (1997). "NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the ...
... a casein kinase II phosphorylation site, a Leucine zipper pattern, two N-myristylation sites, and three protein kinase C ... Casein kinase II is involved with protein stability and cell signaling response. Leucine zippers are sequence motifs that ... Litchfield DW, Lüscher B (November 1993). Khandelwal RL, Wang JH (eds.). "Casein kinase II in signal transduction and cell ... Protein kinase C phosphorylation has to do with regulation of cell proliferation and gene expression. The secondary structure ...
This protein may function in the inhibition of casein kinase. MRP14 complexes with MRP-8 (S100A8), another member of the S100 ... Murao S, Collart FR, Huberman E (1989). "A protein containing the cystic fibrosis antigen is an inhibitor of protein kinases". ...
Casein kinase I isoform alpha is an enzyme that in humans is encoded by the CSNK1A1 gene. Casein kinase 1, alpha 1 has been ... Zhang Y, Qiu WJ, Chan SC, Han J, He X, Lin SC (May 2002). "Casein kinase I and casein kinase II differentially regulate axin ... Casein kinase 1 GRCh38: Ensembl release 89: ENSG00000113712 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024576 ... Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ...
Casein kinase II subunit alpha (maize). Find diseases associated with this biological target and compounds tested against it in ...
Casein Kinase 2 beta (CSNK2B) (NM_001320) Human Untagged Clone - 10 µg - SC108248 from OriGene ...
... Author: Kucherenko, Yuliya; Zelenak, ... Effect of Casein Kinase 1 alpha Activator Pyrvinium Pamoate on Erythrocyte Ion Channels. DSpace Repository. Login ...
Proteins kinase CK2 (previously called casein kinase 2) is a pivotal. immune 5-ht5 Receptors CX-6258 manufacture, ENO2 ... Proteins kinase CK2 (previously called casein kinase 2) is a pivotal and ubiquitously expressed member of the protein CX-6258 ... mitogen-activated protein kinases (MAPKs) glycogen synthase kinases (GSKs) and CDK-like kinases (CLKs). 1999 ?; Pinna 2002 ?; ... cancer may be the most commonly diagnosed malignancy in men and » B kinase is a main regulator of cell division (1). ...
PAWS1 controls Wnt signalling through association with casein kinase 1α. More about Open Access at the Crick Authors list. ... We show that PAWS1 interacts and co-localises with the α isoform of casein kinase 1 (CK1), and that PAWS1 mutations incapable ...
BLAST of Casein kinase I vs. TrEMBL Match: D7FMN1 (Casein kinase (Serine/threonine/tyrosine protein kinase) OS=Ectocarpus ... Casein kinase I isoform alpha OS=Ovis aries OX=994... [more]. sp,P67828,KC1A_RABIT. 2.998e-107. 52.56. Casein kinase I isoform ... Casein kinase I isoform alpha OS=Bos taurus OX=991... [more]. sp,P97633,KC1A_RAT. 5.170e-107. 52.56. Casein kinase I isoform ... casein kinase 1, gamma 2a [Source:ZFIN;Acc:ZDB-GEN... [more]. csnk1g1. 1.065e-67. 48.58. casein kinase 1, gamma 1 [Source:NCBI ...
Human casein kinase 2, alpha 1 polypeptide subunit. with compound 1a [PMID: 24900749] ...
... belongs to the serine/threonine protein kinases. CK1 members, which commonly exist in all eukaryotes, are involved in the ... The casein kinase 1 (CK1) belongs to the serine/threonine protein kinases. CK1 members, which commonly exist in all eukaryotes ... The Role of Casein Kinase 1 in Meiosis. Yue-Fang Zhao and Cheng-Guang Liang ...
Human CSNK1d(Casein Kinase 1 Delta) ELISA Kit. Human CSNK1d(Casein Kinase 1 Delta) ELISA Kit. Contact us to Order: [email ... Description: A sandwich ELISA kit for detection of Casein Kinase 1 Delta from Human in samples from blood, serum, plasma, cell ... Description: A sandwich ELISA for quantitative measurement of Rat Casein kinase I isoform delta(CSNK1D) in samples from blood, ... Description: A sandwich ELISA for quantitative measurement of Rat Casein kinase I isoform delta(CSNK1D) in samples from blood, ...
β-TrCP recognizes cyclin F through a non-canonical degron site (TSGXXS) after its phosphorylation by casein kinase II. The ... β-TrCP- and Casein Kinase II-Mediated Degradation of Cyclin F Controls Timely Mitotic Progression. ... CKII, CRLs, F-box protein, SCF, cell cycle, cyclin F, mitosis, ubiquitin, β-TrCP, Casein Kinase II, Cyclins, HEK293 Cells, HeLa ... β-TrCP- and Casein Kinase II-Mediated Degradation of Cyclin F Controls Timely Mitotic Progression. ...
T2 - "Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated by ... title = "Retraction: {"}Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and ... Retraction: "Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated ... Retraction: "Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated ...
If a damaging outcome is found then we attempt to examine facts contained … Read more Unwinding The Wnt Action Of Casein ... Unwinding The Wnt Action Of Casein Kinase 1. Post date. November 29, 2017. Post last updated dateUpdated November 29, 2017. ...
In the current study, we identified a protein kinase activity in rat liver supernatant that is up-regulated by inositol 1,3,4,5 ... Using the phosphorylation of this substrate in an assay, we purified the inositol phosphate-regulated protein kinase and ... was one of the first protein kinases to be discovered and has been suggested to be responsible for as much as one-fifth of the ... The substrate for the inositol phosphate-regulated protein kinase was identified as a phosphatidylcholine transfer protein-like ...
Casein kinase 1 (CK1) family. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance ... Casein kinase 1 (CK1) family: casein kinase 1 gamma 3. Last modified on 29/01/2016. Accessed on 09/12/2023. IUPHAR/BPS Guide to ... p38 MAP kinase inhibitor III Hs. Inhibitor. Inhibition. 58.4 96.0 21.0 IRAK-1/4 inhibitor Hs. Inhibitor. Inhibition. 58.7 89.0 ... EMD Millipore KinaseProfilerTM screen/Reaction Biology Kinase HotspotSM screen A screen profiling 158 kinase inhibitors ( ...
Resistance to BET inhibitors in lung adenocarcinoma is mediated by casein kinase phosphorylation of BRD4 *Jack Calder ... Our previous work identified TYRO3 (TYRO3 protein tyrosine kinase) and AXL (AXL receptor tyrosine kinase) activation in LMS ... tyrosine kinase) receptor tyrosine kinase family, which emerged as new potential targets in many oncological diseases, from ... Exposure to both kinase inhibitors induced cell cycle arrest and/or apoptosis in the LMS cell lines tested, along with ...
A series of flavonoid compounds was tested as inhibitors of protein kinase CK2. Several substances were found to be highly ... CK2 is a ubiquitous protein kinase involved in many cell functions. During the last years it became an interesting target in ... Casein Kinase II / antagonists & inhibitors* * Casein Kinase II / chemistry * Casein Kinase II / isolation & purification ... Selected flavonoid compounds as promising inhibitors of protein kinase CK2α and CK2α, the catalytic subunits of CK2 ...
Casein kinase-1-Delta(CK1d) is an enzyme known to phosphorylate several key proteins in the circadian rhythm cycle, and in ... Casein Kinase-1𝛿 Delta Is Required for Postnatal Survival In Mice. : Worcester Polytechnic Institute, 2008. ... Casein Kinase-1𝛿 Delta Is Required for Postnatal Survival In Mice. : Worcester Polytechnic Institute. ... Conde, H. (2008). Casein Kinase-1𝛿 Delta is Required for Postnatal Survival in Mice. : Worcester Polytechnic Institute. ...
... a characteristic of casein kinase II phosphorylation sites. Casein kinase II phosphorylated DARPP-32 with an apparent Km value ... However, phosphorylation of DARPP-32 by casein kinase II facilitated phosphorylation of Thr34 by cAMP-dependent protein kinase ... DARPP-32 phosphorylated by casein kinase II was dephosphorylated by protein phosphatases-1 and -2A. Phosphorylation by casein ... Purified bovine DARPP-32 was phosphorylated in vitro by casein kinase II to a stoichiometry greater than 2 mol of phosphate/mol ...
... TIBALDI, ELENA;ARRIGONI, ... In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the ... In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the ... This led to the identification of 47 proteins altogether, none of which is a bona fide protein kinase. At least 9 of the ...
Crystal structure of human protein kinase CK2alpha(CSNK2A2 gene product) in complex with the 2-aminothiazole-type inhibitor Cl ... Casein kinase II subunit alpha. A. 364. Homo sapiens. Mutation(s): 1 Gene Names: CSNK2A2, CK2A2. EC: 2.7.11.1. ... Crystal structure of human protein kinase CK2alpha(CSNK2A2 gene product) in complex with the 2-aminothiazole-type inhibitor Cl ... Structural and Mechanistic Basis of the Inhibitory Potency of Selected 2-Aminothiazole Compounds on Protein Kinase CK2.. ...
Casein kinase II subunit alpha. > Casein Kinase 2, subunit alpha * Occurring in:. *Casein kinase II subunit alpha. > Serine/ ... Casein kinase II subunit alpha. > Protein kinase domain * Occurring in:. *Casein kinase II subunit alpha. > Protein kinase- ... Casein kinase II subunit alpha. > Protein kinase, ATP binding site * Occurring in:. * ... Casein kinase II subunit alpha Chains: A, B Molecule details › Chains: A, B. Length: 352 amino acids. Theoretical weight: 41.47 ...
Shop enQuireBio™ Recombinant Human Casein kinase I isoform epsilon Protein at Fishersci.se ...
T1 - Casein kinase 2-dependent phosphorylation of human Rad9 mediates the interaction between human Rad9-Hus1-Rad1 complex and ... Casein kinase 2-dependent phosphorylation of human Rad9 mediates the interaction between human Rad9-Hus1-Rad1 complex and ... Casein kinase 2-dependent phosphorylation of human Rad9 mediates the interaction between human Rad9-Hus1-Rad1 complex and ... Casein kinase 2-dependent phosphorylation of human Rad9 mediates the interaction between human Rad9-Hus1-Rad1 complex and ...
... is a serine/threonine-selective protein kinase that has been involved in a variety of cellular processes such as DNA repair, ... CK2 (casein kinase 2) is a serine/threonine-selective protein kinase that has been involved in a variety of cellular processes ... CK2 (casein kinase 2) is an ubiquitously expressed and highly conserved serine/threonine protein kinase that forms a tetramer ... Inhibition of casein kinase 2 blocks G2/M transition in early embryo mitosis but not in oocyte meiosis in mouse. J Reprod Dev. ...
casein kinase. IRAK:. interleukin 1 receptor associated kinase. ICAM-1:. intercellular adhesion molecule-1 ... MAPKK kinase (MAP3K or MKKK) and MAPK kinase (MAP2K or MKK) of three pathways have different substrates and intermolecular ... Akt (protein kinase B) can be phosphorylated by PDK1 and PDK2, or directly phosphorylated by phosphatidylinositol 3′-kinase ( ... Berberine induces dedifferentiation by actin cytoskeleton reorganization via phosphoinositide 3-kinase/Akt and p38 kinase ...
Casein Kinase I Family. The casein kinase I (CKI) proteins originally were characterized as ubiquitous serine/threonine kinases ... Abbreviations used in this paper: CDK, cyclin-dependent kinase; CKI, casein kinase I; CTK, cytoplasmic tyrosine kinase; DSP, ... Abbreviations used in this paper: CDK, cyclin-dependent kinase; CKI, casein kinase I; CTK, cytoplasmic tyrosine kinase; DSP, ... SNF1/AMP-dependent kinase, EMK, CHK2, myosin light chain kinase (MLCK), phosphorylase kinase, death-associated protein kinase, ...
AKT Kinase (PKB) (1) Casein kinase (2) Caspase (4) Caspase 1 (1) ... Cyclin-dependent kinase (2) DNA-dependent Protein Kinase (DNA- ... S6 Kinase Substrate (229-239), Amide, Biotinalyted - 1 mg *Biotin-AKRRRLSSLRA-NH2 ...
  • β-TrCP recognizes cyclin F through a non-canonical degron site (TSGXXS) after its phosphorylation by casein kinase II. (ox.ac.uk)
  • Using the phosphorylation of this substrate in an assay, we purified the inositol phosphate-regulated protein kinase and determined it to be CK2. (ox.ac.uk)
  • In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the phosphorylation of caseins in lactating mammary gland, the proteins present in fractions enriched in G-CK activity eluted from DEAE-Sepharose and heparin-Sepharose columns were resolved by two-dimensional electrophoresis and analyzed by mass spectrometry. (unipd.it)
  • Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase II. (cornell.edu)
  • The phosphorylated residues are located NH2-terminal to acidic amino acid residues, a characteristic of casein kinase II phosphorylation sites. (cornell.edu)
  • Phosphorylation by casein kinase II did not affect the potency of DARPP-32 as an inhibitor of protein phosphatase-1, which depended only on phosphorylation of Thr34 by cAMP-dependent protein kinase. (cornell.edu)
  • However, phosphorylation of DARPP-32 by casein kinase II facilitated phosphorylation of Thr34 by cAMP-dependent protein kinase with a 2.2-fold increase in the Vmax and a 1.4-fold increase in the apparent Km. (cornell.edu)
  • Phosphorylation of DARPP-32 by casein kinase II in intact cells may therefore modulate its phosphorylation in response to increased levels of cAMP. (cornell.edu)
  • Levels of cellular protein phosphorylation are modulated both by protein kinases and phosphatases. (rupress.org)
  • To fully understand this complex and essential regulatory process, the kinases and phosphatases mediating the changes in cellular phosphorylation must be identified and characterized. (rupress.org)
  • Phosphorylation by Casein Kinase 2 Facilitates Psh1 Protein-assisted Degradation of Cse4 Protein. (stowers.org)
  • Casein kinase-2 mediated phosphorylation increases the SUMO-dependent activity of the cytomegalovirus transactivator IE2. (ncbs.res.in)
  • A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. (bvsalud.org)
  • The casein kinase 1 (CK1) belongs to the serine/threonine protein kinases. (longdom.org)
  • CK2 (casein kinase 2) is a serine/threonine-selective protein kinase that has been involved in a variety of cellular processes such as DNA repair, cell cycle control and circadian rhythm regulation. (biomedcentral.com)
  • CK2 (casein kinase 2) is an ubiquitously expressed and highly conserved serine/threonine protein kinase that forms a tetramer containing two catalytic (α and/or α´) subunits and two regulatory β subunits [ 1 ]. (biomedcentral.com)
  • The casein kinase 1 enzymes (CK1) form a family of serine/threonine kinases with seven CK1. (muni.cz)
  • Both receptors belong to the TAM (TYRO3, AXL and MER - MER proto-oncogene, tyrosine kinase) receptor tyrosine kinase family, which emerged as new potential targets in many oncological diseases, from leukaemia to solid tumours ( Graham et al, 2014 ). (nature.com)
  • A further 91 subfamilies were found in all three metazoan kinomes, including the tyrosine kinase (TK) group and the TKL group, which mediate much of the complexity of intercellular signal transduction. (wormbook.org)
  • A screen of 72 inhibitors against 456 human kinases. (guidetoimmunopharmacology.org)
  • A screen profiling 158 kinase inhibitors (Calbiochem Protein Kinase Inhibitor Library I and II, catalogue numbers 539744 and 539745) for their inhibitory activity at 1µM and 10µM against 234 human recombinant kinases using the EMD Millipore KinaseProfiler TM service. (guidetoimmunopharmacology.org)
  • A screen profiling the inhibitory activity of 178 commercially available kinase inhibitors at 0.5µM against a panel of 300 recombinant protein kinases using the Reaction Biology Corporation Kinase Hotspot SM platform. (guidetoimmunopharmacology.org)
  • 2011) 7-(4H-1,2,4-Triazol-3-yl)benzo[c][2,6]naphthyridines: a novel class of Pim kinase inhibitors with potent cell antiproliferative activity. (guidetoimmunopharmacology.org)
  • A series of flavonoid compounds was tested as inhibitors of protein kinase CK2. (nih.gov)
  • Selective inhibitors of protein kinase CK2 with significant cytotoxicity on tumor cells based on a 2-aminothiazole scaffold were described recently. (rcsb.org)
  • Proteins kinase CK2 (previously called casein kinase 2) is a pivotal and ubiquitously expressed member of the protein CX-6258 manufacture kinase CMGC subfamily which includes cyclin-dependent kinases (CDKs) mitogen-activated protein kinases (MAPKs) glycogen synthase kinases (GSKs) and CDK-like kinases (CLKs). (immune-source.com)
  • and it has been within many diseases especially cancer rendering it an interesting focus on inside CX-6258 manufacture the druggable category of eukaryotic proteins kinases (Pagano et al. (immune-source.com)
  • This led to the identification of 47 proteins altogether, none of which is a bona fide protein kinase. (unipd.it)
  • Many of the proteins phosphorylated by and/or associated with G-CK belong to the category of chaperonines, including HSP90, GRP-94 and -78, and various isoforms of protein disulfide isomerases, suggesting a global role of this kinase in the modulation of protein folding. (unipd.it)
  • Casein kinase-1-Delta(CK1d) is an enzyme known to phosphorylate several key proteins in the circadian rhythm cycle, and in particular to phosphorylate Per to induce its movement back into the nucleus to regulate the circadian period. (wpi.edu)
  • Purified bovine DARPP-32 was phosphorylated in vitro by casein kinase II to a stoichiometry greater than 2 mol of phosphate/mol of protein whereas two structurally and functionally related proteins, protein phosphatase inhibitor-1 and G-substrate, were poor substrates for this enzyme. (cornell.edu)
  • By phosphorylating substrate proteins, kinases modify the activity, location and affinities of up to 30% of all cellular proteins, and direct most cellular processes, particularly in signal transduction and co-ordination of complex pathways. (wormbook.org)
  • Of the kinases not previously characterized as regulators of early vertebrate development, embryos Nagk may be the first enzyme within the salvage changes and pathway free of charge, cytoplasmic GlcNAc produced from degradative mobile pathways into UDP-GlcNAc, that is after that moved onto oligosaccharide stores that are included into glycosylated proteins and glycosaminoglycans (Hinderlich et al. (exposed-skin-care.net)
  • Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins. (bvsalud.org)
  • The substrate for the inositol phosphate-regulated protein kinase was identified as a phosphatidylcholine transfer protein-like protein. (ox.ac.uk)
  • 1. Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. (guidetoimmunopharmacology.org)
  • Casein (from cow's milk) has been linked to migraines (3), bi-polar (4), schizophrenia(5)… which of those don't run parallel with mood issues? (wholefoodsmagazine.com)
  • Immunoblotting and competitive enzyme-linked immunosorbent assays have identified a 30-kD glycinin from soybeans that cross-reacts with cow's milk caseins and is composed of 2 polypeptides (A5 and B3) linked by a disulphide bond. (medscape.com)
  • Among they were casein kinase 1 epsilon and delta, known regulators of Wnt signaling (Peters et al. (exposed-skin-care.net)
  • Casein kinase I isoform alpha is an enzyme that in humans is encoded by the CSNK1A1 gene. (wikipedia.org)
  • Many of these pathways are highly conserved, and 53 distinct kinase functions and subfamilies appear to have been conserved between yeasts, nematodes, insects and vertebrates, with a further 91 subfamilies of kinases being seen throughout metazoan genomes. (wormbook.org)
  • In vitro, DARPP-32 phosphorylated by casein kinase II was dephosphorylated by protein phosphatases-1 and -2A. (cornell.edu)
  • Here, we demonstrate that in vitro casein kinase 2 (CK2) specifically interacts with human 9-1-1 and phosphorylates serines 341 and 387 (Ser-341 and Ser-387) in the C-terminal tail of Rad9. (elsevierpure.com)
  • Inhibition of protein kinase CK2 by anthraquinone-related compounds. (cathdb.info)
  • Most protein kinases share a common ePK (eukaryotic protein kinase) catalytic domain, and can be identified by sequence similarity with Blast or profile hidden Markov models (HMMs). (wormbook.org)
  • Casein kinase 2 (CK2) was one of the first protein kinases to be discovered and has been suggested to be responsible for as much as one-fifth of the eukaryotic phosphoproteome. (ox.ac.uk)
  • Protein kinases constitute one of the largest and most important of protein families, accounting for ~2% of genes in a variety of eukaryotic genomes. (wormbook.org)
  • Such radiations include genes involved in spermatogenesis, chemosensation, Wnt signaling and FGF receptor-like kinases. (wormbook.org)
  • The LuminoCell costs $40, requires less than 1 h to assemble, and it is capable of performing real-time sensitive detection of both magnitude and duration of the activity of major signalling pathways in cell cultures, including receptor tyrosine kinases (EGF and FGF), WNT/β-catenin, and NF-κB. (muni.cz)
  • The remaining atypical protein kinases (aPK) belong to several families, some of which have structural, but not sequence similarity to ePKs. (wormbook.org)
  • The classification is based on sequence similarity within the kinase domain, the presence of additional domains, known biological functions, and conservation across divergent genomes. (wormbook.org)
  • We show that PAWS1 interacts and co-localises with the α isoform of casein kinase 1 (CK1), and that PAWS1 mutations incapable of binding CK1 fail both to activate Wnt signalling and to elicit axis duplication in embryos. (crick.ac.uk)
  • Casein kinase iδ mutations in familial migraine and advanced sleep phase. (wholefoodsmagazine.com)
  • Using patch-clamp electrophysiology in brain slices prepared from male rats, we reveal that opioid withdrawal abruptly reduces the ability of these peptides to inhibit neurotransmission, a direct consequence of a protein kinase A (PKA)-driven increase in the synaptic activity of peptidases. (jneurosci.org)
  • Casein kinase 1, alpha 1 has been shown to interact with Centaurin, alpha 1 and AXIN1. (wikipedia.org)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Casein Kinase 1 Delta (CSNK1d) in samples from tissue homogenates or other biological fluids. (1elisakits.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Casein Kinase 1 Delta (CSNK1d) in Tissue homogenates and other biological fluids. (1elisakits.com)
  • Description: A sandwich ELISA kit for detection of Casein Kinase 1 Delta from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (1elisakits.com)
  • Kinases are deeply conserved in evolution, and the worm has family homologs for over 80% of the human kinome. (wormbook.org)
  • To put worm kinases into an evolutionary and functional context, we compared them with the distant kinomes of human, fly, and yeast. (wormbook.org)
  • Distribution of 212 kinase subfamilies throughout four kinomes: the yeast Saccharomyces cerevisiae , the nematode worm Caenorhabditis elegans , the fruit fly Drosophila melanogaster and human. (wormbook.org)
  • Nematodes share 153 subfamilies with human, providing close homologs for 81% (419/518) of all human kinases. (wormbook.org)
  • The new study highlights the molecules casein kinase 1δ (CK1δ) and CK1ε, which are essential for human ribosome assembly. (genengnews.com)
  • Section 2.1.1 For testing, 29 swimming pools of 8 TPATs encoding human being kinases were injected into the dorsal blastomeres of 2C4 cell stage BMPS embryos. (exposed-skin-care.net)
  • Casein Kinase-1𝛿 Delta is. (wpi.edu)
  • β-TrCP- and Casein Kinase II-Mediated Degradation of Cyclin F Controls Timely Mitotic Progression. (ox.ac.uk)
  • This chapter will introduce the diversity of kinases in C. elegans , and compare them to those of fungi and other metazoans, as well as to preliminary results from analysis of the C. briggsae kinome. (wormbook.org)
  • These buildings claim that the prolonged N-terminal portion fixes the activation portion and ?C helix the conformational plasticity which is certainly significant for on/off legislation of enzyme activity in CMGC kinases and thus allows CK2?1 to have constitutive activity. (immune-source.com)
  • A variety of approaches, including biochemical purification, gene isolation by homology, and genetic screens, have been successfully used for the identification of putative protein kinases and phosphatases. (rupress.org)
  • Protein kinases are one of the largest and most influential of gene families: constituting some 2% of the proteome, they regulate almost all biochemical pathways and may phosphorylate up to 30% of the proteome. (wormbook.org)
  • Regulation of casein kinase-2 (CK2) activity by inositol phosphates. (ox.ac.uk)
  • In the current study, we identified a protein kinase activity in rat liver supernatant that is up-regulated by inositol 1,3,4,5-tetrakisphosphate (IP4) and inositol hexakisphosphate (IP6). (ox.ac.uk)
  • 2013) A broad activity screen in support of a chemogenomic map for kinase signalling research and drug discovery. (guidetoimmunopharmacology.org)
  • This makes kinase signaling particularly amenable to comparative studies, and kinase activity a particularly good readout of the physiological state of any cell. (wormbook.org)
  • CK2 is a ubiquitous protein kinase involved in many cell functions. (nih.gov)
  • All sequences and supporting data are available at http://kinase.com , and all but 8 sequences are now identical to wormpep (v. 141) sequences. (wormbook.org)
  • Through extensive biochemical and genetic analysis, we now know that pathways are not simply switched on with kinases and off with phosphatases. (rupress.org)
  • Since kinases perform such a variety of distinct basic cellular functions, it is not surprising to see that 53 subfamilies and functions are present in all four kinomes ( Figure 1 ). (wormbook.org)
  • Sequencing of chymotryptic and thermolytic phosphopeptides from bovine DARPP-32 phosphorylated by casein kinase II suggested that the main phosphorylated residues were Ser45 and Ser102. (cornell.edu)
  • We also ran QM/MM simulations on casein-kinase 2 (CK2), where the ligand and a few surrounding residues were treated at the QM level, and the rest of the system at the MM level. (lu.se)
  • Almost half of the 438 worm kinases are members of worm-specific or worm-expanded families. (wormbook.org)
  • Although the importance of kinases in this process has long been recognized, an appreciation for the complex and fundamental role of phosphatases is more recent. (rupress.org)
  • Furthermore, kinases and phosphatases may work together to modulate the strength of a signal. (rupress.org)
  • Adding further complexity to this picture is the fact that both kinases and phosphatases can function in signaling networks where multiple kinases and phosphatases contribute to the outcome of a pathway. (rupress.org)