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.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
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.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
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 key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.
The phosphoric acid ester of serine.
An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.
A pyridoxal phosphate enzyme that catalyzes the reaction of glycine and 5,10-methylene-tetrahydrofolate to form serine. It also catalyzes the reaction of glycine with acetaldehyde to form L-threonine. EC 2.1.2.1.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Established cell cultures that have the potential to propagate indefinitely.
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.
Proteins prepared by recombinant DNA technology.
The rate dynamics in chemical or physical systems.
Serum serine proteases which participate in COMPLEMENT ACTIVATION. They are activated when complexed with the MANNOSE-BINDING LECTIN, therefore also known as Mannose-binding protein-Associated Serine Proteases (MASPs). They cleave COMPLEMENT C4 and COMPLEMENT C2 to form C4b2a, the CLASSICAL PATHWAY C3 CONVERTASE.
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
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.
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.
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 enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
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.
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.
A PYRIDOXAL-phosphate containing enzyme that catalyzes the dehydration and deamination of L-serine to form pyruvate. This enzyme was formerly listed as EC 4.2.1.13.
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 di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
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)
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
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.
An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.
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 protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
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.
The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
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.
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.
Amino acids that contain phosphorus as an integral part of the molecule.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
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)
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.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
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 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.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The sum of the weight of all the atoms in a molecule.
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.
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
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.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
The process of cleaving a chemical compound by the addition of a molecule of water.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62.
An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.
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.
Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).
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.
Physiologically inactive substances that can be converted to active enzymes.
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 transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.
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.
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.
Peptides and proteins found in BODILY SECRETIONS and BODY FLUIDS that are PROTEASE INHIBITORS. They play a role in INFLAMMATION, tissue repair and innate immunity (IMMUNITY, INNATE) by inhibiting endogenous proteinases such as those produced by LEUKOCYTES and exogenous proteases such as those produced by invading microorganisms.
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.
A large family of signal-transducing adaptor proteins present in wide variety of eukaryotes. They are PHOSPHOSERINE and PHOSPHOTHREONINE binding proteins involved in important cellular processes including SIGNAL TRANSDUCTION; CELL CYCLE control; APOPTOSIS; and cellular stress responses. 14-3-3 proteins function by interacting with other signal-transducing proteins and effecting changes in their enzymatic activity and subcellular localization. The name 14-3-3 derives from numerical designations used in the original fractionation patterns of the proteins.
Proteins found in any species of bacterium.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
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.
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.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
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.
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.
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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)
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.
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 lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
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).
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
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 mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
A ubiquitously expressed raf kinase subclass that plays an important role in SIGNAL TRANSDUCTION. The c-raf Kinases are MAP kinase kinase kinases that have specificity for MAP KINASE KINASE 1 and MAP KINASE KINASE 2.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.
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.
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)
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
Serine-threonine protein kinases that relay signals from CYTOKINE RECEPTORS and are involved in control of CELL GROWTH PROCESSES; CELL DIFFERENTIATION; and APOPTOSIS.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
A viscous, hygroscopic amino alcohol with an ammoniacal odor. It is widely distributed in biological tissue and is a component of lecithin. It is used as a surfactant, fluorimetric reagent, and to remove CO2 and H2S from natural gas and other gases.
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
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.
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.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Antibodies directed against immunogen-coupled phosphorylated PEPTIDES corresponding to amino acids surrounding the PHOSPHORYLATION site. They are used to study proteins involved in SIGNAL TRANSDUCTION pathways. (From Methods Mol Biol 2000; 99:177-89)
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
An inhibitor of SERINE ENDOPEPTIDASES. Acts as an alkylating agent and is known to interfere with the translation process.
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.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
A cell line derived from cultured tumor cells.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.
Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.
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.
An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.
Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.
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.
A family of serine endopeptidases found in the SECRETORY GRANULES of LEUKOCYTES such as CYTOTOXIC T-LYMPHOCYTES and NATURAL KILLER CELLS. When secreted into the intercellular space granzymes act to eliminate transformed and virus-infected host cells.
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.
Elements of limited time intervals, contributing to particular results or situations.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Peptides composed of between two and twelve amino acids.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
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)
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
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).
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.
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.
Compounds of the general formula R-O-R arranged in a ring or crown formation.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.
An essential amino acid that is required for the production of HISTAMINE.
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.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
An inhibitor of Serine Endopeptidases. Acts as alkylating agent and is known to interfere with the translation process.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A family of neutral serine proteases with CHYMOTRYPSIN-like activity. Chymases are primarily found in the SECRETORY GRANULES of MAST CELLS and are released during mast cell degranulation.
Proteins found in the PERIPLASM of organisms with cell walls.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
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 77-kDa subcomponent of complement C1, encoded by gene C1S, is a SERINE PROTEASE existing as a proenzyme (homodimer) in the intact complement C1 complex. Upon the binding of COMPLEMENT C1Q to antibodies, the activated COMPLEMENT C1R cleaves C1s into two chains, A (heavy) and B (light, the serine protease), linked by disulfide bonds yielding the active C1s. The activated C1s, in turn, cleaves COMPLEMENT C2 and COMPLEMENT C4 to form C4b2a (CLASSICAL C3 CONVERTASE).
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
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.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.
An oligopeptide produced by various bacteria which acts as a protease inhibitor.
An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.
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.
A protease nexin and serpin subtype that is specific for several SERINE PROTEASES including UROKINASE; THROMBIN; TRYPSIN; and PLASMINOGEN ACTIVATORS.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
A sulfur-containing essential L-amino acid that is important in many body functions.
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 enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.
The relationship between the dose of an administered drug and the response of the organism to the drug.
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 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)
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.
An essential amino acid. It is often added to animal feed.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
Compounds based on 5,6,7,8-tetrahydrofolate.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
A G-protein-coupled, proteinase-activated receptor that is expressed in a variety of tissues including ENDOTHELIUM; LEUKOCYTES; and the GASTROINTESTINAL TRACT. The receptor is activated by TRYPSIN, which cleaves off the N-terminal peptide from the receptor. The new N-terminal peptide is a cryptic ligand for the receptor. The uncleaved receptor can also be activated by the N-terminal peptide present on the activated THROMBIN RECEPTOR and by small synthetic peptides that contain the unmasked N-terminal sequence.

Differential roles for cyclin-dependent kinase inhibitors p21 and p16 in the mechanisms of senescence and differentiation in human fibroblasts. (1/8537)

The irreversible G1 arrest in senescent human diploid fibroblasts is probably caused by inactivation of the G1 cyclin-cyclin-dependent kinase (Cdk) complexes responsible for phosphorylation of the retinoblastoma protein (pRb). We show that the Cdk inhibitor p21(Sdi1,Cip1,Waf1), which accumulates progressively in aging cells, binds to and inactivates all cyclin E-Cdk2 complexes in senescent cells, whereas in young cells only p21-free Cdk2 complexes are active. Furthermore, the senescent-cell-cycle arrest occurs prior to the accumulation of the Cdk4-Cdk6 inhibitor p16(Ink4a), suggesting that p21 may be sufficient for this event. Accordingly, cyclin D1-associated phosphorylation of pRb at Ser-780 is lacking even in newly senescent fibroblasts that have a low amount of p16. Instead, the cyclin D1-Cdk4 and cyclin D1-Cdk6 complexes in these cells are associated with an increased amount of p21, suggesting that p21 may be responsible for inactivation of both cyclin E- and cyclin D1-associated kinase activity at the early stage of senescence. Moreover, even in the late stage of senescence when p16 is high, cyclin D1-Cdk4 complexes are persistent, albeit reduced by +info)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (2/8537)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.  (+info)

AMP-activated protein kinase phosphorylation of endothelial NO synthase. (3/8537)

The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function.  (+info)

Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteins. (4/8537)

Integrin ligand binding induces a signaling complex formation via the direct association of the docking protein p130(Cas) (Cas) with diverse molecules. We report here that the 14-3-3zeta protein interacts with Cas in the yeast two-hybrid assay. We also found that the two proteins associate in mammalian cells and that this interaction takes place in a phosphoserine-dependent manner, because treatment of Cas with a serine phosphatase greatly reduced its ability to bind 14-3-3zeta. Furthermore, the Cas-14-3-3zeta interaction was found to be regulated by integrin-mediated cell adhesion. Thus, when cells are detached from the extracellular matrix, the binding of Cas to 14-3-3zeta is greatly diminished, whereas replating the cells onto fibronectin rapidly induces the association. Consistent with these results, we found that the subcellular localization of Cas and 14-3-3 is also regulated by integrin ligand binding and that the two proteins display a significant co-localization during cell attachment to the extracellular matrix. In conclusion, our results demonstrate that 14-3-3 proteins participate in integrin-activated signaling pathways through their interaction with Cas, which, in turn, may contribute to important biological responses regulated by cell adhesion to the extracellular matrix.  (+info)

Haloanaerobacter salinarius sp. nov., a novel halophilic fermentative bacterium that reduces glycine-betaine to trimethylamine with hydrogen or serine as electron donors; emendation of the genus Haloanaerobacter. (5/8537)

A novel halophilic fermentative bacterium has been isolated from the black sediment below a gypsum crust and a microbial mat in hypersaline ponds of Mediterranean salterns. Morphologically, physiologically and genetically this organism belongs to the genus Haloanaerobacter. Haloanaerobacter strain SG 3903T (T = type strain) is composed of non-sporulating long flexible rods with peritrichous flagella, able to grow in the salinity range of 5-30% NaCl, with an optimum at 14-15%. The strain grows by fermenting carbohydrates or by using the Stickland reaction with either serine or H2 as electron donors and glycine-betaine as acceptor, which is reduced to trimethylamine. The two species described so far in the genus Haloanaerobacter are not capable of Stickland reaction with glycine-betaine + serine; however, Haloanaerobacter chitinovorans can use glycine-betaine with H2 as electron donor. Strain SG 3903T thus represents the first described strain in the genus Haloanaerobacter capable of the Stickland reaction with two amino acids. Although strain SG 3903T showed 67% DNA-DNA relatedness to H. chitinovorans, it is physiologically sufficiently different from the two described species to be considered as a new species which has been named Haloanaerobacter salinarius sp. nov.  (+info)

Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation. (6/8537)

We recently reported that APOE promoter activity is stimulated by cAMP, this effect being mediated by factor AP-2 [Garcia et al. (1996) J. Neurosci. 16, 7550-7556]. Here, we study whether cAMP-induced phosphorylation modulates the activity of AP-2. Recombinant AP-2 was phosphorylated in vitro by protein kinase A (PKA) at Ser239. Mutation of Ser239 to Ala abolished in vitro phosphorylation of AP-2 by PKA, but not the DNA binding activity of AP-2. Cotransfection studies showed that PKA stimulated the effect of AP-2 on the APOE promoter, but not that of the S239A mutant. Therefore, cAMP may modulate AP-2 activity by PKA-induced phosphorylation of this factor.  (+info)

Structure-function studies of Ser-289 in the class C beta-lactamase from Enterobacter cloacae P99. (7/8537)

Site-directed mutagenesis of Ser-289 of the class C beta-lactamase from Enterobacter cloacae P99 was performed to investigate the role of this residue in beta-lactam hydrolysis. This amino acid lies near the active site of the enzyme, where it can interact with the C-3 substituent of cephalosporins. Kinetic analysis of six mutant beta-lactamases with five cephalosporins showed that Ser-289 can be substituted by amino acids with nonpolar or polar uncharged side chains without altering the catalytic efficiency of the enzyme. These data suggest that Ser-289 is not essential in the binding or hydrolytic mechanism of AmpC beta-lactamase. However, replacement by Lys or Arg decreased by two- to threefold the kcat of four of the five beta-lactams tested, particularly cefoperazone, cephaloridine, and cephalothin. Three-dimensional models of the mutant beta-lactamases revealed that the length and positive charge of the side chain of Lys and Arg could create an electrostatic linkage to the C-4 carboxylic acid group of the dihydrothiazine ring of the acyl intermediate which could slow the deacylation step or hinder release of the product.  (+info)

The nucleoprotein of Marburg virus is target for multiple cellular kinases. (8/8537)

The nucleoprotein (NP) of Marburg virus is phosphorylated at serine and threonine residues in a ratio of 85:15, regardless of whether the protein is isolated from virions or from eukaryotic expression systems. Phosphotyrosine is absent. Although many potential phosphorylation sites are located in the N-terminal half of NP, this part of the protein is not phosphorylated. Analyses of phosphorylation state and phosphoamino acid content of truncated NPs expressed in HeLa cells using the vaccinia virus T7 expression system led to the identification of seven phosphorylated regions (region I*, amino acids 404-432; II*, amino acids 446-472; III*, amino acids 484-511; IV*, amino acids 534-543; V*, amino acid 549; VI*, amino acids 599-604; and VII*, amino acid 619) with a minimum of seven phosphorylated amino acid residues located in the C-terminal half of NP. All phosphothreonine residues and consensus recognition sequences for protein kinase CKII are located in regions I*-V*. Regions VI* and VII* contain only phosphoserine with three of four serine residues in consensus recognition motifs for proline-directed protein kinases. Mutagenesis of proline-adjacent serine residues to alanine or aspartic acid did not influence the function of NP in a reconstituted transcription/replication system; thus it is concluded that serine phosphorylation in the most C-terminal part of NP is not a regulatory factor in viral RNA synthesis.  (+info)

This Research Topic addresses the metabolism and function of the amino acid Serine in plants. We emphasize the interaction and coordination between the Serine biosynthetic pathways and other metabolic pathways.Serine is a polar amino acid that plays a fundamental role in plant metabolism, plant development, and cell signalling. In addition to being a building block for proteins, Serine participates in the biosynthesis of biomolecules such as amino acids, nucleotides, phospholipids, and sphingolipids. Plants possess at least two serine biosynthetic pathways: i) the glycolate pathway associated with photorespiration and ii) the so-called Phosphorylated Pathway of Serine Biosynthesis. The biological significance of the coexistence of several pathways for the biosynthesis of Serine is not known. In particular, we poorly understand the contribution that each pathway makes to plant serine homeostasis, how pathways are integrated and coordinated, and how they interact at the transcriptional/translational
We examined the sites of phosphorylation and the role that phosphorylation plays in the function of the M2-1 protein in transcription and interaction with viral RNA. The M2-1 protein was found by proteolytic digestion and site-directed mutagenesis to be phosphorylated at serine 58 and serine 61. Serines 58 and 61 lie in the consensus sequence for phosphorylation by CKI and are conserved in human, bovine, and ovine RS virus and in turkey rhinotracheitis virus (1, 8, 26, 29, 35, 37). The conservation of these residues suggests a functional role for M2-1 phosphorylation. Phosphorylation of serine 58 creates a new CKI site at serine 61. The disruption of serine 58 should prevent phosphorylation at serine 61, which would result in the loss of both phosphorylation sites, which is consistent with our results. Based on sequence analysis, mutation at serine 61 would be expected to affect phosphorylation at only that site and not at serine 58, explaining why the S61A mutant retains 33P incorporation. The ...
BioAssay record AID 1299281 submitted by ChEMBL: Induction of p53 phosphorylation at serine-15 in human p53 +/+ HCT 116 cells bat 5 or 10 uM after 24 hrs by western blot analysis.
TY - JOUR. T1 - An Akt3 splice variant lacking the serine 472 phosphorylation site promotes apoptosis and suppresses mammary tumorigenesis. AU - Suyama, Kimita. AU - Yao, Jiahong. AU - Liang, Huizhi. AU - Benard, Outhiriaradjou. AU - Loudig, Olivier D.. AU - Amgalan, Dulguun. AU - McKimpson, Wendy M.. AU - Phillips, Greg R.. AU - Segall, Jeffrey E.. AU - Wang, Yihong. AU - Fineberg, Susan A.. AU - Norton, Larry. AU - Kitsis, Richard N.. AU - Hazan, Rachel. PY - 2018/1/1. Y1 - 2018/1/1. N2 - The Akt pathway is a well-known promoter of tumormalignancy. Akt3 is expressed as two alternatively spliced variants, one of which lacks the key regulatory serine 472 phosphorylation site. Whereas the function of full-length Akt3 isoform (Akt3/+S472) is well-characterized, that of Akt3/S472 isoformremains unknown. Despite being expressed at a substantially lower level than Akt3/ +S472 in triple-negative breast cancer cells, specific ablation of Akt3/S472 enhanced, whereas overexpression, suppressed mammary ...
The IKK complex, isolated from extracts of HeLa cells treated with the proinflammatory cytokine TNF (tumor necrosis factor), phosphorylates two regulatory serine residues at the NH2-termini of the NF-κB inhibitors IκBα and IκBβ (1). This phosphorylation event triggers the polyubiquitination of IκBs followed by their degradation through the 26S proteasome, and thereby leads to NF-κB activation (2). IKK is a large, 900-kD, protein complex that is composed of multiple subunits. Two of these subunits, IKKα and IKKβ, are serine kinases (1, 3-6). Epitope-tagged IKKα and IKKβ, when produced by cell-free translation in reticulocyte lysates or by transient transfection of mammalian cells, are incorporated into the IKK complex, which can be isolated by immunoprecipitation of either IKKα or IKKβ (1, 4). The IκB kinase activity of the entire complex is rapidly stimulated by TNF or interleukin 1 (IL-1), with kinetics matching those of IκBα phosphorylation and degradation (1,4).. Because ...
Serine definition, definition of serine, Anagrams of serine, words that start with Serine, and words that can be created from serine
BioAssay record AID 493218 submitted by NCGC: Immunofluorescence assay for KAP-1 phosphorylation on Ser824 for Identifying a Potential Treatment of Ataxia-Telangiectasia: Hit Validation.
There might be another problem with the scoring function, along the same lines as the issue with design puzzles favoring the large aromatic side chains.. From what Ive read, serine is considered a structure-breaking amino acids and does not normally show up in sheets or helices. So, if serine doesnt belong in a beta sheet in nature, I wouldnt expect the mutate function to be substituting it into beta sheets very often. However, Ive noticed that in freestyle design Im often getting serine in my beta sheets. If it were just one or two, that would be realistic, but Im looking at a ten-segment beta strand with four serines, and in one case recently I had a sheet that was almost entirely serines. That cant be right.. ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Where to buy Serine? Green Stone offers Serine sales,Serine prices.Molecular Formula:C3H7NO3CAS No.: 56-45-1Molar mass:105.09 g mol?1Product Description: Serine (abbreviated as Ser or S)is an organic compound with the formula HO2CCH(NH2)CH2OH.Applications:
Press Release issued Jul 19, 2017: The purpose of Global Serine Market report is to provide the newest industry data and Serine industry future trends, allowing consumers to identify the Serine market Application, Type, Manufacturers and Regions, Serine market Forecast up to 2022.
The observations that UCN-01 blocked the stabilization and phosphorylation of p53 on serine 20, whereas serine 15 remained phosphorylated, are in agreement with a previous report showing that phosphorylation on serine 20 rather than serine 15 contributes to p53 stabilization (20) , which suggests that UCN-01 blocks IR-induced p53 stabilization, most likely by inhibiting Chk2 kinase. Consistent with this notion, we found that UCN-01 effectively inhibited the immunoprecipitated kinase activity of endogenous Chk2 from HCT116 cells (IC50, ∼10 nm; Fig. 2B ⇓ ). UCN-01 has been shown previously to inhibit recombinant Chk1 rather than recombinant Chk2 kinases as determined by in vitro biochemical assays (24 , 25) . It is not likely that the inhibition of immunoprecipitated Chk2 is caused by the unspecific immunoprecipitation because Chk2 antibody obtained from another source gave a similar result. 3 Furthermore, this kinase would have to be active on GST-Cdc25C and to be sensitive to UCN-01. The ...
Paleologou, K. E.; Oueslati, A.; Shakked, G.; Rospigliosi, C. C.; Kim, H. Y.; Lamberto, G. R.; Fernandez, C. O.; Schmid, A.; Chegini, F.; Gai, W. P. et al.; Chiappe, D.; Moniatte, M.; Schneider, B. L.; Aebischer, P.; Eliezer, D.; Zweckstetter, M.; Masliah, E.; Lashuel, H. A.: Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization and influences synuclein-membrane interactions. Journal of Neuroscience 30 (9), pp. 3184 - 3198 (2010 ...
Paleologou, K. E.; Oueslati, A.; Shakked, G.; Rospigliosi, C. C.; Kim, H. Y.; Lamberto, G. R.; Fernandez, C. O.; Schmid, A.; Chegini, F.; Gai, W. P. et al.; Chiappe, D.; Moniatte, M.; Schneider, B. L.; Aebischer, P.; Eliezer, D.; Zweckstetter, M.; Masliah, E.; Lashuel, H. A.: Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization and influences synuclein-membrane interactions. Journal of Neuroscience 30 (9), pp. 3184 - 3198 (2010 ...
Phosphatidyl L Serine is an important chemical with widespread functions in the body It is part of the cell structure and is key in the maintenance of cellular function, especially in the brain
Immunohistochemical (IHC) staining for pS6 (serine 235/236 and serine 240/244) and PTEN was performed just before and during the everolimus re-treatment. All ph
A scientific resource for the WD40 protein domain containing information on structure, function, and binding to both phospho-Ser/Thr and methylated lysine residues.
Function: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing ...
دانلود مقالات isi انگلیسی درباره پرویناین serine با ترجمه فارسی - مقالات الزویر ساینس دایرکت Science Direct
5 Phosphorylation is needed if an oligo is used as a substrate for DNA ligase. 3 Phosphorylation will inhibit degradation by some 3-exonucleases and can be used to block extension by DNA polymerases.. View product details for Phosphorylation:. ...
MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQI 1 - 70 MKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVH 71 - 140 RDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVL 141 - 210 VCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWMLIEVPVQRP 211 - 280 VLYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRL 281 - 350 DGRQRRPSTIAEQTVAKAQTVGLPVTMHSPNMRLLRSALLPQASNVEAFSFPASGCQAEAAFMEEECVDT 351 - 420 PKVNGCLLDPVPPVLVRKGCQSLPSNMMETSIDEGLETEGEAEEDPAHAFEAFQSTRSGQRRHTLSEVTN 421 - 490 QLVVMPGAGKIFSMNDSPSLDSVDSEYDMGSVQRDLNFLEDNPSLKDIMLANQPSPRMTSPFISLRPTNP 491 - 560 AMQALSSQKREVHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQIGPEADP 561 - 630 NLAPAAPQLQDLASSCPQEEVSQQQESVSTLPASVHPQLSPRQSLETQYLQHRLQKPSLLSKAQNTCQLY 631 - 700 CKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPQPSQQLPLPRQETPPPSQQAPPFSL 701 - 770 TQPLSPVLEPSSEQMQYSPFLSQYQEMQLQPLPSTSGPRAAPPLPTQLQQQQPPPPPPPPPPRQPGAAPA 771 - 840 ...
TY - JOUR. T1 - Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate. T2 - Effects on enzyme stability and activity. AU - Royo, Montserrat. AU - Fitzpatrick, Paul F.. AU - Daubner, S. Colette. PY - 2005/2/15. Y1 - 2005/2/15. N2 - Tyrosine hydroxylase is phosphorylated at four serine residues in its amino-terminus by multiple kinases. Phosphorylation of serine 40 by cAMP-dependent protein kinase results in alleviation of dopamine inhibition [J. Biol. Chem. 267 (1992) 12639]. The other serines are at positions 8, 19, and 31. The effect of phosphorylation at these serines has been investigated using mutated forms of tyrosine hydroxylase containing glutamates at the positions of the serines. The S8E, S19E, and S31E tyrosine hydroxylase variants have similar steady-state kinetic parameters and similar binding affinity for catecholamines to wild-type enzyme. The S8E, S19E, S31E, and S40E variants differ in stability at elevated temperatures. The S40E variant is the least stable, ...
As discussed earlier, cells can acquire serine by either synthesizing it internally or importing serine from the environment. Serine is a small, neutral amino acid and, as such, can be transported by one of three systems. Two of the systems are sodium dependent: the alanine/serine/cysteine/threonine transporters ASCT1 and ASCT2 (encoded by SLC1A4 and SLC1A5, respectively) and the system A transporters SAT1 and SAT2 (encoded by SLC38A1 and SLC38A2, respectively). The third is a family of neutral amino acid antiporters, the alanine/serine/cysteine transporter (ASC) system (El-Hattab, 2016). These antiporters are of particular interest because they are active even at steady state, so that for instance, one molecule of intracellular serine can be exchanged for one molecule of extracellular serine. Normally this process goes unnoticed, but a recent study (DeNicola et al., 2015) points out that it can complicate interpretation of heavy isotope-labeling experiments by setting up an exchange flux ...
Visconti R., Gadina M., Chiariello M., Chen E.H., Stancato L.F., Gutkind J.S., OShea J.J.. Interleukin-12 (IL-12) is a key immunoregulatory cytokine that promotes Th1 differentiation and cell-mediated immune responses. The transcription factor STAT4 (signal transducer and activator of transcription 4) is an important element in mediating IL-12 signals, as evidenced by the fact that STAT4(-/-) mice display impaired responsiveness to IL-12 and deficient Th1 differentiation. STAT4 is inducibly phosphorylated on tyrosine and serine in response to IL-12, but the kinase(s) responsible for the latter event is unknown. Here we show that IL-12 induces STAT4 phosphorylation on serine 721 and that mutation of serine 721 interferes with STAT4 transcriptional activity. In addition, we show that mutation of tyrosine 693 abrogates IL-12-induced STAT4 tyrosine phosphorylation and transcriptional activity. Although the site surrounding serine 721 is an optimum consensus sequence for mitogen-activated family of ...
TrendTerms displays relevant terms of the abstract of this publication and related documents on a map. The terms and their relations were extracted from ZORA using word statistics. Their timelines are taken from ZORA as well. The bubble size of a term is proportional to the number of documents where the term occurs. Red, orange, yellow and green colors are used for terms that occur in the current document; red indicates high interlinkedness of a term with other terms, orange, yellow and green decreasing interlinkedness. Blue is used for terms that have a relation with the terms in this document, but occur in other documents ...
PKA phosphorylation increases the tyrosine kinase activity of Csk towards an endogenous substrate. Tyrosine phosphorylation of heat-inactivated (65°C for 10 mi
FLCN interacts with AMPK via FNIP1 and/or FNIP2, and regulates mTOR signalling (Baba et al., 2006; Hasumi et al., 2008, Takagi et al., 2008). Phosphorylation at S62 of FLCN increases the FLCN-FNIP complexs affinity for AMPK, while phosphorylation at S302 decreases FLCNs affinity for AMPK (Piao et al., 2009, Wang et al., 2010). AMPK is an important energy sensing protein, which inhibits anabolic growth via mTOR signalling and stimulates autophagy to promote cell survival when energy supply is low (Alers et al., 2012).. Loss of FLCN in mouse embryonic fibroblasts (MEFs), leads to the constitutive activation of AMPK (Yan et al., 2014). This ultimately activates HIF signalling and leads to metabolic changes consistent with the Warburg Effect within FLCN-null cells. A nonphosphorylatable FLCN S62A mutant was unable to bind and inhibit AMPK, meaning that FLCN-FNIP binding to AMPK is required for its inhibition.. Possik et al., (2014) also found that deletion of flcn-1 in nematode worms leads to ...
Combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + pro…
The structure of the Mg(2+)-dependent enzyme human phosphoserine phosphatase (HPSP) was exploited to examine the structural and functional role of the divalent cation in the active site of phosphatases. Most interesting is the biochemical observation that a Ca(2+) ion inhibits the activity of HPSP, even in the presence of added Mg(2+). The sixfold coordinated Mg(2+) ion present in the active site of HPSP under normal physiological conditions, was replaced by a Ca(2+) ion by using a crystallization condition with high concentration of CaCl(2) (0.7 m). The resulting HPSP structure now shows a sevenfold coordinated Ca(2+) ion in the active site that might explain the inhibitory effect of Ca(2+) on the enzyme. Indeed, the Ca(2+) ion in the active site captures both side-chain oxygen atoms of the catalytic Asp20 as a ligand, while a Mg(2+) ion ligates only one oxygen atom of this Asp residue. The bidentate character of Asp20 towards Ca(2+) hampers the nucleophilic attack of one of the Asp20 side ...
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Cyclin-afhængig kinase 1 (Cdk1) er aktiveret i G2 fase af cellecyklus og regulerer mange cellulære veje. Her præsenterer vi en protokol ...
Clone REA134 recognizes AKT1, which is also known as protein kinase Bα. AKT1 is a serine/threonine protein kinase, belonging to the AKT family of kinases and like each AKT family member, contains an N-terminal pleckstrin homology (PH) domain, a central kinase domain, and a carboxyl-terminal regulatory domain with a hydrophobic motif (HM). Activation of AKT1 is achieved via phosphorylation at multiple sites, which take place in response to engagement of receptors such as platelet derived growth factor receptor (PDGF-R). Activated AKT1 further phosphorylates and alters the activity of several downstream substrates allowing AKT1 to play a vital role in various biological processes such as cell growth, survival, migration, and proliferation. Additional information: Clone REA134 displays negligible binding to Fc receptors. - Belgique
 종속 키 1 (Cdk1) 세포 주기의 g 2 단계에서 활성화 되 고 많은 세포 경로 조절. 여기, Cdk1, Cdk1-특정 한 인 산화 위치의 식별이 중요 한 키의 셀룰러 목표 설정에 대 한 수와 함께 체 외에 니 분석...
A large body of work has implicated the activity of various kinases and phosphatases in the regulation of synaptic transmission by controlling the phosphorylation state of several synaptic proteins (for review, see Turner et al., 1999). To further understand the physiological significance of these modifications and to gain insights into their role in modulating synaptic strength and plasticity, we have generated a set of antibodies that specifically recognize synaptic proteins only in their phosphorylated form. In this study we report the biochemical characterization of the modulation of phosphorylation of rabphilin, a synaptic protein implicated in exocytosis, using phosphospecific antibodies directed against the two major phosphorylation sites of rabphilin, serine-234 and serine-274.. Our results show that the phosphorylation of rabphilin at serine-234 is greatly stimulated (about sevenfold over basal) by activation of PKA and high K+-induced membrane depolarization, a condition that mimics ...
Detail záznamu - Inhibition of Human Serine Racemase, an Emerging Target for Medicinal Chemistry - Detail záznamu - Knihovna Akademie věd České republiky
Proteins of the Bcl-2 family are important regulators of cell death in mammalian cells (1). BAD, a distant member of the Bcl-2 family, promotes cell death at least in part through heterodimerization with the survival proteins Bcl-2 and Bcl-xL (2). BAD resides in the cytosol and is phosphorylated on serine residues after cells are stimulated with IL-3 (3). Phosphorylation of BAD results in its cytosolic sequestration by the tau form of 14-3-3 proteins and its inactivation, as the phosphorylated form has reduced ability to bind to membrane Bcl-xL (3).. The survival of cells in multicellular organisms requires continuous stimulation from the extracellular enviroment. Certain growth factors maintain cell survival during embryonal and postnatal development (4). The intracellular signaling pathways by which growth factors promote survival are poorly understood. PI 3-kinase is recruited and activated during the intracellular signal transduction of many receptors and has been implicated in the signaling ...
TY - JOUR. T1 - EGFRvIII stimulates glioma growth and invasion through PKA-dependent serine phosphorylation of Dock180. AU - Feng, H.. AU - Hu, B.. AU - Vuori, K.. AU - Sarkaria, J. N.. AU - Furnari, F. B.. AU - Cavenee, W. K.. AU - Cheng, S. Y.. N1 - Funding Information: Most of the studies (and all the animal studies) were performed at the University of Pittsburgh in accordance with a protocol approved by the IACUC of the University of Pittsburgh. We acknowledge the support of University of Pittsburgh Cancer Institute and various core facilities. We also thank M Matsuda, R Tsien, E van Meir and Y Zhou for providing reagents, and Angel Alvarez for proofreading of this manuscript. WK Cavenee is a Fellow of the National Foundation for Cancer Research. This work was supported in part by a NIH grant CA130966, CA158911 to S-Y Cheng, a Zell Scholar Award from the Zell Family Foundation and funds from Northwestern Brain Tumor Institute and Department of Neurology at Northwestern University Feinberg ...
Concepts regarding the controls and consequences of PKD1-Ser738/Ser742 (activation loop) phosphorylation are based largely on early studies that used an anti-PKD1-Ser(P)738/Ser(P)742 PSSA (from Cell Signaling Technology, Danvers, MA) and showed that PMA increases PKD1 activation loop phosphorylation in many cell types via a mechanism that requires nPKC isoform activity (PKCδ, PKCε, PKCη, and/or PKCθ). In vitro kinase assays showing direct phosphorylation of the PKD1 activation loop by certain nPKC isoforms also have been published (Brändlin et al., 2002). However, there is recent evidence that the Cell Signaling Technology anti-PKD1-Ser(P)738/Ser(P)742 PSSA primarily recognizes PKD1 phosphorylation at Ser738 and that PKD1 phosphorylation at Ser742 can be tracked with a different PSSA (commercially available from Abcam Inc., Cambridge, MA). Experiments that use a combined approach with these two PSSAs expose differences in the controls and consequences of PKD1 phosphorylation at Ser738 and ...
A large body of work has implicated the activity of various kinases and phosphatases in the regulation of synaptic transmission by controlling the phosphorylation state of several synaptic proteins (for review, see Turner et al., 1999). To further understand the physiological significance of these modifications and to gain insights into their role in modulating synaptic strength and plasticity, we have generated a set of antibodies that specifically recognize synaptic proteins only in their phosphorylated form. In this study we report the biochemical characterization of the modulation of phosphorylation of rabphilin, a synaptic protein implicated in exocytosis, using phosphospecific antibodies directed against the two major phosphorylation sites of rabphilin, serine-234 and serine-274.. Our results show that the phosphorylation of rabphilin at serine-234 is greatly stimulated (about sevenfold over basal) by activation of PKA and high K+-induced membrane depolarization, a condition that mimics ...
Interestingly, recent in vitro kinetic studies using recombinant active p38α expressed in Escherichia coli showed that p38 phosphorylates GST-ATF2 (amino acids 1-115) via a two‐step (double collision) mechanism, involving the dissociation of mono‐phosphorylated ATF2 Thr71 or Thr69 from the enzyme after the first phosphorylation step (Waas et al., 2001). Moreover, these authors found that mono‐phosphorylation of ATF2 Thr69 strongly reduces the phosphorylation rate of Thr71, whereas, in contrast, mono‐phosphorylation of Thr71 does not reduce the rate of Thr69 phosphorylation. Thus, efficient phosphorylation of ATF2 by recombinant E.coli‐expressed active p38 only occurs in the order Thr71→ Thr69 + 71 (Figure 7). This order of events also seems to occur in mitogen‐treated cells, as ERK, in contrast to p38, does not seem to mono‐phosphorylate Thr69 significantly (Figure 4C).. The fact that ERK does not double‐phosphorylate ATF2 Thr69 + 71 efficiently raises the question as to ...
We have shown that the inhibitory phosphorylation of the WNK/SPAK-regulated Thr906/Thr1007 motif in KCC2 is substantially reduced during the course of CNS development. Second, regulated KCC2 Thr906/Thr1007 phosphorylation is essential for mouse survival; antagonizing the normal developmental down-regulation of KCC2 Thr906/Thr1007 via homozygous phospho-mimetic mutagenesis of these sites causes respiratory arrest and early postnatal death. Third, corroborating and extending previous in vitro findings (24, 26), phospho-mimetic mutation of Thr906/Thr1007 in vivo prevents KCC2 from dynamically increasing its Cl− extrusion capacity (such as in response to a Cl− load). This results in an imbalance of neuronal excitation and inhibition that leads to impaired rhythmogenesis in respiratory and locomotor networks accompanied by profound neuronal hyperexcitability manifesting as touch-evoked generalized seizures. Fourth, Kcc2E/E mice exhibit anomalous neuronal distribution with normal dendritic spine ...
以下に掲載:Cancer Science 105 pp.1307-1312 2014. Japanese Cancer Association 共著者:Eiichi Kato, Makoto Orisaka, Tetsuji Kurokaw
Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. These reactions require the presence of calcium-bound calmodulin ...
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reacts with Akt when phosphorylated at Ser473; also reacts with Akt2 and Akt3 when phosphorylated at corresponding residues. Does not recognize Akt phosphorylated at other sites, nor does it recognize phosphorylated forms of related kinases such as PKC or p70 S6 ...
Serine exists as a zwitterion. In very acidic solutions (pH 1), the COO⁻ group will be protonated The pK_a values are: COOH = 2.2 NH₃⁺ = 9.2 As you make the solution more basic, you will remove the acidic protons one by one. By the time you reach pH 12, you will have removed all of the acidic protons. Serine will exist as NH₂CH(CH₂OH)COO⁻.
Serine Ser, S 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. Name L-Serine MeSH 68012694 CAS No.56-45-1Molecular Formula
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; THR-301; SER-394; SER-397; SER-402; THR-404; THR-449; SER-453; THR-455; SER-495; SER-498; SER-513; SER-780; SER-793; SER-1033; SER-1068; THR-1198; SER-1399; SER-1400; THR-1403; THR-1425; THR-1466; THR-1548; THR-1589; SER-1604; THR-1630; THR-1664; THR-1671; SER-1681; THR-1697; SER-1702; SER-1711; SER-1775 AND THR-1858; VARIANT [LARGE SCALE ANALYSIS] PRO-1540; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; ...
Furthermore, considering that at the N-terminus, the K13 SUMO/ acetylation site is adjacent to the S10 O-GlcNAcylation/phosphorylation website we will further
201 Page 210 202 D. 3 KID domain from CREB, phosphorylated on Ser133 Snovitra xl 60 mg in a complex with the KIX domain of CBP. AlвBadr were applied successfully for the determination of miconazole and the other anti- fungal drug in their pharmaceutical formulation. The snovitra and ventricular electrograms are on top and the s novitra markers at snovtira bottom.
Could the Glycine/Serine ratio could tell us anything about whether a person is over/undermethlyated? I dont think it could be used all by itself, but...
MSDSLWTALSNFSMPSFPGGSMFRRTKSCRTSNRKSLILTSTSPTLPRPHSPLPGHLGSSPLDSPRNFSP 1 - 70 NTPAHFSFASSRRADGRRWSLASLPSSGYGTNTPSSTVSSSCSSQERLHQLPYQPTVDELHFLSKHFGST 71 - 140 ESITDEDGGRRSPAVRPRSRSLSPGRSPSSYDNEIVMMNHVYKERFPKATAQMEEKLRDFTRAYEPDSVL 141 - 210 PLADGVLSFIHHQIIELARDCLTKSRDGLITTVYFYELQENLEKLLQDAYERSESLEVAFVTQLVKKLLI 211 - 280 IISRPARLLECLEFNPEEFYHLLEAAEGHAKEGHLVKTDIPRYIIRQLGLTRDPFPDVVHLEEQDSGGSN 281 - 350 TPEQDDLSEGRSSKAKKPPGENDFDTIKLISNGAYGAVYLVRHRDTRQRFAMKKINKQNLILRNQIQQAF 351 - 420 VERDILTFAENPFVVGMFCSFETRRHLCMVMEYVEGGDCATLLKNIGALPVEMARMYFAETVLALEYLHN 421 - 490 YGIVHRDLKPDNLLITSMGHIKLTDFGLSKMGLMSLTTNLYEGHIEKDAREFLDKQVCGTPEYIAPEVIL 491 - 560 RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDDILWPEGDEALPTEAQLLISSLLQTNPL 561 - 630 VRLGAGGAFEVKQHSFFRDLDWTGLLRQKAEFIPHLESEDDTSYFDTRSDRYHHVNSYDEDDTTEEEPVE 631 - 700 IRQFSSCSPRFSKVYSSMEQLSQHEPKTPVAAAGSSKREPSTKGPEEKVAGKREGLGGLTLREKTWRGGS 701 - 770 PEIKRFSASEASFLEGEASPPLGARRRFSALLEPSRFSAPQEDEDEARLRRPPRPSSDPAGSLDARAPKE 771 - 840 ...
Mediator of cell growth. Modulates apoptosis. In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation.
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Members LATS1 LATS2 WKP Serine/threonine-protein kinase LATS1 is an enzyme that in humans is encoded by the LATS1 gene. It has been (...)
Carter HE, West HD (1955). "dl-Serine". Organic Syntheses.; Collective Volume, 3, p. 774 Hofmann, K. A.; Sand, J. (January- ...
Serine phosphorylation. Most of the seven STATs (except STAT2) undergo serine phosphorylation. Serine phosphorylation of STATs ... It has been proposed that phosphorylation of serine can regulate STAT1 dimerization, and that continuous serine phosphorylation ... Decker, Thomas; Kovarik, Pavel (2000). "Serine phosphorylation of STATs". Oncogene. 19 (21): 2628-2637. doi:10.1038/sj.onc. ... These modifications include: methylation, acetylation and serine phosphorylation. Methylation. STAT3 can be dimethylated (have ...
Greenberg, Leslie S.; Warwar, Serine; Malcolm, Wanda (January 2010). "Emotion-focused couples therapy and the facilitation of ...
The serine family of amino acid includes: serine, cysteine, and glycine. Most microorganisms and plants obtain the sulfur for ... In the glycolytic pathway, the enzyme serine hydroxymethyltransferase catalyzes the cleavage of serine to yield glycine and ... enzyme serine acetyltransferase catalyzes the transfer of acetyl group from acetyl-CoA onto L-serine to yield O-acetyl-L-serine ... In the case of methionine, the methyl carbon is derived from serine and the sulfur group, but in most organisms, it is derived ...
Greenberg, Leslie S.; Warwar, Serine H.; Malcolm, Wanda M. (April 2008). "Differential effects of emotion-focused therapy and ...
30 mg serine; 20 mg each aspartic acid, glutamic acid, hydroxyproline, proline, threonine, tyrosine, and valine; 15 mg each ...
Serine Regine Normann was born at Bø in Nordland, Norway. She was the daughter of Mikkel Normann (1827-71) and Tina Amalie ... "Serine Regine Normann". The History of Nordic Women's Literature. Retrieved April 1, 2018. CS1 maint: discouraged parameter ( ...
Greenberg, Leslie S; Warwar, Warwar, Serine H; Malcolm, Wanda M (April 2008). "Differential effects of emotion-focused therapy ...
... (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. This ... Wera S, Hemmings BA (October 1995). "Serine/threonine protein phosphatases". The Biochemical Journal. 311 ( Pt 1) (1): 17-29. ... "Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1". Nature. 376 (6543): 745-53. ...
"MetaCyc L-serine biosynthesis". biocyc.org. Retrieved 2016-03-01. Ros R, Muñoz-Bertomeu J, Krueger S (Sep 2014). "Serine in ... Ho CL, Noji M, Saito M, Saito K (Jan 1999). "Regulation of serine biosynthesis in Arabidopsis. Crucial role of plastidic 3- ... This pathway represents the only way to synthesize serine in most organisms except plants, which uniquely possess multiple ... Nonetheless, the phosphorylated pathway that PHGDH participates in is still suspected to have an essential role in serine ...
Ayriyan, Serine (April 2016). "Armenia a gateway for Iranian goods?". Russia/CIS Riskwatch. ControlRisks. Retrieved 20 April ...
Receptor serine/threonine kinases; Receptor guanylyl cyclases and histidine kinase associated receptors. Receptor tyrosine ...
Hz2V110 is homologous to serine/threonine protein kinase (S_TPK). S_TPK catalyzes phosphorylation of serine and threonine ... Edelman AM, Blumenthal DK, Krebs EG (June 1987). "Protein serine/threonine kinases". Annual Review of Biochemistry. 56 (1): 567 ... Blakley RL (October 1955). "The interconversion of serine and glycine: participation of pyridoxal phosphate". The Biochemical ... Hz2V066 is most homologous with the Bombyx mori serine hydroxymethyltransferase (SHMT), which catalyzes the reversible ...
Focus on serine proteases". Chemical Biology & Drug Design. 74 (1): 1-15. doi:10.1111/j.1747-0285.2009.00836.x. PMID 19519739. ...
"Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by ...
"Proline-serine-threonine phosphatase-interacting protein 1". Uniprot. "Serine/threonine-protein kinase Nek4". Uniprot. "SNW ...
Serine protease 55 is a protein that in humans is encoded by the PRSS55 gene. This gene encodes a member of a group of membrane ... "Entrez Gene: Serine protease 55". Retrieved 2018-04-24. CS1 maint: discouraged parameter (link) v t e This article incorporates ... chymotrypsin (S1)-like serine proteases. The encoded protein is primarily expressed in the Leydig and Sertoli cells of the ...
Zachau HG, Dütting D, Feldmann H, Melchers F, Karau W (1966). "Serine specific transfer ribonucleic acids. XIV. Comparison of ...
Serine octamer clusters are also contenders. These clusters of 8 serine molecules appear in mass spectrometry with an unusual ... S2CID 27891319.CS1 maint: multiple names: authors list (link) Nanita, S., Cooks, R. G. (2006). "Serine Octamers: Cluster ... Cooks, R. G., Zhang, D., Koch, K. J. (2001). "Chiroselective Self-Directed Octamerization of Serine: Implications for ... serine (Ser), valine (Val), tyrosine (Tyr), and tryptophan (Trp). The enantiomeric excess ee = 100 ×(L-D)/(L+D) of these amino ...
The protein is serine/threonine-rich. The expression of BCK2 with a deletion of 189 amino acids of the C-terminus resulted in ...
Liu, Qiang; Florea, Bogdan I.; Filippov, Dmitri V. (2017). "ADP-Ribosylation Goes Normal: Serine as the Major Site of the ... However, many other ADP-ribose acceptor sites such as serine, arginine, cysteine, lysine, diphthamide, phosphoserine, and ... "Serine is a new target residue for endogenous ADP-ribosylation on histones". Nature Chemical Biology. 12 (12): 998-1000. doi: ... "Serine ADP-Ribosylation Depends on HPF1". Molecular Cell. 65 (5): 932-940.e6. doi:10.1016/j.molcel.2017.01.003. PMC 5344681. ...
... is a member of the myosin light-chain kinase family of serine/threonine-specific protein kinases that phosphorylate the ... MYLK4 may also be involved in transferase activity, ATP binding, protein serine/threonine kinase activity, and also nucleotide ... Uncharacterized serine/threonine-protein kinase SgK085. There are other known myosin light-chain kinase enzymes. "RCSB Protein ...
Serine, Threonine, and Tyrosine Phosphorylation Sites. Patent US20110045603 A1. 20 Apr. 2010. Print. Kelley, LA; Sternberg, MJE ...
It acts as a serine protease. C-terminal two thirds of the protein also acts as helicase and nucleoside triphosphatase. First ( ...
... is a family of extracellular bacterial serine proteases. The proteases within this family have been ... S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases". Proteolytic Enzymes: Serine and Cysteine Peptidases. ... Other common references to this protease are staphylococcal serine protease, and SspA from its corresponding gene. ...
"GO:0008236 serine-type peptidase activity". QuickGO. EMBL-EBI. Retrieved 2018-10-17. Wey L (2016). McKay D (ed.). "Regulation ... Assembled in the genome of the clavibacter michiganensis specie, It is a putative serine protease gene that belongs to the ... This is possible due to the catalytic triad in their active site of their protein sequence: Aspartate, Serine and Histidine ( ... "AmiGO 2: Term Details for "serine-type endopeptidase activity" (GO:0004252)". Amigo. Gene Ontology Consortium. Retrieved 2018- ...
Transmembrane serine protease 11F is a protein that in humans is encoded by the TMPRSS11F gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Transmembrane serine protease 11F". Retrieved 2018-03-21. CS1 maint: discouraged parameter (link) v t e. ...
For example, the energetics of the covalent bond to the serine molecule in chymotrypsin should be compared to the well- ... Trypsin (EC 3.4.21.4) is a serine protease that cleaves protein substrates after lysine or arginine residues using a catalytic ... Warshel, A.; Naray-Szabo, G.; Sussman, F.; Hwang, J.-K. (1989). "How do Serine Proteases Really Work?". Biochemistry. 28 (9): ... as well as serine and threonine. In addition, the peptide backbone, with carbonyl and amide N groups is often employed. Cystine ...
He also discovered that a mutation in the mitochondrial serine protease Omi causes neurodegeneration. He studied at the ... Archibald, Sarah (December 2003). "Mutated mitochondrial serine protease causes neurodegeneration". Lancet Neurology. 2 (12): ...
Schwartz, Lawrence B. (1994). "[6] Tryptase: A mast cell serine protease". Proteolytic Enzymes: Serine and Cysteine Peptidases ... "Structural Changes Associated with the Spontaneous Inactivation of the Serine Proteinase Human Tryptase". Biochemistry. 34 (33 ...
Serine proteases are a common type of protease. D-Serine, synthesized in neurons by serine racemase from L-serine (its ... Serine hydroxymethyltransferase (SHMT = serine transhydroxymethylase) also catalyzes the reversible conversions of L-serine to ... L-Serine is sweet with minor umami and sour tastes at high concentration.[citation needed] Pure D-serine is an off-white ... D-Serine is being studied in rodents as a potential treatment for schizophrenia. D-Serine also has been described as a ...
L-serine ammonia-lyase Serine deaminase L-hydroxyaminoacid dehydratase L-serine deaminase L-serine dehydratase L-serine hydro- ... Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is ... In panel 3 of Figure 5) The COOH group of serine is positioned tightly in the SDH enzyme so that the serine molecule is ... L-Serine dehydratase condenses homocysteine with serine to form cystathionine. The foregoing paragraph is however mistaken as ...
serine (sĕr´ēn), organic compound, one of the 20 amino acids [1] commonly found in animal proteins. Only the l-stereoisomer ... serine An aliphatic, polar (see POLAR MOLECULE) alpha-amino acid. It is often associated with the active site of an enzyme.. ... serine (sĕr´ēn), organic compound, one of the 20 amino acids commonly found in animal proteins. Only the l-stereoisomer appears ... serine An aliphatic, polar, alpha amino acid that is often associated with the active site of an enzyme.. ...
serine-type peptidase activity. • serine-type endopeptidase activity. • hydrolase activity. • peptidase activity. • identical ... Protein HtrA2, also known as Omi, is a mitochondrially-located serine protease. The human protein Serine protease HTRA2, ... "Entrez Gene: HTRA2 HtrA serine peptidase 2".. *^ a b Jones JM, Datta P, Srinivasula SM, Ji W, Gupta S, Zhang Z, Davies E, ... Serine protease HTRA2, mitochondrial is an enzyme that in humans is encoded by the HTRA2 gene.[5][6][7] This protein is ...
... is a D-α-amino acid (CHEBI:16733) D-serine (CHEBI:16523) is a serine (CHEBI:17822) D-serine (CHEBI:16523 ... D-serine (CHEBI:16523) is enantiomer of L-serine (CHEBI:17115) D-serine (CHEBI:16523) is tautomer of D-serine zwitterion (CHEBI ... L-serine (CHEBI:17115) is enantiomer of D-serine (CHEBI:16523). D-serine residue (CHEBI:29998) is substituent group from D- ... D-serine (CHEBI:16523) has role Escherichia coli metabolite (CHEBI:76971) D-serine (CHEBI:16523) has role human metabolite ( ...
A serine/threonine protein kinase (EC 2.7.11.1) is a kinase enzyme that phosphorylates the OH group of serine or threonine ( ... Serine/threonine-specific protein kinase. From Wikipedia, the free encyclopedia. (Redirected from Non-specific serine/threonine ... While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific ... specifically protein-serine/threonine kinases. These enzymes transfer phosphates to the oxygen atom of a serine or threonine ...
Serine , Monograph containing literature references, physical and biological properties and relevant information ...
Serine phosphorylation of STATs.. Decker T1, Kovarik P.. Author information. 1. Vienna Biocenter, Institute of Microbiology and ... The phosphorylated residue in this case is a serine contained within a P(M)SP motif, and in the majority of situations its ... This review addresses recent advances in understanding the regulation of STAT serine phosphorylation, as well as the kinases ... The biochemical and biological consequences of STAT serine phosphorylation are discussed. Oncogene (2000). ...
Serine definition, a crystalline amino acid, HOCH 2 CH(NH 2)COOH, found in many proteins and obtained by the hydrolysis of ... serine in Medicine Expand. serine ser·ine (sěrēn). n. Abbr. Ser An amino acid that is a common constituent of many proteins. ... Word Origin and History for serine Expand. n. type of amino acid, 1880, from German serin (1865), from Latin sericum "silk" ( ...
Yamashita A. (2018) Serine/Threonine-Protein Kinase SMG1. In: Choi S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham ...
Brands A-Z Lake Avenue Nutrition L-Serine Categories Supplements Amino Acids L-Serine Categories Health Topics Anti-Aging & ...
... *Formula: C15H35NO3Si2 ... Other names: l-Serine, o-(tert-butyldimethylsilyl)-, tert- ...
Help!] Amidase ,-, Serine Proteinase. Hyunmin Kim vurk at hymail.hanyang.ac.kr Wed Nov 25 02:48:58 EST 1998 *Previous message: ... 2. Homology searching in GenBank shown me that the gene(magA) has best identity(70-80%) with lots of serine proteinases. Based ...
... are involved in many aspects of biology from embryonic development to cancer metastasis. For ...
Serine proteases are a common type of protease. SignalingEdit. D-Serine, synthesized in neurons by serine racemase from L- ... D-Serine is being studied in rodents as a potential treatment for schizophrenia[22] and L-serine is in a FDA-approved human ... Pure D-serine is an off-white crystalline powder with a very faint musty aroma. D-Serine is sweet with an additional minor sour ... Serine deficiency disorders are rare defects in the biosynthesis of the amino acid L-serine. At present three disorders have ...
Glycine, serine and threonine metabolism Glycine, serine and threonine metabolismSerine is derived from 3-phospho-D-glycerate, ... RecName: Full=Serine hydroxymethyltransferase, cytosolic; Short=SHMT; AltName: F... RecName: Full=Serine ... Serine hydroxymethyl transferase 1 stimulates pro-oncogenic cytokine expression through sialic acid to promote ovarian cancer ... Serine hydroxymethyl transferase 1 stimulates pro-oncogenic cytokine expression through sialic acid to promote ovarian cancer ...
4), has strong homology to a cytoplasmic Xenopus serine/threonine protein kinase XEEK1 (ref. 5), and weaker similarity to many ... A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. *Akseli Hemminki1. , ... 4), has strong homology to a cytoplasmic Xenopus serine/threonine protein kinase XEEK1 (ref. 5), and weaker similarity to many ... Su, J.-Y., Erikson, E. & Maller, J. L. Cloning and characterization of a novel serine/threonine protein kinase expressed in ...
Genealogy for Anna Serine Asbjørnsdatter (deceased) family tree on Geni, with over 180 million profiles of ancestors and living ...
One classic feature of water-soluble serine proteases is an asparagine-histidine-serine catalytic triad (25, 26). The relative ... which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed ... The catalytic serine residue (Ser-201) (8) flanks the membrane-embedded N-terminal end of TM4 (Fig. 2 A). The catalytic ... The GlpG active site viewed from the membrane (A) compared with that of the soluble serine protease trypsin (B) (PDB entry 1TLD ...
Water-insoluble serine proteases derivatives from Acremonium chrysogenum, Bac. subtilis, and trypsin were prepared by ... Bendikiene, V., & Juodka, B. (1998). Stabilization of serine proteases by immobilization. Progress in Biotechnology, 15(C), 583 ... Water-insoluble serine proteases derivatives from Acremonium chrysogenum, Bac. subtilis, and trypsin were prepared by ... The stabilization of trypsin and serine proteases I and II from Acremonium chrysogenum against thermal inactivation and ...
Profiling of serine protease activities in human stratum corneum and detection of a stratum corneum tryptase-like enzyme. * ... In this study, we examined the distribution of key serine protease activities (kallikrein 5, kallikrein 7, urokinase, plasmin ... the outer SC exhibits greater serine protease activity than its deeper layers, (iii) compared with the forearm, urokinase- and ...
... Olga Mitrofanova. ,1 Ayslu Mardanova. ,1 Vladimir Evtugyn. ,1 ... The interest of Bacillus serine proteases AprBp and GseBp lies in the fact that these enzymes were able to disrupt tightly ... The studies on Bacillus biofilms support the hypothesis that serine proteases are sufficient alone to remove biofilms by ... L. A. Lyublinskaya, T. L. Voyushina, and V. M. Stepanov, "Enzymatic synthesis of serine proteases peptide substrates," Russian ...
... used books by Steven L Serine, including hardcovers, softcovers, rare, out-of-print first editions, signed copies, and more. ...
Christ (Serine) Stockland of rural Binford died February 18 in the hospital here, where she had been a patient about three ... Add Photos for Serine Rugland Stockland. Fulfill Photo Request for Serine Rugland Stockland. ... Serine Rugland Stockland Birth. 9 Nov 1873. Stavanger, Stavanger kommune, Rogaland fylke, Norway ... Christ (Serine) Stockland of rural Binford died February 18 in the hospital here, where she had been a patient about three ...
... serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in ... Digestive serine proteases. Members. Chymotrypsin-clan. The three serine proteases of the chymotrypsin-like clan that have been ... The serine -OH attacks the carbonyl carbon, and the nitrogen of the histidine accepts the hydrogen from the -OH of the [serine ... In biochemistry, serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide ...
... The serine hydrolase superfamily is one of the largest known enzyme families comprising approximately 1% of ... The serine hydrolase superfamily is one of the largest known enzyme families comprising approximately 1% of the genes in the ... all of these enzymes share a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is ... It uses material from the Wikipedia article "Serine_hydrolase". A list of authors is available in Wikipedia. ...
D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.. ... L-Serine plays a role in cell growth and development (cellular proliferation). The conversion of L-serine to glycine by serine ... Serine is needed for the proper metabolism of fats and fatty acids. It also helps in the production of antibodies. Serine is ... proteinogenic amino acid, L-alpha-amino acid, serine, serine family amino acid (CHEBI:17115) / Common amino acids (C00065) ...
a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. ... sp,P03772,PP_LAMBD Serine/threonine-protein phosphatase OS=Escherichia phage lambda PE=1 SV=1 ...
membrane-anchored serine proteases. Join us at this small, focused meeting in September in Maryland. By Karin List and Toni ... The unveiling of a new family of serine proteases that are anchored directly to the plasma membrane was an unexpected outcome ... Karin List studies the role of type II transmembrane serine proteases and their inhibitors in cancer progression at Wayne State ... Qingyu Wu is a longstanding investigator of corin, a membrane serine protease essential for natriuretic peptide processing and ...
L-Serine benzyl ester hydrochloride for your research needs. Find product specific information including CAS, MSDS, protocols ...
  • The high-temperature requirement (HtrA) family are conserved evolutionarily and these oligomeric serine proteases has been classified in family S1B of the PA protease clan in the MEROPS protease database. (wikipedia.org)
  • Membrane-anchored serine proteases are involved in many aspects of biology from embryonic development to cancer metastasis. (asbmb.org)
  • Rhomboids are evolutionarily widespread intramembrane serine proteases. (pnas.org)
  • Another family, which is the subject of our study, is the intramembrane serine proteases, termed rhomboids. (pnas.org)
  • Rhomboids are evolutionarily widespread intramembrane serine proteases ( 7 , 8 ) that act as regulators of intercellular signaling ( 9 , 10 ), parasite invasion ( 11 ), quorum sensing ( 12 ), mitochondrial morphology and dynamics ( 13 , 14 ), and apoptosis ( 15 ). (pnas.org)
  • Stabilization of serine proteases. (mendeley.com)
  • Both Pseudomonas aeruginosa LasB elastase and Esp serine protease secreted by Staphylococcus epidermidis emerge as major antibiofilm proteases that inhibit S. aureus biofilm formation and detach preexisting biofilms [ 14 , 15 ]. (hindawi.com)
  • In biochemistry , serine proteases or serine endopeptidases (newer name) are a class of peptidases ( enzymes that cleave peptide bonds in proteins ) that are characterised by the presence of a serine residue in the active site of the enzyme . (bionity.com)
  • Serine proteases are grouped into clans that share structural homology and then further subgrouped into families that share close sequence homology. (bionity.com)
  • Serine proteases participate in a wide range of functions in the body, including blood clotting , immunity , and inflammation , as well as contributing to digestive enzymes in both prokaryotes and eukaryotes. (bionity.com)
  • The three serine proteases of the chymotrypsin-like clan that have been studied in greatest detail are chymotrypsin , trypsin , and elastase . (bionity.com)
  • Serine proteases and their natural protein inhibitors are among the most intensively studied protein complexes. (springer.com)
  • The unveiling of a new family of serine proteases that are anchored directly to the plasma membrane was an unexpected outcome of the complete sequencing of several vertebrate genomes at the turn of the millennium. (asbmb.org)
  • The American Society for Biochemistry and Molecular Biology will host a special symposium this fall focusing on the biochemistry, biology and pathophysiological functions of membrane-anchored serine proteases, including the translational research opportunities afforded by this interesting group of enzymes. (asbmb.org)
  • Recent studies have revealed that the membrane-anchored serine proteases are important components of the mammalian degradome, playing critical roles in both health and disease through the regulation of metabolic homeostasis, fertilization, morphogenesis, epithelial biology, iron homeostasis, cardiovascular diseases, viral infection and cancer. (asbmb.org)
  • Her laboratory discovered that infection and dissemination of influenza virus is dependent on cleavage activation of influenza virus hemagglutinin by the host transmembrane serine proteases TMPRSS2 and HAT in the human airway epithelium. (asbmb.org)
  • Thomas Kleyman , a longtime investigator of epithelial Na+ channels, has made key contributions to understanding the molecular structure of the channel's pore and the key roles of Na+, divalent metal ions and membrane serine proteases in the regulation of channel activities. (asbmb.org)
  • His emphasis is on identifying the roles and regulation of the activities of membrane-anchored serine proteases associated with infectious diseases, cancer and development. (asbmb.org)
  • Jan K. Jensen is a structural biologist whose work has provided new insight into the structure and function of hepatocyte growth factor activator inhibitor, or HAI, domains, the proteins that act as cofactors for many of the type-2 transmembrane serine proteases. (asbmb.org)
  • Karin List studies the role of type II transmembrane serine proteases and their inhibitors in cancer progression at Wayne State University School of Medicine. (asbmb.org)
  • Toni Antalis studies the physiological roles of membrane-anchored serine proteases at the University of Maryland School of Medicine. (asbmb.org)
  • Dang QD, Di Cera E Residue 225 determines the Na (+) - induced allosteric regulation of catalytic activity in serine proteases. (wordnik.com)
  • In one investigation, Schmitt found that enzymes called serine -class proteases, which break down proteins in the sprouting grain, can also break down beta-amylase, an important enzyme for converting carbs to simple sugars. (wordnik.com)
  • Serine proteases play pivotal roles in normal physiology and a spectrum of patho-physiological processes. (diva-portal.org)
  • to jointly develop monoclonal antibodies and peptides as new cancer therapeutics targeting two lead serine proteases isolated and characterized by Corvas. (thefreedictionary.com)
  • When neutrophil granule proteases were inhibited with either a protease mixture, or specific serine protease inhibitors 4-(2-Aminoethyl)benzenesulfonylfluoride and diisopropylfluorophosphate, killing by neutrophils was inhibited in a manner that correlated with increased intracellular survival. (jimmunol.org)
  • All three compounds inhibited intracellular activity of the three major neutrophil serine proteases: elastase, cathepsin G, and proteinase 3. (jimmunol.org)
  • Inhibition studies using specific inhibitors of these serine proteases suggested that while each serine protease is sufficient to kill the pneumococcus, none is essential. (jimmunol.org)
  • Our findings show that Gram-positive pathogens are killed by human neutrophils via different mechanisms involving serine proteases. (jimmunol.org)
  • A ready-to-use reverse transfection format RNAi screening library targeting human serine proteases. (horizondiscovery.com)
  • They are evolutionarily conserved ATP-independent serine proteases, widely distributed from bacteria to humans. (atlasgeneticsoncology.org)
  • Serine proteases in the adult CNS contribute both to activity-dependent structural changes accompanying learning and to the regulation of excitotoxic cell death. (jneurosci.org)
  • Within the hippocampus, our data suggest that BSP1/neuropsin, unlike other serine proteases, has little effect on physiological synaptic remodeling and instead plays a role in limiting neuronal hyperexcitability induced by epileptogenic insult. (jneurosci.org)
  • Serine proteases fulfil diverse roles in the CNS. (jneurosci.org)
  • Serine proteases also regulate excitotoxic neuronal cell death. (jneurosci.org)
  • Such potentially paradoxical findings suggest complex regulation of neurodegeneration by serine proteases. (jneurosci.org)
  • Serine is derived from 3-phospho-D-glycerate, an intermediate of glycolysis [MD:M00020], and glycine is derived from serine. (nih.gov)
  • The conversion of L-serine to glycine by serine hydroxymethyltransferase results in the formation of the one-carbon units necessary for the synthesis of the purine bases, adenine and guanine. (drugbank.ca)
  • In addition, L-serine conversion to glycine via this same enzyme provides the one-carbon units necessary for production of the pyrimidine nucleotide, deoxythymidine monophosphate, also an essential component of DNA. (drugbank.ca)
  • Unlike other neurotransmitter receptors, which are activated by individual neurotransmitters, activation of NMDARs requires the binding of a coagonist (D-serine or glycine) in addition to glutamate. (curriki.org)
  • We integrated metabolic tracing and transcriptional profiling of a large panel of non-small cell lung cancer (NSCLC) cell lines to characterize the activity and regulation of the serine/glycine biosynthetic pathway in NSCLC. (nih.gov)
  • We found that NRF2 controls the expression of the key serine/glycine biosynthesis enzyme genes PHGDH, PSAT1 and SHMT2 via ATF4 to support glutathione and nucleotide production. (nih.gov)
  • Thus, a substantial fraction of human NSCLCs activates an NRF2-dependent transcriptional program that regulates serine and glycine metabolism and is linked to clinical aggressiveness. (nih.gov)
  • M00020 ], and glycine is derived from serine. (genome.jp)
  • M. Lowry, D. E. Hall, M. S. Hall and J. T. Brosnan, "Renal Metabolism of Amino Acids in Vivo: Studies On Serine and Glycine Fluxes," American Journal of Physiology, Vol. 252, No. 2, February 1987, pp. (scirp.org)
  • Serine is a precursor of the nonessential amino acids glycine and cysteine. (rupress.org)
  • The conversion of serine to glycine, catalyzed by serine hydroxymethyltransferase (SHMT), donates a one-carbon unit to tetrahydrofolate to produce 5,10-methylenetetrahydrofolate (CH 2 -THF). (rupress.org)
  • LDRPFDETTYEETED , corresponding to amino acids 548-562 of Human Serine Palmitoyltransferase. (abcam.com)
  • Human serine racemase is a pyridoxal 5'-phosphate (PLP)-dependent dimeric enzyme that catalyzes the reversible racemization of L-serine and D-serine and their dehydration to pyruvate and ammonia. (frontiersin.org)
  • The cumulative knowledge on human serine racemase allowed obtaining insights into its conformational landscape and into the mechanisms of cross-talk between the effector binding sites and the active site. (frontiersin.org)
  • Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. (wikipedia.org)
  • A defining characteristic of these enzymes is the presence of a nucleophilic serine in their active site, which is used for the hydrolysis of substrates. (wikipedia.org)
  • Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. (wikipedia.org)
  • When incorporated into the structure of enzymes, serine often plays an important role in their catalytic function. (encyclopedia.com)
  • Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. (wikipedia.org)
  • The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. (wikipedia.org)
  • Serine plays an important role in the catalytic function of many enzymes . (wikipedia.org)
  • The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all serine protease enzymes. (bionity.com)
  • Serine is critical for the production of the body's proteins, enzymes and muscle tissue. (drugbank.ca)
  • Molecular cloning revealed that serine/threonine phosphatases belong to two different families of about a dozen of genes each in mammals: the phosphoprotein phosphatase P (PPP) family includes PP1, PP2A, PP2B, and a few related enzymes, PP4, PP5, PP6 and PP7, while the phosphoprotein phosphatase M family (PPM) includes PP2C and related enzymes. (sigmaaldrich.com)
  • In particular, the researchers were focusing on a group of enzymes, called serine hydrolases, that break down proteins, fats, and other molecules in cells. (wordnik.com)
  • The present invention relates to serinecarbonates and the use of serine carbonates as precursors for (a) organoleptic compounds, especially for fragrances, flavors and/or (b) masking agents, and/or (c) antimicrobial compounds and/or (d) alternative substrates for malodor producing enzymes. (patentgenius.com)
  • Serine can also be found on the active sites of various enzymes to support their catalytic function. (sciencephoto.com)
  • J. E. Antflick, G. B. Baker and D. R. Hampson, "The Effects of a Low Protein Diet on Amino Acids and Enzymes in the Serine Synthesis Pathway in Mice," Amino Acids, Vol. 39, No. 1, June 2010, pp. 145-153. (scirp.org)
  • The Human siGENOME Serine Protease RNA Library consists of siRNAs targeting enzymes with known or predicted protease activity. (horizondiscovery.com)
  • serine (sĕr´ēn) , organic compound, one of the 20 amino acids commonly found in animal proteins. (encyclopedia.com)
  • Serine , an amino acid obtainable by hydrolysis of most common proteins , sometimes constituting 5 to 10 percent by weight of the total product. (britannica.com)
  • Serine (symbol Ser or S ) [3] [4] is an ɑ- amino acid that is used in the biosynthesis of proteins. (wikipedia.org)
  • Genes coding for phosphoserine/threonine phosphatases are less numerous in vertebrate genomes than those for serine /threonine kinases, and the complexity of phosphatases function arises in part from the interactions of catalytic subunits with other proteins. (sigmaaldrich.com)
  • In addition to being a building block for proteins, Serine participates in the biosynthesis of biomolecules such as amino acids, nucleotides, phospholipids, and sphingolipids. (frontiersin.org)
  • Serine residues are found in most proteins and within proteins function as a site for phosphorylation. (clinicaltrials.gov)
  • We offer Serine Palmitoyltransferase 2 Peptides and Serine Palmitoyltransferase 2 Proteins for use in common research applications: Blocking/Neutralizing, ELISA, Protein Array, Western Blot. (novusbio.com)
  • Our Serine Palmitoyltransferase 2 Peptides and Serine Palmitoyltransferase 2 Proteins can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Serine Palmitoyltransferase 2 Peptides and Proteins. (novusbio.com)
  • Additionally we are shipping serine Dehydratase Antibodies (53) and serine Dehydratase Proteins (6) and many more products for this protein. (antibodies-online.com)
  • Serine Dehydratase is also known as: L-serine ammonia-lyase Serine deaminase L-hydroxyaminoacid dehydratase L-serine deaminase L-serine dehydratase L-serine hydro-lyase HoloEnzyme: The holoenzyme SDH contains 319 residues, 1 PLP cofactor molecule, and 131 water molecules. (wikipedia.org)
  • Figure 1 shows the large catalytic domain in purple and cyan and the small regulatory domain in green in a monomer of Serine Dehydratase. (wikipedia.org)
  • In overall terms, the reaction catalyzed by serine dehydratase involves two steps: catalytic elimination and a nonenzymatic hydrolysis reaction. (wikipedia.org)
  • We offer Serine Dehydratase Lysates for use in common research applications: Western Blot. (novusbio.com)
  • Each Serine Dehydratase Lysate is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Our Serine Dehydratase Lysates can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Serine Dehydratase Lysates. (novusbio.com)
  • On www.antibodies-online.com are 12 serine Dehydratase (SDS) ELISA Kits from 5 different suppliers available. (antibodies-online.com)
  • A total of 78 serine Dehydratase products are currently listed. (antibodies-online.com)
  • Catalysis proceeds by the formation of an acyl-enzyme intermediate through this serine, followed by water/hydroxide-induced saponification of the intermediate and regeneration of the enzyme. (wikipedia.org)
  • The so-called nerve gases and many substances used in insecticides have been shown to act by combining with a residue of serine in the active site of acetylcholine esterase, inhibiting the enzyme completely. (encyclopedia.com)
  • Serine protease HTRA2, mitochondrial is an enzyme that in humans is encoded by the HTRA2 gene . (wikipedia.org)
  • Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. (wikipedia.org)
  • This gene encodes the cytosolic form of serine hydroxymethyltransferase, a pyridoxal phosphate-containing enzyme that catalyzes the reversib. (nih.gov)
  • The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. (pnas.org)
  • In this study, we examined the distribution of key serine protease activities (kallikrein 5, kallikrein 7, urokinase, plasmin and a tryptase-like enzyme) in different layers of the SC on the cheek and the forearm by analysis of consecutive tape strippings of healthy Caucasian subjects during winter and summer. (mendeley.com)
  • The serine hydrolase superfamily is one of the largest known enzyme families comprising approximately 1% of the genes in the human genome. (bionity.com)
  • However, recent findings indicate that D-serine signaling does not depend solely on glia, because D-serine and its biosynthetic enzyme are also present in substantial amounts in neurons. (curriki.org)
  • Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. (rcsb.org)
  • This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. (rcsb.org)
  • Phosphoglycerate dehydrogenase (PHGDH), the first rate-limiting enzyme of serine synthesis, is frequently overexpressed in human cancer. (jci.org)
  • Serine racemase belongs to the fold-type II of the PLP-dependent enzyme family and structural models from several orthologs are available. (frontiersin.org)
  • The comparison of structures of serine racemase co-crystallized with or without ligands indicates the presence of at least one open and one closed conformation, suggesting that conformational flexibility plays a relevant role in enzyme regulation. (frontiersin.org)
  • The enzyme serine racemase, found primarily in glia, synthesizes D-serine from L-serine. (alzforum.org)
  • De Belleroche proposes the following hypothesis for DAO and ALS: Young people carrying only one functional DAO gene have enough of the enzyme to mop up D-serine, keeping the NMDA receptors from going overboard. (alzforum.org)
  • K. Snell and D. A. Fell, "Metabolic Control Analysis of Mam-Malian Serine Metabolism," Advances in Enzyme Regulation, Vol. 30, 1990, pp. 13-32. (scirp.org)
  • Unlike other non-catalytic serines, the nucleophilic serine of these hydrolases is typically activated by a proton relay involving a catalytic triad consisting of the serine, an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine), although variations on this mechanism exist. (wikipedia.org)
  • The phosphorylated residue in this case is a serine contained within a P(M)SP motif, and in the majority of situations its mutation to alanine alters transcription factor activity. (nih.gov)
  • By examining the means by which podocytes influence the glomerular endothelial phenotype, we identified a role for phosphorylation of histone H3 on serine residue 10 (phospho-histone H3Ser10) in mediating endothelial activation in diabetes. (diabetesjournals.org)
  • Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines , cysteine , tryptophan (in bacteria), and a large number of other metabolites. (encyclopedia.com)
  • Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines . (wikipedia.org)
  • Impaired serine metabolism has been assigned a role in psychiatric disorder and neurological disease. (uib.no)
  • Serine is needed for the proper metabolism of fats and fatty acids. (drugbank.ca)
  • This Research Topic addresses the metabolism and function of the amino acid Serine in plants. (frontiersin.org)
  • Serine is a polar amino acid that plays a fundamental role in plant metabolism, plant development, and cell signalling. (frontiersin.org)
  • The interactions between the photorespiratory and non-photorespiratory serine biosynthetic pathways may be particularly important in environments with increased CO2 concentrations in forthcoming years, which could have unpredictable effects on plants, and for plants with a C4 photosynthetic metabolism where photorespiratory activity is restricted. (frontiersin.org)
  • In conclusion, L-serine modifies the metabolism of taurine and L-alanine in the extracellular space in chick brain. (scirp.org)
  • Recent studies cast new light on the role of serine metabolism in cancer, suggesting that active serine synthesis might be required to facilitate amino acid transport, nucleotide synthesis, folate metabolism, and redox homeostasis in a manner that impacts cancer. (rupress.org)
  • The importance of serine metabolism in multiple cancers is increasingly apparent, and how the metabolism of this amino acid influences cancer phenotypes is an area of active investigation. (rupress.org)
  • This review discusses the discovery of the serine synthesis pathway and its dysregulation in cancer and summarizes the findings of many recent studies on the role of serine metabolism in cancer. (rupress.org)
  • Phosphoglycerate dehydrogenase (PHGDH) amplification in select cancers, the role of extracellular serine in supporting cell proliferation, potential benefits of increased serine synthesis pathway (SSP) flux, and the interaction between glycolysis, the SSP, and nucleotide biosynthesis are all discussed with a perspective on how altered serine metabolism plays a role in cancer. (rupress.org)
  • Additionally, serine supplies carbon to the one-carbon pool, which is involved in folate metabolism ( Fig. 2 ). (rupress.org)
  • The diffraction pattern being created in the art and craft piece is that of a target called serine racemase, which is an important target in the fight against pain and neurodegenerative disorders such as Alzheimer's disease. (wordnik.com)
  • As D-serine is the co-agonist of the N-methyl D-aspartate receptors for glutamate, the most abundant excitatory neurotransmitter in the brain, the structure, dynamics, function, regulation and cellular localization of serine racemase have been investigated in detail. (frontiersin.org)
  • Further information on serine racemase structure and dynamics resulted from the search for inhibitors with potential therapeutic applications. (frontiersin.org)
  • A gene on chromosome 17p13 that encodes serine racemase, which converts L-serine to D-serine, a key co-agonist with glutamate at NMDA receptors. (thefreedictionary.com)
  • The biosynthesis of serine starts with the oxidation of 3-phosphoglycerate (an intermediate from glycolysis ) to 3-phosphohydroxypyruvate and NADH by phosphoglycerate dehydrogenase ( EC 1.1.1.95 ). (wikipedia.org)
  • Plants possess at least two serine biosynthetic pathways: i) the glycolate pathway associated with photorespiration and ii) the so-called Phosphorylated Pathway of Serine Biosynthesis. (frontiersin.org)
  • The biological significance of the coexistence of several pathways for the biosynthesis of Serine is not known. (frontiersin.org)
  • L-serine is directly involved in the biosynthesis of purines, pyrimidines, and other amino acids. (clinicaltrials.gov)
  • S. Furuya, "An Essential Role for de Novo Biosynthesis of L-Serine in CNS Development," Asia Pacific Journal of Clinical Nutrition, Vol. 17, Supplement, No. 1, 2008, pp. 312-315. (scirp.org)
  • D. A. Fell and K. Snell, "Control Analysis Of Mammalian Serine Biosynthesis. (scirp.org)
  • The catabolic L-serine (L-threonine) deaminase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. (genetics.org)
  • In particular, we poorly understand the contribution that each pathway makes to plant serine homeostasis, how pathways are integrated and coordinated, and how they interact at the transcriptional/translational/posttranslational levels. (frontiersin.org)
  • Tumors have high energetic and anabolic needs for rapid cell growth and proliferation, and the serine biosynthetic pathway was recently identified as an important source of metabolic intermediates for these processes. (nih.gov)
  • D-amino oxidase (DAO) oxidizes D-serine, a co-factor in activation of NMDA-type glutamate receptors. (alzforum.org)
  • The reaction it catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia. (wikipedia.org)
  • By orienting the substrates and utilizing the PLP coenzyme, SDH lowers the activation energy to convert L-Serine into pyruvate, which can then be converted into glucose. (wikipedia.org)
  • The degradation of serine to pyruvate is an example of a pyridoxal phosphate-dependent (PLP) catalyzed Beta-elimination reaction. (wikipedia.org)
  • This review addresses recent advances in understanding the regulation of STAT serine phosphorylation, as well as the kinases and other signal transducers implied in this process. (nih.gov)
  • Perhaps reflecting this complex regulation, diverse members of the serine protease family are expressed in the CNS, notably in the hippocampus. (jneurosci.org)
  • Parkin deficiency in cancer cells stabilized PHGDH and activated serine synthesis to promote cell proliferation and tumorigenesis, which was largely abolished by targeting PHGDH with RNA interference, CRISPR/Cas9 KO, or small-molecule PHGDH inhibitors. (jci.org)
  • Su, J.-Y., Erikson, E. & Maller, J. L. Cloning and characterization of a novel serine/threonine protein kinase expressed in early Xenopus embryos. (nature.com)
  • 2. Homology searching in GenBank shown me that the gene(magA) has best identity(70-80%) with lots of serine proteinases. (bio.net)
  • para]]"This is a significant milestone for the company and shows the power of Abide's unique approach to target the validated but largely underexplored class of serine hydrolases," said Alan Ezekowitz, MBChB, D. (thefreedictionary.com)
  • Subtilisin is evolutionary unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a catalytic triad , to create a nucleophilic serine . (bionity.com)
  • it is thought that the hydroxyl group of the serine side chain initiates cleavage by nucleophilic attack of the hydroxyl oxygen on the peptide carbonyl carbon, with subsequent hydrolysis by a water molecule. (horizondiscovery.com)
  • Women who are pregnant or breastfeeding shouldn't use serine supplements. (lifebridgehealth.org)
  • We put our players on a brain healthy program that included a weight-loss group, regular exercise (surprisingly many of these former elite athletes had become couch potatoes), mental exercises, and nutritional supplements that support brain health, such as fish oil, and a proprietary formula including ginkgo biloba, huperzine A, phosphatidyl serine and vinpocetine, among others. (wordnik.com)
  • Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. (asm.org)
  • In many cases, extracellular serine alone is sufficient to support cancer cell proliferation, whereas some cancer cells increase serine synthesis from glucose and require de novo serine synthesis even in the presence of abundant extracellular serine. (rupress.org)
  • The serine/threonine phosphatases of the PPP family are mostly regulated by protein-protein interactions. (sigmaaldrich.com)
  • We emphasize the interaction and coordination between the Serine biosynthetic pathways and other metabolic pathways. (frontiersin.org)
  • We also poorly understand the coordination of Serine biosynthetic pathways with other essential metabolic pathways, such as photosynthesis, respiration, protein synthesis, and nitrogen assimilation to control plant growth and development. (frontiersin.org)
  • Molecular genetics of serine and threonine catabolism in Saccharomyces cerevisiae. (genetics.org)
  • A molecular model of serine, a proteinogenic amino acid synthesized within the human body. (sciencephoto.com)
  • Serine phosphorylation of STATs. (nih.gov)
  • The biochemical and biological consequences of STAT serine phosphorylation are discussed. (nih.gov)
  • Instead, metabolic studies indicated a requirement for serine to allow cells to compensate for biguanide-induced decrease in oxidative phosphorylation by upregulating glycolysis. (aacrjournals.org)
  • Phosphorylation of certain serine at ER may relate to breast cancer process and on-going treatment. (thefreedictionary.com)
  • Global L-Serine research report provides the complete and precise view of the market during the forecast period from 2017-2022. (openpr.com)
  • To conclude with the L-Serine Report has done the exhaustive study of the market during the projected span of 2017 to 2022 which will help them to make right decisions at right time to see the growth of their industry. (openpr.com)
  • D-serine is a naturally occurring activator of the N-methyl-d-aspartate-type glutamate receptors (NMDAR) in the brain, and this project will assess the optimal dose of D-serine treatment over three sessions of a program designed to measure auditory plasticity. (clinicaltrials.gov)
  • Phosphatidyl Serine is a major structural component of neural membranes where it assists in the conduction of electrical impulses and facilitates the activity of neurotransmitters involved in learning, memory and mood. (a1supplements.com)
  • Serine and some of its derivatives (e.g., ethanolamine ) are also important components of a class of lipids ( phospholipids ) found in biological membranes . (britannica.com)
  • Phosphatidyl Serine (Phosphatidylserine) is one of the key human brain phospholipids and is essential for normal neuron structure and function. (vitasprings.com)
  • Serine is necessary for the production of sphingolipids via the synthesis of sphingosine, and serine is a headgroup, or headgroup precursor, for phospholipids. (rupress.org)
  • Accordingly, while L-serine is a candidate anti-stress factor, the central mechanism of L-serine is not clear. (scirp.org)
  • Nature's Way Phosphatidyl-Serine at Netrition.com. (netrition.com)
  • Nature's Way Phosphatidyl-Serine assists in regulating membrane transfer of nutrients and neurotransmitters necessary for proper mental function. (netrition.com)
  • Nature's Way Phosphatidyl-Serine may be a safe and effective therapeutic agent in treating memory deficit disorders and for improving other higher brain functions. (netrition.com)
  • Buy Phosphatidyl Serine from Carlson Labs at VitaSprings, and we guarantee you a safe, secure online shopping experience! (vitasprings.com)
  • PHGDH overexpression activates serine synthesis to promote cancer progression. (jci.org)
  • Parkin interacted with PHGDH and ubiquitinated PHGDH at lysine 330, leading to PHGDH degradation to suppress serine synthesis. (jci.org)
  • D-serine is a NMDAR modulator that when combined with neuroplasticity-based auditory remediation, leads to highly significant, acute improvement in both auditory plasticity and the early auditory processing measures mismatch negativity (MMN) and theta intertrial coherence (theta). (clinicaltrials.gov)
  • We will be investigating the effect of D-serine, (DSR), a selective and potent NMDAR agonist, as monotherapy for treatment resistant schizophrenics. (clinicaltrials.gov)
  • Although previously considered an "unnatural" amino acid, D-serine is a key regulator of NMDAR activity and may be the main physiological ligand at the coagonist site. (curriki.org)
  • Astrocytes physiologically affect NMDAR neurotransmission by releasing D-serine, suggesting that D-serine acts as a gliotransmitter. (curriki.org)
  • These results suggest that L-serine has an ability to promote L-alanine synthesis facilitating the catabolism of taurine. (scirp.org)
  • D-Serine is synthesized in the mammalian brain and is enriched in astrocytes, a class of glial cells that ensheath synapses in the brain. (curriki.org)
  • Since some L-serine is produced by astrocytes in the brain, it is considered a non-essential amino acid. (clinicaltrials.gov)
  • J. Mitoma, S. Furuya and Y. Hirabayashi, "A Novel Metabolic Communication between Neurons and Astrocytes: Non-Essential Amino Acid L-Serine Released from Astrocytes is Essential for Developing Hippocampal Neurons," Neuroscience Research, Vol. 30, No. 2, February 1998, pp. 195-199. (scirp.org)
  • Subtilisin is a serine protease in prokaryotes . (bionity.com)
  • Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. (nih.gov)
  • Serine enters the active site and its positively charged amino group attracts the negatively charged phosphate group of PLP. (wikipedia.org)
  • In panel 2 of Figure 5) The PLP phosphate deprotonate the amino group of serine. (wikipedia.org)
  • a protein]-serine/threonine phosphate + H 2 O = [a protein]-serine/threonine + phosphate. (uniprot.org)