A cyclin subtype that is found abundantly in post-mitotic tissues. In contrast to the classical cyclins, its level does not fluctuate during the cell cycle.
Protein encoded by the bcl-1 gene which plays a critical role in regulating the cell cycle. Overexpression of cyclin D1 is the result of bcl-1 rearrangement, a t(11;14) translocation, and is implicated in various neoplasms.
A cyclin subtype that has specificity for CDC2 PROTEIN KINASE and CYCLIN-DEPENDENT KINASE 2. It plays a role in progression of the CELL CYCLE through G1/S and G2/M phase transitions.
A serine-threonine kinase that plays important roles in CELL DIFFERENTIATION; CELL MIGRATION; and CELL DEATH of NERVE CELLS. It is closely related to other CYCLIN-DEPENDENT KINASES but does not seem to participate in CELL CYCLE regulation.
A 50-kDa protein that complexes with CYCLIN-DEPENDENT KINASE 2 in the late G1 phase of the cell cycle.
Highly differentiated epithelial cells of the visceral layer of BOWMAN CAPSULE of the KIDNEY. They are composed of a cell body with major CELL SURFACE EXTENSIONS and secondary fingerlike extensions called pedicels. They enwrap the KIDNEY GLOMERULUS capillaries with their cell surface extensions forming a filtration structure. The pedicels of neighboring podocytes interdigitate with each other leaving between them filtration slits that are bridged by an extracellular structure impermeable to large macromolecules called the slit diaphragm, and provide the last barrier to protein loss in the KIDNEY.
A cyclin subtype that is transported into the CELL NUCLEUS at the end of the G2 PHASE. It stimulates the G2/M phase transition by activating CDC2 PROTEIN KINASE.
A cyclin B subtype that colocalizes with MICROTUBULES during INTERPHASE and is transported into the CELL NUCLEUS at the end of the G2 PHASE.
A 44 kDa mitogen-activated protein kinase kinase with specificity for MITOGEN-ACTIVATED PROTEIN KINASE 1 and MITOGEN-ACTIVATED PROTEIN KINASE 3.
A cyclin D subtype which is regulated by GATA4 TRANSCRIPTION FACTOR. Experiments using KNOCKOUT MICE suggest a role for cyclin D2 in granulosa cell proliferation and gonadal development.
A broadly expressed type D cyclin. Experiments using KNOCKOUT MICE suggest a role for cyclin D3 in LYMPHOCYTE development.
A cyclin A subtype primarily found in male GERM CELLS. It may play a role in the passage of SPERMATOCYTES into meiosis I.
A widely-expressed cyclin A subtype that functions during the G1/S and G2/M transitions of the CELL CYCLE.
A cyclin subtype that is specific for CYCLIN-DEPENDENT KINASE 4 and CYCLIN-DEPENDENT KINASE 6. Unlike most cyclins, cyclin D expression is not cyclical, but rather it is expressed in response to proliferative signals. Cyclin D may therefore play a role in cellular responses to mitogenic signals.
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
An abundant 43-kDa mitogen-activated protein kinase kinase subtype with specificity for MITOGEN-ACTIVATED PROTEIN KINASE 1 and MITOGEN-ACTIVATED PROTEIN KINASE 3.
A cyclin G subtype that is constitutively expressed throughout the cell cycle. Cyclin G1 is considered a major transcriptional target of TUMOR SUPPRESSOR PROTEIN P53 and is highly induced in response to DNA damage.
A cyclin subtype that is found associated with CYCLIN-DEPENDENT KINASE 5; cyclin G associated kinase, and PROTEIN PHOSPHATASE 2.
A large family of regulatory proteins that function as accessory subunits to a variety of CYCLIN-DEPENDENT KINASES. They generally function as ENZYME ACTIVATORS that drive the CELL CYCLE through transitions between phases. A subset of cyclins may also function as transcriptional regulators.
A cyclin subtype that binds to the CYCLIN-DEPENDENT KINASE 3 and CYCLIN-DEPENDENT KINASE 8. Cyclin C plays a dual role as a transcriptional regulator and a G1 phase CELL CYCLE regulator.
The property of emitting radiation while being irradiated. The radiation emitted is usually of longer wavelength than that incident or absorbed, e.g., a substance can be irradiated with invisible radiation and emit visible light. X-ray fluorescence is used in diagnosis.
Protein kinases that control cell cycle progression in all eukaryotes and require physical association with CYCLINS to achieve full enzymatic activity. Cyclin-dependent kinases are regulated by phosphorylation and dephosphorylation events.
A cyclin B subtype that colocalizes with GOLGI APPARATUS during INTERPHASE and is transported into the CELL NUCLEUS at the end of the G2 PHASE.
A cyclin subtype that is found associated with CYCLIN-DEPENDENT KINASE 9. Unlike traditional cyclins, which regulate the CELL CYCLE, type T cyclins appear to regulate transcription and are components of positive transcriptional elongation factor B.
A key regulator of CELL CYCLE progression. It partners with CYCLIN E to regulate entry into S PHASE and also interacts with CYCLIN A to phosphorylate RETINOBLASTOMA PROTEIN. Its activity is inhibited by CYCLIN-DEPENDENT KINASE INHIBITOR P27 and CYCLIN-DEPENDENT KINASE INHIBITOR P21.
An unusual cyclin subtype that is found highly expressed in terminally differentiated cells. Unlike conventional cyclins increased expression of cyclin G2 is believed to cause a withdrawal of cells from the CELL CYCLE.
A cyclin subtype that is found as a component of a heterotrimeric complex containing cyclin-dependent kinase 7 and CDK-activating kinase assembly factor. The complex plays a role in cellular proliferation by phosphorylating several CYCLIN DEPENDENT KINASES at specific regulatory threonine sites.
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
Cyclin-dependent kinase 4 is a key regulator of G1 PHASE of the CELL CYCLE. It partners with CYCLIN D to phosphorylate RETINOBLASTOMA PROTEIN. CDK4 activity is inhibited by CYCLIN-DEPENDENT KINASE INHIBITOR P16.
A family of cell cycle-dependent kinases that are related in structure to CDC28 PROTEIN KINASE; S CEREVISIAE; and the CDC2 PROTEIN KINASE found in mammalian species.
Phosphoprotein with protein kinase activity that functions in the G2/M phase transition of the CELL CYCLE. It is the catalytic subunit of the MATURATION-PROMOTING FACTOR and complexes with both CYCLIN A and CYCLIN B in mammalian cells. The maximal activity of cyclin-dependent kinase 1 is achieved when it is fully dephosphorylated.
The period of the CELL CYCLE preceding DNA REPLICATION in S PHASE. Subphases of G1 include "competence" (to respond to growth factors), G1a (entry into G1), G1b (progression), and G1c (assembly). Progression through the G1 subphases is effected by limiting growth factors, nutrients, or inhibitors.
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 cyclin-dependent kinase inhibitor that coordinates the activation of CYCLIN and CYCLIN-DEPENDENT KINASES during the CELL CYCLE. It interacts with active CYCLIN D complexed to CYCLIN-DEPENDENT KINASE 4 in proliferating cells, while in arrested cells it binds and inhibits CYCLIN E complexed to CYCLIN-DEPENDENT KINASE 2.
Phase of the CELL CYCLE following G1 and preceding G2 when the entire DNA content of the nucleus is replicated. It is achieved by bidirectional replication at multiple sites along each chromosome.
Product of the retinoblastoma tumor suppressor gene. It is a nuclear phosphoprotein hypothesized to normally act as an inhibitor of cell proliferation. Rb protein is absent in retinoblastoma cell lines. It also has been shown to form complexes with the adenovirus E1A protein, the SV40 T antigen, and the human papilloma virus E7 protein.
A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.
Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).
The B-cell leukemia/lymphoma-1 genes, associated with various neoplasms when overexpressed. Overexpression results from the t(11;14) translocation, which is characteristic of mantle zone-derived B-cell lymphomas. The human c-bcl-1 gene is located at 11q13 on the long arm of chromosome 11.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Cyclin-dependent kinase 6 associates with CYCLIN D and phosphorylates RETINOBLASTOMA PROTEIN during G1 PHASE of the CELL CYCLE. It helps regulate the transition to S PHASE and its kinase activity is inhibited by CYCLIN-DEPENDENT KINASE INHIBITOR P18.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A cyclin-dependent kinase inhibitor that mediates TUMOR SUPPRESSOR PROTEIN P53-dependent CELL CYCLE arrest. p21 interacts with a range of CYCLIN-DEPENDENT KINASES and associates with PROLIFERATING CELL NUCLEAR ANTIGEN and CASPASE 3.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
The period of the CELL CYCLE following DNA synthesis (S PHASE) and preceding M PHASE (cell division phase). The CHROMOSOMES are tetraploid in this point.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
Proteins that are normally involved in holding cellular growth in check. Deficiencies or abnormalities in these proteins may lead to unregulated cell growth and tumor development.
A cell line derived from cultured tumor cells.
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 family of basic helix-loop-helix transcription factors that control expression of a variety of GENES involved in CELL CYCLE regulation. E2F transcription factors typically form heterodimeric complexes with TRANSCRIPTION FACTOR DP1 or transcription factor DP2, and they have N-terminal DNA binding and dimerization domains. E2F transcription factors can act as mediators of transcriptional repression or transcriptional activation.
A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.
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.
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.
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)
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.
High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in neoplastic tissue.
Nuclear antigen with a role in DNA synthesis, DNA repair, and cell cycle progression. PCNA is required for the coordinated synthesis of both leading and lagging strands at the replication fork during DNA replication. PCNA expression correlates with the proliferation activity of several malignant and non-malignant cell types.
A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.
An aspect of protein kinase (EC 2.7.1.37) in which serine residues in protamines and histones are phosphorylated in the presence of ATP.
A quiescent state of cells during G1 PHASE.
Established cell cultures that have the potential to propagate indefinitely.
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.
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.
Protein kinase that drives both the mitotic and meiotic cycles in all eukaryotic organisms. In meiosis it induces immature oocytes to undergo meiotic maturation. In mitosis it has a role in the G2/M phase transition. Once activated by CYCLINS; MPF directly phosphorylates some of the proteins involved in nuclear envelope breakdown, chromosome condensation, spindle assembly, and the degradation of cyclins. The catalytic subunit of MPF is PROTEIN P34CDC2.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
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.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
A product of the p16 tumor suppressor gene (GENES, P16). It is also called INK4 or INK4A because it is the prototype member of the INK4 CYCLIN-DEPENDENT KINASE INHIBITORS. This protein is produced from the alpha mRNA transcript of the p16 gene. The other gene product, produced from the alternatively spliced beta transcript, is TUMOR SUPPRESSOR PROTEIN P14ARF. Both p16 gene products have tumor suppressor functions.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A transcription factor that possesses DNA-binding and E2F-binding domains but lacks a transcriptional activation domain. It is a binding partner for E2F TRANSCRIPTION FACTORS and enhances the DNA binding and transactivation function of the DP-E2F complex.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
A multifunctional CDC2 kinase-related kinase that plays roles in transcriptional elongation, CELL DIFFERENTIATION, and APOPTOSIS. It is found associated with CYCLIN T and is a component of POSITIVE TRANSCRIPTIONAL ELONGATION FACTOR B.
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.
Echinoderms having bodies of usually five radially disposed arms coalescing at the center.
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.
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 ubiquitously expressed regulatory protein that contains a retinoblastoma protein binding domain and an AT-rich interactive domain. The protein may play a role in recruiting HISTONE DEACETYLASES to the site of RETINOBLASTOMA PROTEIN-containing transcriptional repressor complexes.
Nuclear phosphoprotein encoded by the p53 gene (GENES, P53) whose normal function is to control CELL PROLIFERATION and APOPTOSIS. A mutant or absent p53 protein has been found in LEUKEMIA; OSTEOSARCOMA; LUNG CANCER; and COLORECTAL CANCER.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
An E2F transcription factor that interacts directly with RETINOBLASTOMA PROTEIN and CYCLIN A and activates GENETIC TRANSCRIPTION required for CELL CYCLE entry and DNA synthesis. E2F1 is involved in DNA REPAIR and APOPTOSIS.
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.
A negative regulator of the CELL CYCLE that undergoes PHOSPHORYLATION by CYCLIN-DEPENDENT KINASES. It contains a conserved pocket region that binds E2F4 TRANSCRIPTION FACTOR and interacts with viral ONCOPROTEINS such as POLYOMAVIRUS TUMOR ANTIGENS; ADENOVIRUS E1A PROTEINS; and PAPILLOMAVIRUS E7 PROTEINS.
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 sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).
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.
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 protein kinase encoded by the Saccharomyces cerevisiae CDC28 gene and required for progression from the G1 PHASE to the S PHASE in the CELL CYCLE.
A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
A group of cell cycle proteins that negatively regulate the activity of CYCLIN/CYCLIN-DEPENDENT KINASE complexes. They inhibit CELL CYCLE progression and help control CELL PROLIFERATION following GENOTOXIC STRESS as well as during CELL DIFFERENTIATION.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Tumors or cancer of the human BREAST.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).
A form of non-Hodgkin lymphoma having a usually diffuse pattern with both small and medium lymphocytes and small cleaved cells. It accounts for about 5% of adult non-Hodgkin lymphomas in the United States and Europe. The majority of mantle-cell lymphomas are associated with a t(11;14) translocation resulting in overexpression of the CYCLIN D1 gene (GENES, BCL-1).
A CELL CYCLE and tumor growth marker which can be readily detected using IMMUNOCYTOCHEMISTRY methods. Ki-67 is a nuclear antigen present only in the nuclei of cycling cells.
A continuous cell line of high contact-inhibition established from NIH Swiss mouse embryo cultures. The cells are useful for DNA transfection and transformation studies. (From ATCC [Internet]. Virginia: American Type Culture Collection; c2002 [cited 2002 Sept 26]. Available from http://www.atcc.org/)
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.
A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells.
Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.
Cell changes manifested by escape from control mechanisms, increased growth potential, alterations in the cell surface, karyotypic abnormalities, morphological and biochemical deviations from the norm, and other attributes conferring the ability to invade, metastasize, and kill.
Cellular DNA-binding proteins encoded by the c-myc genes. They are normally involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Elevated and deregulated (constitutive) expression of c-myc proteins can cause tumorigenesis.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
A CYCLIN C dependent kinase that is an important component of the mediator complex. The enzyme is activated by its interaction with CYCLIN C and plays a role in transcriptional regulation by phosphorylating RNA POLYMERASE II.
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 large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
The process by which a DNA molecule is duplicated.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Cdh1 is an activator of the anaphase-promoting complex-cyclosome, and is involved in substrate recognition. It associates with the complex in late MITOSIS from anaphase through G1 to regulate activity of CYCLIN-DEPENDENT KINASES and to prevent premature DNA replication.
A cyclin-dependent kinase that forms a complex with CYCLIN C and is active during the G1 PHASE of the CELL CYCLE. It plays a role in the transition from G1 to S PHASE and in transcriptional regulation.
Elements of limited time intervals, contributing to particular results or situations.
Transport proteins that carry specific substances in the blood or across cell membranes.
Cellular proteins encoded by the c-mos genes (GENES, MOS). They function in the cell cycle to maintain MATURATION PROMOTING FACTOR in the active state and have protein-serine/threonine kinase activity. Oncogenic transformation can take place when c-mos proteins are expressed at the wrong time.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
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.
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 interval between two successive CELL DIVISIONS during which the CHROMOSOMES are not individually distinguishable. It is composed of the G phases (G1 PHASE; G0 PHASE; G2 PHASE) and S PHASE (when DNA replication occurs).
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.
Regulatory signaling systems that control the progression through the CELL CYCLE. They ensure that the cell has completed, in the correct order and without mistakes, all the processes required to replicate the GENOME and CYTOPLASM, and divide them equally between two daughter cells. If cells sense they have not completed these processes or that the environment does not have the nutrients and growth hormones in place to proceed, then the cells are restrained (or "arrested") until the processes are completed and growth conditions are suitable.
A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
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.
The phase of cell nucleus division following PROMETAPHASE, in which the CHROMOSOMES line up across the equatorial plane of the SPINDLE APPARATUS prior to separation.
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.

Cyclin I protects podocytes from apoptosis. (1/7)

The limited regenerative capacity of the glomerular podocyte following injury underlies the development of glomerulosclerosis and progressive renal failure in a diverse range of kidney diseases. We discovered that, in the kidney, cyclin I is uniquely expressed in the glomerular podocyte, and have constructed cyclin I knock-out mice to explore the biological function of cyclin I in these cells. Cyclin I knock-out (-/-) podocytes showed an increased susceptibility to apoptosis both in vitro and in vivo. Following induction of experimental glomerulonephritis, podocyte apoptosis was increased 4-fold in the cyclin I -/- mice, which was associated with dramatically decreased renal function. Our previous data showed that the Cdk inhibitor p21(Cip1/Waf1) protects podocytes from certain apoptotic stimuli. In cultured cyclin I -/- podocytes, the level of p21(Cip1/Waf1) was lower at base line, had a shorter half-life, and declined more rapidly in response to apoptotic stimuli than in wild-type cells. Enforced expression of p21(Cip1/Waf1) reversed the susceptibility of cyclin I -/- podocytes to apoptosis. Cyclin I protects podocytes from apoptosis, and we provide preliminary data to suggest that this is mediated by stabilization of p21(Cip1/Waf1).  (+info)

Serum proteomic-based analysis of pancreatic carcinoma for the identification of potential cancer biomarkers. (2/7)

To identify new biomarkers that improve the early diagnosis and lead to possible therapeutic targets in pancreatic carcinoma, we performed a proteomic approach to compare serum protein expression patterns of pancreatic carcinoma patients with that of gastric cancer patients, other pancreatic disease patients, and healthy volunteers. By two-dimensional gel electrophoresis (2-DE) analyses and mass spectroscopic identification, 10 protein spots were found significantly changed in pancreatic carcinoma and 5 proteins including cyclin I, Rab GDP dissociation inhibitor beta (GDI2), alpha-1 antitrypsin precursor, Haptoglobin precursor, and Serotransferrin precursor were successfully identified. The increased levels of cyclin I and GDI2 found to be associated with pancreatic carcinoma were further confirmed by Western blot analyses in an independent series of serum samples and/or pancreatic juice samples. Applying immunohistochemistry, we further validated expression of cyclin I and GDI2 in additional pancreatic carcinomas. These results indicate that cyclin I and GDI2 may be potential molecular targets for pancreatic cancer diagnostics and therapeutics.  (+info)

Microarray analysis of the cellular pathways involved in the adaptation to and progression of motor neuron injury in the SOD1 G93A mouse model of familial ALS. (3/7)

The cellular pathways of motor neuronal injury have been investigated in the SOD1 G93A murine model of familial amyotrophic lateral sclerosis (ALS) using laser-capture microdissection and microarray analysis. The advantages of this study include the following: analysis of changes specifically in motor neurons (MNs), while still detecting effects of interactions with neighboring cells; the ability to profile changes during disease progression, an approach not possible in human ALS; and the use of transgenic mice bred on a homogeneous genetic background, eliminating the confounding effects arising from a mixed genetic background. By using this rigorous approach, novel changes in key cellular pathways have been detected at both the presymptomatic and late stages, which have been validated by quantitative reverse transcription-PCR. At the presymptomatic stage (60 d), MNs extracted from SOD1 G93A mice show a significant increase in expression of genes subserving both transcriptional and translational functions, as well as lipid and carbohydrate metabolism, mitochondrial preprotein translocation, and respiratory chain function, suggesting activation of a strong cellular adaptive response. Mice 90 d old still show upregulation of genes involved in carbohydrate metabolism, whereas transcription and mRNA processing genes begin to show downregulation. Late in the disease course (120 d), important findings include the following: marked transcriptional repression, with downregulation of multiple transcripts involved in transcriptional and metabolic functions; upregulation of complement system components; and increased expression of key cyclins involved in cell-cycle regulation. The changes described in the motor neuron transcriptome evolving during the disease course highlight potential novel targets for neuroprotective therapeutic intervention.  (+info)

Cyclin I activates Cdk5 and regulates expression of Bcl-2 and Bcl-XL in postmitotic mouse cells. (4/7)

 (+info)

Cyclin I-Cdk5 governs survival in post-mitotic cells. (5/7)

Cdk5 has long been recognized to play an important role in development, maturation and apoptosis of postmitotic and terminally differentiated cells. Activation of Cdk5 is tightly regulated by specific activators. Cyclin I was recently characterized as the first cyclin protein that binds to and activates Cdk5. Cyclin I-Cdk5 activates the MEK-ERK pathway and results in increased Bcl-2 and Bcl-X(L) mRNA and protein levels. Lack of Cyclin I renders podocytes more susceptible to apoptosis. Interestingly, activation of Cdk5 by p35 is also involved in the podocytes' response to injury. In the absence of p35, podocytes are more prone to undergo apoptosis. Here, we propose a new model where Cdk5 plays a central role in the cellular response machinery against injury-induced apoptosis of post-mitotic cells. While Cyclin I-Cdk5 regulates Bcl-2 family proteins through activation of the MEK-ERK pathway, p35-Cdk5 directly phosphorylates and stabilizes Bcl-2.  (+info)

Both cyclin I and p35 are required for maximal survival benefit of cyclin-dependent kinase 5 in kidney podocytes. (6/7)

 (+info)

Cyclin I is involved in the regulation of cell cycle progression. (7/7)

 (+info)

I'm sorry for any confusion, but a specific medical definition for 'Cyclin I' could not be found. Cyclins are a family of proteins that regulate the cell cycle in cells. They are so named because their levels fluctuate or cycle during different phases of the cell cycle. However, there is no specific cyclin referred to as "Cyclin I" in current medical and scientific literature.

There is a protein called "cyclin I" found in some organisms like Drosophila melanogaster (fruit flies), but it doesn't have a well-established role or equivalent in human cell cycle regulation. Therefore, it may not be relevant to provide a medical definition for a protein that is not directly involved in human physiology or pathophysiology.

Cyclin D1 is a type of cyclin protein that plays a crucial role in the regulation of the cell cycle, which is the process by which cells divide and grow. Specifically, Cyclin D1 is involved in the transition from the G1 phase to the S phase of the cell cycle. It does this by forming a complex with and acting as a regulatory subunit of cyclin-dependent kinase 4 (CDK4) or CDK6, which phosphorylates and inactivates the retinoblastoma protein (pRb). This allows the E2F transcription factors to be released and activate the transcription of genes required for DNA replication and cell cycle progression.

Overexpression of Cyclin D1 has been implicated in the development of various types of cancer, as it can lead to uncontrolled cell growth and division. Therefore, Cyclin D1 is an important target for cancer therapy, and inhibitors of CDK4/6 have been developed to treat certain types of cancer that overexpress Cyclin D1.

Cyclin A is a type of cyclin protein that regulates the progression of the cell cycle, particularly through the G1 and S phases. It forms a complex with and acts as a regulatory subunit for cyclin-dependent kinases (CDKs), specifically CDK2 and CDK1. The activation of Cyclin A-CDK complexes leads to phosphorylation of various target proteins, which in turn regulates DNA replication and the transition to mitosis.

Cyclin A levels rise during the late G1 phase and peak during the S phase, after which they decline rapidly during the G2 phase. Any abnormalities in Cyclin A regulation or expression can contribute to uncontrolled cell growth and cancer development.

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

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

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

Cyclin E is a type of cyclin protein that plays a crucial role in the regulation of the cell cycle, particularly during the G1 phase and the transition to the S phase. It functions as a regulatory subunit of the Cyclin-dependent kinase 2 (CDK2) complex, which is responsible for promoting the progression of the cell cycle.

Cyclin E is synthesized during the late G1 phase of the cell cycle and accumulates to high levels until it forms a complex with CDK2. The Cyclin E-CDK2 complex then phosphorylates several target proteins, leading to the activation of various downstream pathways that promote DNA replication and cell cycle progression.

The regulation of Cyclin E expression and activity is tightly controlled through multiple mechanisms, including transcriptional regulation, protein stability, and proteasomal degradation. Dysregulation of Cyclin E has been implicated in various human cancers, including breast, ovarian, and lung cancer, due to its role in promoting uncontrolled cell proliferation and genomic instability.

Podocytes are specialized cells that make up the visceral epithelial layer of the glomerular basement membrane in the kidney. They have long, interdigitating foot processes that wrap around the capillaries of the glomerulus and play a crucial role in maintaining the filtration barrier of the kidney. The slit diaphragms between the foot processes allow for the passage of small molecules while retaining larger proteins in the bloodstream. Podocytes also contribute to the maintenance and regulation of the glomerular filtration rate, making them essential for normal renal function. Damage or loss of podocytes can lead to proteinuria and kidney disease.

Cyclin B is a type of cyclin protein that regulates the cell cycle, specifically the transition from G2 phase to mitosis (M phase) in eukaryotic cells. Cyclin B binds and activates cyclin-dependent kinase 1 (CDK1), forming the complex known as M-phase promoting factor (MPF). This complex triggers the events leading to cell division, such as chromosome condensation, nuclear envelope breakdown, and spindle formation. The levels of cyclin B increase during the G2 phase and are degraded by the anaphase-promoting complex/cyclosome (APC/C) at the onset of anaphase, allowing the cell cycle to progress into the next phase.

Cyclin B1 is a type of cyclin protein that regulates the cell cycle, specifically the transition from G2 phase to mitosis (M phase) in eukaryotic cells. It forms a complex with and acts as a regulatory subunit of cyclin-dependent kinase 1 (CDK1), also known as CDC2. During the G2 phase, Cyclin B1 levels accumulate and upon reaching a certain threshold, it binds to CDK1 to form the maturation promoting factor (MPF). The activation of MPF triggers the onset of mitosis by promoting nuclear envelope breakdown, chromosome condensation, and other events required for cell division. After the completion of mitosis, Cyclin B1 is degraded by the ubiquitin-proteasome system, allowing the cell cycle to progress back into G1 phase.

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

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

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

Cyclin D2 is a type of cyclin protein that regulates the cell cycle, particularly in the G1 phase. It forms a complex with and acts as a regulatory subunit of cyclin-dependent kinase 4 (CDK4) or CDK6, promoting the transition from G1 to S phase of the cell cycle. The expression of cyclin D2 is regulated by various growth factors, hormones, and oncogenes, and its dysregulation has been implicated in the development of several types of cancer.

Cyclin D3 is a type of cyclin protein that regulates the cell cycle, particularly during the G1 phase. It forms a complex with and acts as a regulatory subunit of CDK4 or CDK6, which are cyclin-dependent kinases. This complex plays a crucial role in phosphorylating and inactivating the retinoblastoma protein (pRb), leading to the release of E2F transcription factors that promote the expression of genes required for DNA replication and cell cycle progression into the S phase.

Cyclin D3 is primarily expressed in activated lymphocytes and is essential for normal immune function, as well as in certain tissues during development. Alterations in CYCLIN D3 gene expression or function have been implicated in several types of cancer, such as leukemias and lymphomas, due to their role in uncontrolled cell proliferation.

Cyclin A1 is a type of cyclin protein that regulates the cell cycle, particularly during the S and G2 phases. It forms a complex with and acts as a regulatory subunit of cyclin-dependent kinase 2 (CDK2), helping to control the transition from the G1 phase to the S phase and from the S phase to the G2 phase. Cyclin A1 is expressed in various tissues, including ovary, testis, bone marrow, and lymphoid cells. Overexpression or dysregulation of cyclin A1 has been implicated in several types of cancer, making it a potential target for cancer therapy.

Cyclin A2 is a type of cyclin protein that regulates the cell cycle, which is the series of events that cells undergo as they grow and divide. Specifically, Cyclin A2 plays a role in the progression from the G1 phase to the S phase (DNA synthesis phase) and from the G2 phase to the M phase (mitosis phase) of the cell cycle. It does this by binding to and activating cyclin-dependent kinases (CDKs), which are enzymes that help regulate the cell cycle.

Cyclin A2 is expressed at various points during the cell cycle, but its levels peak during the S and G2 phases. The protein is degraded during mitosis, ensuring that it is not present in excess during the next cell cycle. Dysregulation of Cyclin A2 has been implicated in the development of cancer, as uncontrolled cell growth and division are hallmarks of this disease.

Cyclin D is a type of cyclin protein that plays a crucial role in the regulation of the cell cycle, which is the process by which cells grow and divide. Specifically, Cyclin D is involved in the G1 phase of the cell cycle and works in conjunction with its partner enzyme, cyclin-dependent kinase 4 (CDK4) or CDK6, to phosphorylate and regulate the activity of several key proteins that control the transition from G1 to S phase.

There are several different types of Cyclin D proteins, including Cyclin D1, Cyclin D2, and Cyclin D3, which are encoded by different genes but share similar structures and functions. Overexpression or dysregulation of Cyclin D has been implicated in the development of various human cancers, as it can lead to uncontrolled cell growth and division. Therefore, understanding the role of Cyclin D in the cell cycle and its regulation is important for developing potential cancer therapies.

Proteolysis is the biological process of breaking down proteins into smaller polypeptides or individual amino acids by the action of enzymes called proteases. This process is essential for various physiological functions, including digestion, protein catabolism, cell signaling, and regulation of numerous biological activities. Dysregulation of proteolysis can contribute to several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

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

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

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

Cyclin G1 is a type of protein that belongs to the cyclin family, which are involved in the regulation of the cell cycle. The cell cycle is the series of events that take place as a cell grows, copies its DNA, and divides into two daughter cells.

Cyclin G1 regulates the cell cycle by interacting with various cyclin-dependent kinases (CDKs), which are enzymes that help control the progression of the cell cycle. Specifically, Cyclin G1 has been shown to inhibit the activity of CDK1 and CDK2, which play important roles in regulating the transition from the G1 phase to the S phase of the cell cycle.

Cyclin G1 has also been implicated in other cellular processes, including DNA damage repair, apoptosis (programmed cell death), and tumor suppression. Dysregulation of Cyclin G1 has been linked to various types of cancer, making it a potential target for cancer therapy.

Cyclin G is a type of protein that belongs to the cyclin family, which are involved in the regulation of the cell cycle. The human Cyclin G gene encodes two isoforms, Cyclin G1 and Cyclin G2, which share a similar structure but have different functions.

Cyclin G1 is known to play a role in the negative regulation of the cell cycle, particularly during the G1 phase. It interacts with several proteins, including CDKs (cyclin-dependent kinases), to regulate the activity of various transcription factors and other signaling pathways that control cell growth and division.

Cyclin G2, on the other hand, has been implicated in the regulation of DNA damage response and apoptosis (programmed cell death). It interacts with CDKs and other proteins to modulate the activity of various signaling pathways involved in these processes.

Overall, Cyclin G plays important roles in regulating cell cycle progression, DNA damage response, and apoptosis, and its dysregulation has been linked to several human diseases, including cancer.

Cyclins are a family of regulatory proteins that play a crucial role in the cell cycle, which is the series of events that take place as a cell grows, divides, and produces two daughter cells. They are called cyclins because their levels fluctuate or cycle during the different stages of the cell cycle.

Cyclins function as subunits of serine/threonine protein kinase complexes, forming an active enzyme that adds phosphate groups to other proteins, thereby modifying their activity. This post-translational modification is a critical mechanism for controlling various cellular processes, including the regulation of the cell cycle.

There are several types of cyclins (A, B, D, and E), each of which is active during specific phases of the cell cycle:

1. Cyclin D: Expressed in the G1 phase, it helps to initiate the cell cycle by activating cyclin-dependent kinases (CDKs) that promote progression through the G1 restriction point.
2. Cyclin E: Active during late G1 and early S phases, it forms a complex with CDK2 to regulate the transition from G1 to S phase, where DNA replication occurs.
3. Cyclin A: Expressed in the S and G2 phases, it associates with both CDK2 and CDK1 to control the progression through the S and G2 phases and entry into mitosis (M phase).
4. Cyclin B: Active during late G2 and M phases, it partners with CDK1 to regulate the onset of mitosis by controlling the breakdown of the nuclear envelope, chromosome condensation, and spindle formation.

The activity of cyclins is tightly controlled through several mechanisms, including transcriptional regulation, protein degradation, and phosphorylation/dephosphorylation events. Dysregulation of cyclin expression or function can lead to uncontrolled cell growth and proliferation, which are hallmarks of cancer.

Cyclin C is a type of cyclin protein that plays a crucial role in the regulation of the cell cycle, which is the process by which cells grow and divide. Specifically, Cyclin C is involved in the transition from the G1 phase to the S phase of the cell cycle, during which DNA replication occurs.

Cyclin C forms a complex with cyclin-dependent kinase 8 (CDK8) and other regulatory subunits to form the CDK8 module, which is part of the mediator complex that regulates gene transcription. The activity of Cyclin C/CDK8 is regulated by various mechanisms, including phosphorylation and degradation, to ensure proper control of the cell cycle and prevent uncontrolled cell growth and division.

Mutations in the gene encoding Cyclin C have been associated with certain types of cancer, highlighting its importance in maintaining genomic stability and preventing tumorigenesis.

Fluorescence is not a medical term per se, but it is widely used in the medical field, particularly in diagnostic tests, medical devices, and research. Fluorescence is a physical phenomenon where a substance absorbs light at a specific wavelength and then emits light at a longer wavelength. This process, often referred to as fluorescing, results in the emission of visible light that can be detected and measured.

In medical terms, fluorescence is used in various applications such as:

1. In-vivo imaging: Fluorescent dyes or probes are introduced into the body to highlight specific structures, cells, or molecules during imaging procedures. This technique can help doctors detect and diagnose diseases such as cancer, inflammation, or infection.
2. Microscopy: Fluorescence microscopy is a powerful tool for visualizing biological samples at the cellular and molecular level. By labeling specific proteins, nucleic acids, or other molecules with fluorescent dyes, researchers can observe their distribution, interactions, and dynamics within cells and tissues.
3. Surgical guidance: Fluorescence-guided surgery is a technique where surgeons use fluorescent markers to identify critical structures such as blood vessels, nerves, or tumors during surgical procedures. This helps ensure precise and safe surgical interventions.
4. Diagnostic tests: Fluorescence-based assays are used in various diagnostic tests to detect and quantify specific biomarkers or analytes. These assays can be performed using techniques such as enzyme-linked immunosorbent assay (ELISA), polymerase chain reaction (PCR), or flow cytometry.

In summary, fluorescence is a physical process where a substance absorbs and emits light at different wavelengths. In the medical field, this phenomenon is harnessed for various applications such as in-vivo imaging, microscopy, surgical guidance, and diagnostic tests.

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

Cyclin B2 is a type of cyclin protein that regulates the cell cycle, particularly at the G2 phase and the beginning of mitosis. It forms a complex with and acts as a regulatory subunit of cyclin-dependent kinase 1 (CDK1), which plays a crucial role in the transition from G2 phase to mitosis. The expression and activity of Cyclin B2 are tightly regulated during the cell cycle, and its dysregulation can lead to abnormal cell division and contribute to the development of cancer.

Cyclin T is a type of cyclin protein that is encoded by the CCNT2 gene in humans. Cyclins are a family of regulatory proteins that play a crucial role in the cell cycle, which is the series of events that cells undergo as they grow and divide. Specifically, cyclin T is a component of the CDK9/cyclin T complex, also known as positive transcription elongation factor b (P-TEFb), which plays a key role in regulating gene expression by controlling the elongation phase of RNA polymerase II-mediated transcription.

Cyclin T is expressed at various stages of the cell cycle and has been shown to interact with several other proteins involved in cell cycle regulation, including the retinoblastoma protein (pRb) and the E2F family of transcription factors. Dysregulation of cyclin T expression or activity has been implicated in several human diseases, including cancer.

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

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

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

Cyclin G2 is a type of protein that belongs to the cyclin family, which are involved in the regulation of the cell cycle. The cell cycle is the series of events that cells undergo as they grow and divide. Specifically, Cyclin G2 regulates the G1 phase of the cell cycle, which is the phase where the cell prepares to divide.

Cyclin G2 has been found to play a role in several important cellular processes, including DNA damage response, apoptosis (programmed cell death), and differentiation. It has also been implicated in the development of certain diseases, such as cancer. For example, Cyclin G2 has been shown to have tumor-suppressive functions, and its expression is often reduced in cancer cells.

In summary, Cyclin G2 is a regulatory protein that plays a critical role in controlling the cell cycle and maintaining genomic stability. Its dysregulation has been associated with various diseases, including cancer.

Cyclin H is a type of protein that is classified as a cyclin, which is a regulatory subunit of cyclin-dependent kinases (CDKs). Specifically, Cyclin H forms a complex with CDK7 and functions as an essential component of the cell cycle transcriptional coactivator known as TFIIH.

TFIIH plays a crucial role in the initiation of transcription by RNA polymerase II and also participates in the process of DNA repair. The Cyclin H-CDK7 complex phosphorylates the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II, which is a critical step in the transcription cycle. Additionally, Cyclin H-CDK7 also plays a role in regulating the cell cycle by controlling the activity of certain cell cycle regulators, such as E2F transcription factors.

Mutations in the gene that encodes Cyclin H have been associated with certain human diseases, including a rare inherited disorder called Cockayne syndrome, which is characterized by developmental abnormalities, neurological dysfunction, and premature aging.

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

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

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

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

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

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

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

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

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

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

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

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

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

The G1 phase, or Gap 1 phase, is the first phase of the cell cycle, during which the cell grows in size and synthesizes mRNA and proteins in preparation for subsequent steps leading to mitosis. During this phase, the cell also checks its growth and makes sure that it is large enough to proceed through the cell cycle. If the cell is not large enough, it will arrest in the G1 phase until it has grown sufficiently. The G1 phase is followed by the S phase, during which DNA replication occurs.

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

The major groups of cell cycle proteins include:

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

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

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

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

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

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

In the context of cell biology, "S phase" refers to the part of the cell cycle during which DNA replication occurs. The "S" stands for synthesis, reflecting the active DNA synthesis that takes place during this phase. It is preceded by G1 phase (gap 1) and followed by G2 phase (gap 2), with mitosis (M phase) being the final stage of the cell cycle.

During S phase, the cell's DNA content effectively doubles as each chromosome is replicated to ensure that the two resulting daughter cells will have the same genetic material as the parent cell. This process is carefully regulated and coordinated with other events in the cell cycle to maintain genomic stability.

Retinoblastoma Protein (pRb or RB1) is a tumor suppressor protein that plays a critical role in regulating the cell cycle and preventing uncontrolled cell growth. It is encoded by the RB1 gene, located on chromosome 13. The retinoblastoma protein functions as a regulatory checkpoint in the cell cycle, preventing cells from progressing into the S phase (DNA synthesis phase) until certain conditions are met.

When pRb is in its active state, it binds to and inhibits the activity of E2F transcription factors, which promote the expression of genes required for DNA replication and cell cycle progression. Phosphorylation of pRb by cyclin-dependent kinases (CDKs) leads to the release of E2F factors, allowing them to activate their target genes and drive the cell into S phase.

Mutations in the RB1 gene can result in the production of a nonfunctional or reduced amount of pRb protein, leading to uncontrolled cell growth and an increased risk of developing retinoblastoma, a rare form of eye cancer, as well as other types of tumors.

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

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

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

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

Oncogene proteins are derived from oncogenes, which are genes that have the potential to cause cancer. Normally, these genes help regulate cell growth and division, but when they become altered or mutated, they can become overactive and lead to uncontrolled cell growth and division, which is a hallmark of cancer. Oncogene proteins can contribute to tumor formation and progression by promoting processes such as cell proliferation, survival, angiogenesis, and metastasis. Examples of oncogene proteins include HER2/neu, EGFR, and BCR-ABL.

BCL-1 (B-cell leukemia/lymphoma 1) is not a gene itself but rather a chromosomal translocation that results in the formation of an abnormal fusion gene. The BCL-1 translocation, also known as t(14;18)(q32;q21), is most commonly found in follicular lymphoma, a type of slow-growing non-Hodgkin lymphoma.

The BCL-1 translocation involves the juxtaposition of the BCL-2 gene, which is located on chromosome 18, with the IGH (immunoglobulin heavy chain) gene, which is located on chromosome 14. This translocation results in the overexpression of the BCL-2 protein, which inhibits apoptosis or programmed cell death. The overexpression of BCL-2 leads to the accumulation of cancer cells and contributes to the development and progression of follicular lymphoma.

It is important to note that while BCL-1 is a chromosomal translocation, it can also refer to the protein encoded by the BCL-2 gene when it is overexpressed due to the t(14;18) translocation. In this context, BCL-1 is considered a proto-oncogene because its overexpression promotes cancer development and progression.

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

Cyclin-Dependent Kinase 6 (CDK6) is a type of enzyme known as a protein kinase, which adds phosphate groups to other proteins in the cell. CDK6 is primarily involved in regulating the cell cycle, the process by which cells divide and grow.

CDK6 functions by binding to cyclin proteins, forming active complexes that help drive the progression of the cell cycle from one phase to the next. Specifically, CDK6 plays a crucial role in the transition from the G1 phase to the S phase of the cell cycle, where DNA replication occurs.

CDK6 activity is tightly regulated by various mechanisms, including phosphorylation and dephosphorylation, as well as by binding to inhibitory proteins such as p16INK4a and p21CIP1. Dysregulation of CDK6 has been implicated in the development of several types of cancer, making it a potential target for cancer therapy.

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

Cyclin-dependent kinase inhibitor p21, also known as CDKN1A or p21/WAF1/CIP1, is a protein that regulates the cell cycle. It inhibits the activity of cyclin-dependent kinases (CDKs), which are enzymes that play crucial roles in controlling the progression of the cell cycle.

The binding of p21 to CDKs prevents the phosphorylation and activation of downstream targets, leading to cell cycle arrest. This protein is transcriptionally activated by tumor suppressor protein p53 in response to DNA damage or other stress signals, and it functions as an important mediator of p53-dependent growth arrest.

By inhibiting CDKs, p21 helps to ensure that cells do not proceed through the cell cycle until damaged DNA has been repaired, thereby preventing the propagation of potentially harmful mutations. Additionally, p21 has been implicated in other cellular processes such as apoptosis, differentiation, and senescence. Dysregulation of p21 has been associated with various human diseases, including cancer.

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

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

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

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

The G2 phase, also known as the "gap 2 phase," is a stage in the cell cycle that occurs after DNA replication (S phase) and before cell division (mitosis). During this phase, the cell prepares for mitosis by completing the synthesis of proteins and organelles needed for chromosome separation. The cell also checks for any errors or damage to the DNA before entering mitosis. This phase is a critical point in the cell cycle where proper regulation ensures the faithful transmission of genetic information from one generation of cells to the next. If significant DNA damage is detected during G2, the cell may undergo programmed cell death (apoptosis) instead of dividing.

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

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

Tumor suppressor proteins are a type of regulatory protein that helps control the cell cycle and prevent cells from dividing and growing in an uncontrolled manner. They work to inhibit tumor growth by preventing the formation of tumors or slowing down their progression. These proteins can repair damaged DNA, regulate gene expression, and initiate programmed cell death (apoptosis) if the damage is too severe for repair.

Mutations in tumor suppressor genes, which provide the code for these proteins, can lead to a decrease or loss of function in the resulting protein. This can result in uncontrolled cell growth and division, leading to the formation of tumors and cancer. Examples of tumor suppressor proteins include p53, Rb (retinoblastoma), and BRCA1/2.

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

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

E2F transcription factors are a family of proteins that play crucial roles in the regulation of the cell cycle, DNA repair, and apoptosis (programmed cell death). These factors bind to specific DNA sequences called E2F responsive elements, located in the promoter regions of target genes. They can act as either transcriptional activators or repressors, depending on which E2F family member is involved, the presence of co-factors, and the phase of the cell cycle.

The E2F family consists of eight members, divided into two groups based on their functions: activator E2Fs (E2F1, E2F2, and E2F3a) and repressor E2Fs (E2F3b, E2F4, E2F5, E2F6, and E2F7). Activator E2Fs promote the expression of genes required for cell cycle progression, DNA replication, and repair. Repressor E2Fs, on the other hand, inhibit the transcription of these same genes as well as genes involved in differentiation and apoptosis.

Dysregulation of E2F transcription factors has been implicated in various human diseases, including cancer. Overexpression or hyperactivation of activator E2Fs can lead to uncontrolled cell proliferation and tumorigenesis, while loss of function or inhibition of repressor E2Fs can result in impaired differentiation and increased susceptibility to malignancies. Therefore, understanding the roles and regulation of E2F transcription factors is essential for developing novel therapeutic strategies against cancer and other diseases associated with cell cycle dysregulation.

CDC25 phosphatases are a group of enzymes that play crucial roles in the regulation of the cell cycle, which is the series of events that cells undergo as they grow and divide. Specifically, CDC25 phosphatases function to remove inhibitory phosphates from certain cyclin-dependent kinases (CDKs), thereby activating them and allowing the cell cycle to progress.

There are three main types of CDC25 phosphatases in humans, known as CDC25A, CDC25B, and CDC25C. These enzymes are named after the original yeast homolog, called Cdc25, which was discovered to be essential for cell cycle progression.

CDC25 phosphatases are tightly regulated during the cell cycle, with their activity being controlled by various mechanisms such as phosphorylation, protein-protein interactions, and subcellular localization. Dysregulation of CDC25 phosphatases has been implicated in several human diseases, including cancer, where they can contribute to uncontrolled cell growth and division. Therefore, understanding the functions and regulation of CDC25 phosphatases is an important area of research in molecular biology and medicine.

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

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

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

Examples of proto-oncogene proteins include:

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

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

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

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

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

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

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

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

Medical Definition:
Microtubule-associated proteins (MAPs) are a diverse group of proteins that bind to microtubules, which are key components of the cytoskeleton in eukaryotic cells. MAPs play crucial roles in regulating microtubule dynamics and stability, as well as in mediating interactions between microtubules and other cellular structures. They can be classified into several categories based on their functions, including:

1. Microtubule stabilizers: These MAPs promote the assembly of microtubules and protect them from disassembly by enhancing their stability. Examples include tau proteins and MAP2.
2. Microtubule dynamics regulators: These MAPs modulate the rate of microtubule polymerization and depolymerization, allowing for dynamic reorganization of the cytoskeleton during cell division and other processes. Examples include stathmin and XMAP215.
3. Microtubule motor proteins: These MAPs use energy from ATP hydrolysis to move along microtubules, transporting various cargoes within the cell. Examples include kinesin and dynein.
4. Adapter proteins: These MAPs facilitate interactions between microtubules and other cellular structures, such as membranes, organelles, or signaling molecules. Examples include MAP4 and CLASPs.

Dysregulation of MAPs has been implicated in several diseases, including neurodegenerative disorders like Alzheimer's disease (where tau proteins form abnormal aggregates called neurofibrillary tangles) and cancer (where altered microtubule dynamics can contribute to uncontrolled cell division).

Neoplastic gene expression regulation refers to the processes that control the production of proteins and other molecules from genes in neoplastic cells, or cells that are part of a tumor or cancer. In a normal cell, gene expression is tightly regulated to ensure that the right genes are turned on or off at the right time. However, in cancer cells, this regulation can be disrupted, leading to the overexpression or underexpression of certain genes.

Neoplastic gene expression regulation can be affected by a variety of factors, including genetic mutations, epigenetic changes, and signals from the tumor microenvironment. These changes can lead to the activation of oncogenes (genes that promote cancer growth and development) or the inactivation of tumor suppressor genes (genes that prevent cancer).

Understanding neoplastic gene expression regulation is important for developing new therapies for cancer, as targeting specific genes or pathways involved in this process can help to inhibit cancer growth and progression.

Proliferating Cell Nuclear Antigen (PCNA) is a protein that plays an essential role in the process of DNA replication and repair in eukaryotic cells. It functions as a cofactor for DNA polymerase delta, enhancing its activity during DNA synthesis. PCNA forms a sliding clamp around DNA, allowing it to move along the template and coordinate the actions of various enzymes involved in DNA metabolism.

PCNA is often used as a marker for cell proliferation because its levels increase in cells that are actively dividing or have been stimulated to enter the cell cycle. Immunostaining techniques can be used to detect PCNA and determine the proliferative status of tissues or cultures. In this context, 'proliferating' refers to the rapid multiplication of cells through cell division.

F-box proteins are a family of proteins that are characterized by the presence of an F-box domain, which is a motif of about 40-50 amino acids. This domain is responsible for binding to Skp1, a component of the SCF (Skp1-Cul1-F-box protein) E3 ubiquitin ligase complex. The F-box proteins serve as the substrate recognition subunit of this complex and are involved in targeting specific proteins for ubiquitination and subsequent degradation by the 26S proteasome.

There are multiple types of F-box proteins, including FBXW (also known as β-TrCP), FBXL, and FBLX, each with different substrate specificities. These proteins play important roles in various cellular processes such as cell cycle regulation, signal transduction, and DNA damage response by controlling the stability of key regulatory proteins.

Abnormal regulation of F-box proteins has been implicated in several human diseases, including cancer, developmental disorders, and neurodegenerative diseases.

I'm sorry for any confusion, but "Protamine Kinase" is not a widely recognized or established term in medical or biological sciences. Protamines are small, arginine-rich proteins found in the sperm cells of many organisms, and they play a crucial role in the packaging and protection of DNA during spermatogenesis.

Kinases, on the other hand, are enzymes that catalyze the transfer of phosphate groups from ATP to specific amino acids in proteins, thereby modulating their function, localization, or stability.

A search of scientific literature reveals only a few instances where "protamine kinase" is mentioned, usually in the context of potential regulatory mechanisms during sperm maturation or fertilization. However, there is no widely accepted or well-characterized enzyme known as "protamine kinase." Therefore, it would be challenging to provide a concise and accurate medical definition for this term.

G0 phase, also known as the resting phase or quiescent stage, is a part of the cell cycle in which cells are not actively preparing to divide. In this phase, cells are metabolically active and can carry out their normal functions, but they are not synthesizing DNA or dividing. Cells in G0 phase have left the cell cycle and may remain in this phase for an indefinite period of time, until they receive signals to re-enter the cell cycle and begin preparing for division again.

It's important to note that not all cells go through the G0 phase. Some cells, such as stem cells and certain types of immune cells, may spend most of their time in G0 phase and only enter the cell cycle when they are needed to replace damaged or dying cells. Other cells, such as those lining the digestive tract, continuously divide and do not have a G0 phase.

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

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

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

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

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

The Western blotting procedure involves several steps:

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

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

Maturation-Promoting Factor (MPF) is not a medical term per se, but it is commonly used in the field of cell biology and cancer research. MPF refers to a complex of two proteins that play a crucial role in regulating the cell cycle, specifically during the transition from the G2 phase to mitosis (M phase).

MPF is composed of a cyclin-dependent kinase (CDK1) and a regulatory subunit called cyclin B. During the late G2 phase, the levels of cyclin B increase, which leads to the activation of CDK1. Once activated, MPF triggers a series of events that promote mitosis, including chromosome condensation, nuclear envelope breakdown, and spindle formation.

In summary, Maturation-Promoting Factor (MPF) is a protein complex made up of CDK1 and cyclin B, which regulates the transition from the G2 phase to mitosis during the cell cycle.

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

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

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

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

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

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

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

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

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

Cyclin-Dependent Kinase Inhibitor p16, also known as CDKN2A or INK4a, is a protein that regulates the cell cycle. It functions as an inhibitor of cyclin-dependent kinases (CDKs) 4 and 6, which are enzymes that play a crucial role in regulating the progression of the cell cycle.

The p16 protein is produced in response to various signals, including DNA damage and oncogene activation, and its main function is to prevent the phosphorylation and activation of the retinoblastoma protein (pRb) by CDK4/6. When pRb is not phosphorylated, it binds to and inhibits the E2F transcription factor, which results in the suppression of genes required for cell cycle progression.

Therefore, p16 acts as a tumor suppressor protein by preventing the uncontrolled proliferation of cells that can lead to cancer. Mutations or deletions in the CDKN2A gene, which encodes the p16 protein, have been found in many types of human cancers, including lung, breast, and head and neck cancers.

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

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

Transcription factor DP1 (TFDP1) is not a specific medical term, but it is a term used in molecular biology and genetics. TFDP1 is a protein that functions as a transcription factor, which means it helps regulate the expression of genes by binding to specific DNA sequences and controlling the rate of transcription of those genes into messenger RNA (mRNA).

TFDP1 typically forms a complex with another transcription factor called E2F, and this complex plays a critical role in regulating the cell cycle and promoting cell division. TFDP1 can act as both a transcriptional activator and repressor, depending on which E2F family member it binds to and the specific context of the cell.

Mutations or dysregulation of TFDP1 have been implicated in various human diseases, including cancer. For example, overexpression of TFDP1 has been observed in several types of cancer, such as breast, lung, and prostate cancer, and is often associated with poor clinical outcomes. Therefore, understanding the role of TFDP1 in gene regulation and cellular processes may provide insights into the development of new therapeutic strategies for treating human diseases.

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

Cyclin-Dependent Kinase 9 (CDK9) is a type of serine/threonine protein kinase that plays a crucial role in the regulation of transcription. It forms a complex with cyclin T1, K or H and gets activated by phosphorylation. This complex, known as P-TEFb, is involved in the phosphorylation and activation of the C-terminal domain of RNA polymerase II, which is essential for the transcription elongation of most protein-coding genes. CDK9 also regulates other cellular processes such as apoptosis, differentiation, and cell cycle progression. Dysregulation of CDK9 has been implicated in various diseases including cancer.

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

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

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

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

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

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

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

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

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

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

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

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

Retinoblastoma-Binding Protein 1 (RBP1) is not a medical term itself, but it is a protein that has been studied in the context of cancer research, including retinoblastoma. According to scientific and medical literature, RBP1 is a protein that binds to the retinoblastoma protein (pRb), which is a tumor suppressor protein. The binding of RBP1 to pRb can influence the activity of this tumor suppressor and contribute to the regulation of the cell cycle and cell growth.

In the case of retinoblastoma, mutations in the RB1 gene, which encodes for the pRb protein, have been identified as a cause of this rare eye cancer in children. However, the role of RBP1 in retinoblastoma or other cancers is not well-defined and requires further research to fully understand its implications in disease development and potential therapeutic targets.

Tumor suppressor protein p53, also known as p53 or tumor protein p53, is a nuclear phosphoprotein that plays a crucial role in preventing cancer development and maintaining genomic stability. It does so by regulating the cell cycle and acting as a transcription factor for various genes involved in apoptosis (programmed cell death), DNA repair, and cell senescence (permanent cell growth arrest).

In response to cellular stress, such as DNA damage or oncogene activation, p53 becomes activated and accumulates in the nucleus. Activated p53 can then bind to specific DNA sequences and promote the transcription of target genes that help prevent the proliferation of potentially cancerous cells. These targets include genes involved in cell cycle arrest (e.g., CDKN1A/p21), apoptosis (e.g., BAX, PUMA), and DNA repair (e.g., GADD45).

Mutations in the TP53 gene, which encodes p53, are among the most common genetic alterations found in human cancers. These mutations often lead to a loss or reduction of p53's tumor suppressive functions, allowing cancer cells to proliferate uncontrollably and evade apoptosis. As a result, p53 has been referred to as "the guardian of the genome" due to its essential role in preventing tumorigenesis.

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

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

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

E2F1 is a member of the E2F family of transcription factors, which are involved in the regulation of cell cycle progression and apoptosis (programmed cell death). Specifically, E2F1 plays a role as a transcriptional activator, binding to specific DNA sequences and promoting the expression of genes required for the G1/S transition of the cell cycle.

In more detail, E2F1 forms a complex with a retinoblastoma protein (pRb) in the G0 and early G1 phases of the cell cycle. When pRb is phosphorylated by cyclin-dependent kinases during the late G1 phase, E2F1 is released and can then bind to its target DNA sequences and activate transcription of genes involved in DNA replication and cell cycle progression.

However, if E2F1 is overexpressed or activated inappropriately, it can also promote apoptosis, making it a key player in both cell proliferation and cell death pathways. Dysregulation of E2F1 has been implicated in the development of various human cancers, including breast, lung, and prostate cancer.

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

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

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

Retinoblastoma-like protein p107, also known as RBL1 or p107, is a tumor suppressor protein that belongs to the family of "pocket proteins." This protein is encoded by the RBL1 gene in humans. It plays a crucial role in regulating the cell cycle and preventing uncontrolled cell growth, which can lead to cancer.

The p107 protein is structurally similar to the retinoblastoma protein (pRb) and functions in a related manner. Both proteins interact with E2F transcription factors to control the expression of genes required for DNA replication and cell division. When the p107 protein is phosphorylated by cyclin-dependent kinases during the G1 phase of the cell cycle, it releases E2F transcription factors, allowing them to activate the transcription of target genes necessary for S phase entry and DNA replication.

Retinoblastoma-like protein p107 is often inactivated or mutated in various human cancers, including retinoblastoma, small cell lung cancer, and certain types of sarcomas. Loss of p107 function can lead to uncontrolled cell growth and tumor formation. However, it's important to note that the role of p107 in cancer development is complex and may depend on its interactions with other proteins and signaling pathways.

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

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

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

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

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

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

Ubiquitin-Protein Ligase Complexes, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or altering their function, localization, or interaction with other proteins.

The ubiquitination process involves three main steps:

1. Ubiquitin activation: Ubiquitin is activated by an E1 ubiquitin-activating enzyme in an ATP-dependent reaction.
2. Ubiquitin conjugation: The activated ubiquitin is then transferred to an E2 ubiquitin-conjugating enzyme.
3. Ubiquitin ligation: Finally, the E2 ubiquitin-conjugating enzyme interacts with a specific E3 ubiquitin ligase complex, which facilitates the transfer and ligation of ubiquitin to the target protein.

Ubiquitin-Protein Ligase Complexes are responsible for recognizing and binding to specific substrate proteins, ensuring that ubiquitination occurs on the correct targets. They can be divided into three main categories based on their structural features and mechanisms of action:

1. Really Interesting New Gene (RING) finger E3 ligases: These E3 ligases contain a RING finger domain, which directly interacts with both the E2 ubiquitin-conjugating enzyme and the substrate protein. They facilitate the transfer of ubiquitin from the E2 to the target protein by bringing them into close proximity.
2. Homologous to E6-AP C terminus (HECT) E3 ligases: These E3 ligases contain a HECT domain, which interacts with the E2 ubiquitin-conjugating enzyme and forms a thioester bond with ubiquitin before transferring it to the substrate protein.
3. RING-between-RING (RBR) E3 ligases: These E3 ligases contain both RING finger and HECT-like domains, which allow them to function similarly to both RING finger and HECT E3 ligases. They first form a thioester bond with ubiquitin using their RING1 domain before transferring it to the substrate protein via their RING2 domain.

Dysregulation of Ubiquitin-Protein Ligase Complexes has been implicated in various diseases, including cancer and neurodegenerative disorders. Understanding their mechanisms and functions can provide valuable insights into disease pathogenesis and potential therapeutic strategies.

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

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

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

Examples of recombinant fusion proteins include:

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

CDC28 protein kinase in Saccharomyces cerevisiae (Baker's yeast) is a crucial cell cycle regulator, specifically a cyclin-dependent kinase (CDK). It plays a pivotal role in controlling the G1 to S phase transition during the cell division cycle. CDC28 forms complexes with various cyclins, such as G1 cyclins CLN1, CLN2, and CLN3, and S phase cyclin CLB5, to regulate different stages of the cell cycle. The activity of CDC28 is tightly controlled through phosphorylation, dephosphorylation, and proteolysis of the cyclin subunits. Inhibition or mutation of CDC28 can lead to cell cycle arrest and various developmental defects in yeast.

S-phase kinase-associated proteins (Skp2) are a group of proteins that are associated with the S-phase kinase, which is a type of enzyme that helps to regulate the cell cycle. Specifically, Skp2 is involved in the ubiquitination and degradation of certain proteins that play a role in controlling the progression of the cell cycle.

Skp2 is a member of the F-box protein family, which are components of the Skp1-Cul1-F-box (SCF) complex, a type of E3 ubiquitin ligase. The SCF complex recognizes and binds to specific proteins, tagging them for ubiquitination and subsequent degradation by the proteasome.

One of the key targets of Skp2 is the tumor suppressor protein p27, which inhibits the activity of cyclin-dependent kinases (CDKs) and helps to regulate the transition from the G1 phase to the S phase of the cell cycle. By targeting p27 for degradation, Skp2 promotes the progression of the cell cycle and has been implicated in the development of various types of cancer.

Overall, Skp2 plays a critical role in regulating the cell cycle and has important implications for the development and treatment of various diseases, including cancer.

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

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

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

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

Cyclin-dependent kinase inhibitor proteins (CDKIs) are a family of regulatory proteins that play a crucial role in the control of the cell cycle. They function by binding to and inhibiting the activity of cyclin-dependent kinases (CDKs), which are serine/threonine protein kinases that help drive the progression of the cell cycle.

There are two main families of CDKIs: the Ink4 family and the Cip/Kip family. The Ink4 family members, including p16INK4a, p15INK4b, p18INK4c, and p19INK4d, specifically inhibit CDK4 and CDK6, preventing their association with cyclin D and thus blocking the transition from G1 to S phase of the cell cycle. The Cip/Kip family members, including p21CIP1, p27KIP1, and p57KIP2, inhibit a broader range of CDKs, including CDK1, CDK2, CDK4, and CDK6, and can regulate multiple stages of the cell cycle.

CDKIs play important roles in various biological processes, such as cell growth, differentiation, and apoptosis. Dysregulation of CDKI function has been implicated in several human diseases, including cancer, where loss or mutation of CDKIs can lead to uncontrolled cell proliferation and tumorigenesis. Therefore, CDKIs are attractive targets for the development of anti-cancer therapies.

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

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

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

Breast neoplasms refer to abnormal growths in the breast tissue that can be benign or malignant. Benign breast neoplasms are non-cancerous tumors or growths, while malignant breast neoplasms are cancerous tumors that can invade surrounding tissues and spread to other parts of the body.

Breast neoplasms can arise from different types of cells in the breast, including milk ducts, milk sacs (lobules), or connective tissue. The most common type of breast cancer is ductal carcinoma, which starts in the milk ducts and can spread to other parts of the breast and nearby structures.

Breast neoplasms are usually detected through screening methods such as mammography, ultrasound, or MRI, or through self-examination or clinical examination. Treatment options for breast neoplasms depend on several factors, including the type and stage of the tumor, the patient's age and overall health, and personal preferences. Treatment may include surgery, radiation therapy, chemotherapy, hormone therapy, or targeted therapy.

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

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

Mantle cell lymphoma (MCL) is a type of non-Hodgkin lymphoma (NHL), which is a cancer of the lymphatic system. Specifically, MCL arises from abnormal B-lymphocytes (a type of white blood cell) that typically reside in the "mantle zone" of the lymph node. The malignant cells in MCL tend to have a characteristic genetic abnormality where the cyclin D1 gene is translocated to the immunoglobulin heavy chain gene locus, resulting in overexpression of cyclin D1 protein. This leads to uncontrolled cell division and proliferation.

Mantle cell lymphoma often presents with advanced-stage disease, involving multiple lymph nodes, bone marrow, and sometimes extranodal sites such as the gastrointestinal tract. Symptoms may include swollen lymph nodes, fatigue, weight loss, night sweats, and abdominal pain or discomfort.

Treatment for MCL typically involves a combination of chemotherapy, immunotherapy, and sometimes targeted therapy or stem cell transplantation. However, the prognosis for MCL is generally less favorable compared to other types of NHL, with a median overall survival of around 5-7 years.

The Ki-67 antigen is a cellular protein that is expressed in all active phases of the cell cycle (G1, S, G2, and M), but not in the resting phase (G0). It is often used as a marker for cell proliferation and can be found in high concentrations in rapidly dividing cells. Immunohistochemical staining for Ki-67 can help to determine the growth fraction of a group of cells, which can be useful in the diagnosis and prognosis of various malignancies, including cancer. The level of Ki-67 expression is often associated with the aggressiveness of the tumor and its response to treatment.

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

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

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

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

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

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

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

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

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

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

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

Flow cytometry is a medical and research technique used to measure physical and chemical characteristics of cells or particles, one cell at a time, as they flow in a fluid stream through a beam of light. The properties measured include:

* Cell size (light scatter)
* Cell internal complexity (granularity, also light scatter)
* Presence or absence of specific proteins or other molecules on the cell surface or inside the cell (using fluorescent antibodies or other fluorescent probes)

The technique is widely used in cell counting, cell sorting, protein engineering, biomarker discovery and monitoring disease progression, particularly in hematology, immunology, and cancer research.

Meiosis is a type of cell division that results in the formation of four daughter cells, each with half the number of chromosomes as the parent cell. It is a key process in sexual reproduction, where it generates gametes or sex cells (sperm and eggs).

The process of meiosis involves one round of DNA replication followed by two successive nuclear divisions, meiosis I and meiosis II. In meiosis I, homologous chromosomes pair, form chiasma and exchange genetic material through crossing over, then separate from each other. In meiosis II, sister chromatids separate, leading to the formation of four haploid cells. This process ensures genetic diversity in offspring by shuffling and recombining genetic information during the formation of gametes.

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

Some examples of Xenopus proteins that are widely studied include:

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

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

Neoplastic cell transformation is a process in which a normal cell undergoes genetic alterations that cause it to become cancerous or malignant. This process involves changes in the cell's DNA that result in uncontrolled cell growth and division, loss of contact inhibition, and the ability to invade surrounding tissues and metastasize (spread) to other parts of the body.

Neoplastic transformation can occur as a result of various factors, including genetic mutations, exposure to carcinogens, viral infections, chronic inflammation, and aging. These changes can lead to the activation of oncogenes or the inactivation of tumor suppressor genes, which regulate cell growth and division.

The transformation of normal cells into cancerous cells is a complex and multi-step process that involves multiple genetic and epigenetic alterations. It is characterized by several hallmarks, including sustained proliferative signaling, evasion of growth suppressors, resistance to cell death, enabling replicative immortality, induction of angiogenesis, activation of invasion and metastasis, reprogramming of energy metabolism, and evading immune destruction.

Neoplastic cell transformation is a fundamental concept in cancer biology and is critical for understanding the molecular mechanisms underlying cancer development and progression. It also has important implications for cancer diagnosis, prognosis, and treatment, as identifying the specific genetic alterations that underlie neoplastic transformation can help guide targeted therapies and personalized medicine approaches.

Proto-oncogene proteins, such as c-Myc, are crucial regulators of normal cell growth, differentiation, and apoptosis (programmed cell death). When proto-oncogenes undergo mutations or alterations in their regulation, they can become overactive or overexpressed, leading to the formation of oncogenes. Oncogenic forms of c-Myc contribute to uncontrolled cell growth and division, which can ultimately result in cancer development.

The c-Myc protein is a transcription factor that binds to specific DNA sequences, influencing the expression of target genes involved in various cellular processes, such as:

1. Cell cycle progression: c-Myc promotes the expression of genes required for the G1 to S phase transition, driving cells into the DNA synthesis and division phase.
2. Metabolism: c-Myc regulates genes associated with glucose metabolism, glycolysis, and mitochondrial function, enhancing energy production in rapidly dividing cells.
3. Apoptosis: c-Myc can either promote or inhibit apoptosis, depending on the cellular context and the presence of other regulatory factors.
4. Differentiation: c-Myc generally inhibits differentiation by repressing genes that are necessary for specialized cell functions.
5. Angiogenesis: c-Myc can induce the expression of pro-angiogenic factors, promoting the formation of new blood vessels to support tumor growth.

Dysregulation of c-Myc is frequently observed in various types of cancer, making it an important therapeutic target for cancer treatment.

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

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

Cyclin-Dependent Kinase 8 (CDK8) is a type of serine/threonine protein kinase that plays a crucial role in the regulation of gene transcription. It forms a complex with cyclin C, and its activity is required for various cellular processes such as cell cycle progression, differentiation, and apoptosis. CDK8 has been shown to phosphorylate several transcription factors and coactivators, thereby modulating their activities and contributing to the control of gene expression. Dysregulation of CDK8 activity has been implicated in various diseases, including cancer, making it a potential target for therapeutic intervention.

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

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

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

The proteasome endopeptidase complex is a large protein complex found in the cells of eukaryotic organisms, as well as in archaea and some bacteria. It plays a crucial role in the degradation of damaged or unneeded proteins through a process called proteolysis. The proteasome complex contains multiple subunits, including both regulatory and catalytic particles.

The catalytic core of the proteasome is composed of four stacked rings, each containing seven subunits, forming a structure known as the 20S core particle. Three of these rings are made up of beta-subunits that contain the proteolytic active sites, while the fourth ring consists of alpha-subunits that control access to the interior of the complex.

The regulatory particles, called 19S or 11S regulators, cap the ends of the 20S core particle and are responsible for recognizing, unfolding, and translocating targeted proteins into the catalytic chamber. The proteasome endopeptidase complex can cleave peptide bonds in various ways, including hydrolysis of ubiquitinated proteins, which is an essential mechanism for maintaining protein quality control and regulating numerous cellular processes, such as cell cycle progression, signal transduction, and stress response.

In summary, the proteasome endopeptidase complex is a crucial intracellular machinery responsible for targeted protein degradation through proteolysis, contributing to various essential regulatory functions in cells.

DNA replication is the biological process by which DNA makes an identical copy of itself during cell division. It is a fundamental mechanism that allows genetic information to be passed down from one generation of cells to the next. During DNA replication, each strand of the double helix serves as a template for the synthesis of a new complementary strand. This results in the creation of two identical DNA molecules. The enzymes responsible for DNA replication include helicase, which unwinds the double helix, and polymerase, which adds nucleotides to the growing strands.

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

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

Cdh1 proteins are part of the anaphase-promoting complex/cyclosome (APC/C), which is a multi-subunit E3 ubiquitin ligase that plays a critical role in regulating the cell cycle. Cdh1, specifically, is a regulatory subunit of the APC/C and is essential for the proper progression through the cell cycle.

Cdh1 binds to and activates the APC/C in late mitosis and early G1 phase, targeting specific proteins for ubiquitination and subsequent degradation by the proteasome. This helps to ensure that key events of the cell cycle, such as chromosome segregation and mitotic exit, occur in a timely and orderly fashion.

Cdh1 has been shown to regulate the degradation of several important cell cycle regulators, including cyclins A and B, securin, and aurora kinase A. By targeting these proteins for destruction, Cdh1 helps to prevent premature entry into mitosis and ensures that cells do not exit mitosis until all chromosomes have been properly aligned and segregated.

Mutations in the genes encoding Cdh1 and other components of the APC/C have been implicated in a variety of human cancers, highlighting the importance of this complex in maintaining genomic stability.

Cyclin-Dependent Kinase 3 (CDK3) is a type of enzyme, specifically a serine/threonine protein kinase, that plays a crucial role in the regulation of the cell cycle. CDK3 functions by binding to specific regulatory subunits known as cyclins, forming active complexes that phosphorylate various target proteins involved in cell cycle progression and transcriptional regulation.

CDK3 is primarily active during the G1 phase and the early S phase of the cell cycle. It forms a complex with cyclin C to regulate the transition from the G1 phase to the S phase, where CDK3 helps initiate DNA replication by phosphorylating key proteins involved in this process.

CDK3 is also known to play a role in neuronal differentiation and development, as well as in tumorigenesis when dysregulated or overexpressed. Inhibition of CDK3 activity has been explored as a potential therapeutic strategy for treating certain types of cancer.

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

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

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

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

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

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

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

Proto-oncogene proteins c-mos are a type of serine/threonine protein kinase that play crucial roles in cell cycle regulation, particularly during the G2 phase and the transition to mitosis. The c-mos gene is a normal version of an oncogene, which can become cancer-causing when mutated or overexpressed. In its normal form, the c-mos protein is involved in controlling the progression of the cell cycle, meiosis, and also has been implicated in neuronal development and synaptic plasticity. Dysregulation of c-mos proto-oncogene proteins can contribute to tumorigenesis and cancer development.

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

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

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

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

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

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

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

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

Examples of biological models include:

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

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

Interphase is a phase in the cell cycle during which the cell primarily performs its functions of growth and DNA replication. It is the longest phase of the cell cycle, consisting of G1 phase (during which the cell grows and prepares for DNA replication), S phase (during which DNA replication occurs), and G2 phase (during which the cell grows further and prepares for mitosis). During interphase, the chromosomes are in their relaxed, extended form and are not visible under the microscope. Interphase is followed by mitosis, during which the chromosomes condense and separate to form two genetically identical daughter cells.

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

Cell cycle checkpoints are control mechanisms that regulate the cell cycle and ensure the accurate and timely progression through different phases of the cell cycle. These checkpoints monitor specific cellular events, such as DNA replication and damage, chromosome separation, and proper attachment of the mitotic spindle to the chromosomes. If any of these events fail to occur properly or are delayed, the cell cycle checkpoints trigger a response that can halt the cell cycle until the problem is resolved. This helps to prevent cells with damaged or incomplete genomes from dividing and potentially becoming cancerous.

There are three main types of cell cycle checkpoints:

1. G1 Checkpoint: Also known as the restriction point, this checkpoint controls the transition from the G1 phase to the S phase of the cell cycle. It monitors the availability of nutrients, growth factors, and the integrity of the genome before allowing the cell to proceed into DNA replication.
2. G2 Checkpoint: This checkpoint regulates the transition from the G2 phase to the M phase of the cell cycle. It checks for completion of DNA replication and absence of DNA damage before allowing the cell to enter mitosis.
3. Mitotic (M) Checkpoint: Also known as the spindle assembly checkpoint, this checkpoint ensures that all chromosomes are properly attached to the mitotic spindle before anaphase begins. It prevents the separation of sister chromatids until all kinetochores are correctly attached and tension is established between them.

Cell cycle checkpoints play a crucial role in maintaining genomic stability, preventing tumorigenesis, and ensuring proper cell division. Dysregulation of these checkpoints can lead to various diseases, including cancer.

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

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

Metaphase is a phase in the cell division process (mitosis or meiosis) where the chromosomes align in the middle of the cell, also known as the metaphase plate or equatorial plane. During this stage, each chromosome consists of two sister chromatids attached to each other by a protein complex called the centromere. The spindle fibers from opposite poles of the cell attach to the centromeres of each chromosome, and through a process called congression, they align the chromosomes in the middle of the cell. This alignment allows for accurate segregation of genetic material during the subsequent anaphase stage.

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

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

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

... D / CDK4, Cyclin D / CDK6, and Cyclin E / CDK2 - regulates transition from G1 to S phase. G2/M cyclins - essential for ... The rise in presence of G1/S cyclins is paralleled by a rise in S cyclins. G1 cyclins do not behave like the other cyclins, in ... G1 cyclins, G1/S cyclins, S cyclins, and M cyclins. This division is useful when talking about most cell cycles, but it is not ... Note that the cyclins are now classified according to their conserved cyclin box structure, and not all these cyclins alter in ...
Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which ... Cyclin-T2 is a protein that in humans is encoded by the CCNT2 gene. The protein encoded by this gene belongs to the highly ... This cyclin and its kinase partner CDK9 were found to be subunits of the transcription elongation factor p-TEFb. The p-TEFb ... "Entrez Gene: CCNT2 cyclin T2". Simone C, Bagella L, Bellan C, Giordano A (Jun 2002). "Physical interaction between pRb and cdk9 ...
Cyclin-O is a protein that in humans is encoded by the CCNO gene. Cyclin O has been shown to interact with RPA2 and PCNA. ... "Entrez Gene: CCNO cyclin O". Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O ... Hirst R, Gosden R, Miller D (June 2006). "The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its relationship ... Muller SJ, Caradonna S (January 1993). "Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase". The ...
Cyclins function as activating subunits of enzymatic complex together with cyclin-dependent kinases (CDKs). Different cyclins ... Cyclin-A1 interacts with: CDC20, Cyclin-dependent kinase 2, E2F1, GNB2L1, GPS2, MYBL2, and Retinoblastoma protein. GRCh38: ... "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine ... "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine ...
... is a member of the cyclin family, specifically the B-type cyclins. The B-type cyclins, B1 and B2, associate with ... Cyclin B1 co-localizes with microtubules, whereas cyclin B2 is primarily associated with the Golgi region. Cyclin B2 also binds ... Cyclin B2 has been shown to interact with TGF beta receptor 2. Cyclin B GRCh38: Ensembl release 89: ENSG00000157456 - Ensembl, ... "Cyclin B2-null mice develop normally and are fertile whereas cyclin B1-null mice die in utero". Proc. Natl. Acad. Sci. U.S.A. ...
... is a member of the cyclin family. Cyclin B is a mitotic cyclin. The amount of cyclin B (which binds to Cdk1) and the ... Because cyclin B is necessary for cells to enter mitosis and therefore necessary for cell division, cyclin B levels are often ... The fact that cyclin B is often disregulated in cancer cells makes cyclin B an attractive biomarker. Many studies have been ... Cyclin+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Drosophila Cyclin B - The Interactive Fly ( ...
"Entrez Gene: CCNE1 cyclin E1". Shanahan F, Seghezzi W, Parry D, Mahony D, Lees E (February 1999). "Cyclin E associates with ... Mumberg D, Wick M, Bürger C, Haas K, Funk M, Müller R (1997). "Cyclin ET, a new splice variant of human cyclin E with a unique ... Cyclin E1 has been shown to interact with: CDC25A, CDKN1B, CUL3 Cdk1, Cyclin-dependent kinase 2, HERC5, P21, Retinoblastoma- ... Lew DJ, Dulić V, Reed SI (October 1991). "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast ...
Other than Rb, viral cyclin D-Cdk6 complex also targets p27Kip, a Cdk inhibitor of cyclin E and A. In addition, viral cyclin D- ... The phosphorylation of Rb by cyclin A-Cdk2, cyclin B-Cdk1, and cyclin E-Cdk2 are unaffected. The C terminus has a stretch of 21 ... In mice and humans, two more cyclin D proteins have been identified. The three homologues, called cyclin D1, cyclin D2, and ... among which is cyclin D. In this way, cyclin D is synthesized as long as the growth factor is present. Cyclin D levels in ...
Cyclins function as regulators of cyclin-dependent kinases. Different cyclins exhibit distinct expression and degradation ... Brooks AR, Shiffman D, Chan CS, Brooks EE, Milner PG (Apr 1996). "Functional analysis of the human cyclin D2 and cyclin D3 ... "The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2". The ... G1/S-specific cyclin-D2 is a protein that in humans is encoded by the CCND2 gene. The protein encoded by this gene belongs to ...
Cyclins function as regulators of CDKs (cyclin-dependent kinase). Different cyclins exhibit distinct expression and degradation ... cyclin D1 is translocated to the IgH promoter leading to cyclin D1 overexpression. Chromosomal translocation of the cyclin D1 ... Cyclin D1 is a protein that in humans is encoded by the CCND1 gene. The CCND1 gene encodes the cyclin D1 protein. The human ... Cyclin D1 and the mechanisms it regulates have the potential to be a therapeutic target for cancer drugs: Cyclin D1 has been ...
"Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 ... "Entrez Gene: CCNK cyclin K". Baek K, Brown RS, Birrane G, Ladias JA (February 2007). "Crystal structure of human cyclin K, a ... Cyclin K also interacts with HIV nef protein. In the presence of overexpressed Nef protein, Cyclin k and CDK9 binding is ... Cyclin K is indispensable for Leukemia growth. SETD1A, is also known to bind Cyclin K through its FLOS domain. The interaction ...
"Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction". EMBO J. 19 (6): 1378-88. doi: ... G2/mitotic-specific cyclin-B1 is a protein that in humans is encoded by the CCNB1 gene. Cyclin B1 is a regulatory protein ... Like all cyclins, levels of cyclin B1 oscillate over the course of the cell cycle. Just prior to mitosis, a large amount of ... Cyclin B1 can reside in the nucleus or the cytoplasm which can have an effect on the malignant potential of cyclin B1 when ...
... is a protein that in humans is encoded by the CCNE2 gene. It is a G1 cyclin that binds Cdk2 and is inhibited by p27( ... Gudas JM, Payton M, Thukral S, Chen E, Bass M, Robinson MO, Coats S (January 1999). "Cyclin E2, a novel G1 cyclin that binds ... Zariwala, M.; Liu, J.; Xiong, Y. (1998-11-26). "Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and CDK3, is ...
Like all cyclin family members, cyclin E forms complexes with cyclin-dependent kinases. In particular, Cyclin E binds with CDK2 ... Cyclin E is a member of the cyclin family. Cyclin E binds to G1 phase Cdk2, which is required for the transition from G1 to S ... Cyclin E/CDK2 plays a critical role in the G1 phase and in the G1-S phase transition. Cyclin E/CDK2 phosphorylates ... Dysregulation of cyclin E occurs in 18-22% of the breast cancers. Cyclin E is a prognostic marker in breast cancer, its altered ...
Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns that ... Cyclin-T1 is a protein that in humans is encoded by the CCNT1 gene. The protein encoded by this gene belongs to the highly ... This cyclin tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p- ... This cyclin and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal ...
Cyclin-A2 is a protein that in humans is encoded by the CCNA2 gene. It is one of the two types of cyclin A: cyclin A1 is ... Cyclin A2 belongs to the cyclin family, whose members regulate cell cycle progression by interacting with CDK kinases. Cyclin ... The cyclin A2-CDK2 complex eventually phosphorylates E2F, turning off cyclin A2 transcription. E2F promotes cyclin A2 ... Cyclin A2 is synthesized at the onset of S phase and localizes to the nucleus, where the cyclin A2-CDK2 complex is implicated ...
... has been shown to interact with P53, Cyclin-dependent kinase 7 and MNAT1. GRCh38: Ensembl release 89: ENSG00000134480 ... Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which ... Cyclin-H is a protein that in humans is encoded by the CCNH gene. The protein encoded by this gene belongs to the highly ... This cyclin forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and ...
... remains associated with CDK1 from late S into late G2 phase when it is replaced by cyclin B. Cyclin A/CDK1 is thought ... Cyclin A is the only cyclin that regulates multiple steps of the cell cycle. Cyclin A can regulate multiple cell cycle steps ... Cyclin A2 is expressed in dividing somatic cells. Cyclin A, along with the other members of the cyclin family, regulates cell ... P21 is a CDK inhibitor that binds to several cyclin/CDK complexes, including cyclin A-CDK2/1 and cyclin D/CDK4, and blocks the ...
Cyclin-dependent kinase 4, Cyclin-dependent kinase 6, EIF3K, and Retinoic acid receptor alpha. Cyclin Cyclin D GRCh38: Ensembl ... Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which ... Brooks AR, Shiffman D, Chan CS, Brooks EE, Milner PG (1996). "Functional analysis of the human cyclin D2 and cyclin D3 ... G1/S-specific cyclin-D3 is a protein that in humans is encoded by the CCND3 gene. The protein encoded by this gene belongs to ...
CDK6; cyclin D1, cyclin D2, cyclin D3 CDK7; cyclin H CDK8; cyclin C CDK9; cyclin T1, cyclin T2a, cyclin T2b, cyclin K CDK10 ... cyclin A, cyclin B CDK2; cyclin A, cyclin E CDK3; cyclin C CDK4; cyclin D1, cyclin D2, cyclin D3 CDK5; CDK5R1, CDK5R2. See also ... Furthermore, cyclin binding determines the specificity of the cyclin-CDK complex for particular substrates. Cyclins can ... Viruses can encode proteins with sequence homology to cyclins. One much-studied example is K-cyclin (or v-cyclin) from Kaposi ...
E2F.2FpRb complexes Hyperphosphorylation cdc25 Maturation promoting factor CDK cyclin A cyclin B cyclin D cyclin E Wee (cell ... "Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction". EMBO J. 19 (6): 1378-1388. doi: ... Cyclin binding alters access to the active site of Cdk1, allowing for Cdk1 activity; furthermore, cyclins impart specificity to ... Furthermore, cyclins can target Cdk1 to particular subcellular locations. In addition to regulation by cyclins, Cdk1 is ...
"Entrez Gene: CDK10 cyclin-dependent kinase (CDC2-like) 10". Kasten M, Giordano A (Apr 2001). "Cdk10, a Cdc2-related kinase, ... Cyclin-dependent kinase 10 has been shown to interact with ETS2. GRCh38: Ensembl release 89: ENSG00000185324 - Ensembl, May ...
A Cyclin-dependent kinase 6 interacts with: CDKN2C, Cyclin D1, Cyclin D3, P16, PPM1B, and PPP2CA. Cell cycle Cyclin-dependent ... It is regulated by cyclins, more specifically by Cyclin D proteins and Cyclin-dependent kinase inhibitor proteins. The protein ... 2003). "Expression of Cyclin-Dependent Kinase 6, but Not Cyclin-Dependent Kinase 4, Alters Morphology of Cultured Mouse ... Kozar K, Sicinski P (March 2005). "Cell cycle progression without cyclin D-CDK4 and cyclin D-CDK6 complexes". Cell Cycle. ...
... has been shown to interact with: BRCA1, CDK2AP1, CDKN1B CDKN3, CEBPA, Cyclin A1, Cyclin E1, Flap ... "Entrez Gene: CDK2 cyclin-dependent kinase 2". Echalier A, Endicott JA, Noble ME (March 2010). "Recent developments in cyclin- ... This protein associates with and is regulated by the regulatory subunits of the complex including cyclin E or A. Cyclin E binds ... Lacy S, Whyte P (May 1997). "Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 ...
... has been shown to interact with: Androgen receptor, Cyclin H, GTF2H1, MNAT1, P53, SUPT5H, and XPB. ... Cyclin-dependent kinase 7, or cell division protein kinase 7, is an enzyme that in humans is encoded by the CDK7 gene. The ... The growth suppressor p53 has been shown to interact with cyclin H both in vitro and in vivo. Addition of wild type p53 was ... "Entrez Gene: CDK7 cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)". Patel H, Abduljabbar R, Lai ...
"OMIM Entry - * 123831 - CYCLIN-DEPENDENT KINASE 5; CDK5". omim.org. Retrieved 2020-11-02. Tsai, Li-Huei. Cyclin Dependent ... Cyclin-dependent kinase 5 is a protein, and more specifically an enzyme, that is encoded by the Cdk5 gene. It was discovered 15 ... Cyclin-Dependent+Kinase+5 at the U.S. National Library of Medicine Medical Subject Headings (MeSH) CDK5 human gene location in ... Cyclin Dependent Kinase 5. Springer. 19 August 2008. ISBN 978-0-387-78886-9. Patrick GN, Zukerberg L, Nikolic M, de la Monte S ...
During G2 phase, cyclin A is degraded, while cyclin B is synthesized and cyclin B-Cdk1 complexes form. Not only are cyclin B- ... cyclin-dependent kinase (CDK), with a regulatory subunit, cyclin. Once cyclin-dependent kinases bind to cyclin, the formed ... Cyclin Cyclin-dependent kinase Malumbres M, Barbacid M. Mammalian cyclin-dependent kinases. Trends Biochem. Sci. 2005 Nov;30(11 ... cyclin D1-Cdk4 and cyclin D1-Cdk6 phosphorylate pRB, followed by additional phosphorylation from the cyclin E-Cdk2 CDKC. Once ...
"Entrez Gene: CDK4 cyclin-dependent kinase 4". "CDK4 - Cyclin-dependent kinase 4 - Homo sapiens (Human) - CDK4 gene & protein". ... Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 ... 1993). "Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent ... 1995). "Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C". Proc. Natl. Acad. ...
... or CDK9 is a cyclin-dependent kinase associated with P-TEFb. The protein encoded by this gene is a ... This protein forms a complex with and is regulated by its regulatory subunit cyclin T or cyclin K. HIV-1 Tat protein was found ... Cyclin-Dependent+Kinase+9 at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Drosophila Cyclin dependent ... "Entrez Gene: CDK9 cyclin-dependent kinase 9 (CDC2-related kinase)". MacLachlan TK, Sang N, De Luca A, Puri PL, Levrero M, ...
"Entrez Gene: CDK3 cyclin-dependent kinase 3". Bullrich F, MacLachlan TK, Sang N, et al. (1995). "Chromosomal mapping of members ... 2002). "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)". Eur. J. Biochem. 268 (23): 6076-82. doi:10.1046/j. ... Ren S, Rollins BJ (2004). "Cyclin C/cdk3 promotes Rb-dependent G0 exit". Cell. 117 (2): 239-51. doi:10.1016/S0092-8674(04)00300 ... CDK3 can phosphorylate histone H1 and interacts with an unknown type of cyclin. GRCh38: Ensembl release 89: ENSG00000250506 - ...
Cyclin D / CDK4, Cyclin D / CDK6, and Cyclin E / CDK2 - regulates transition from G1 to S phase. G2/M cyclins - essential for ... The rise in presence of G1/S cyclins is paralleled by a rise in S cyclins. G1 cyclins do not behave like the other cyclins, in ... G1 cyclins, G1/S cyclins, S cyclins, and M cyclins. This division is useful when talking about most cell cycles, but it is not ... Note that the cyclins are now classified according to their conserved cyclin box structure, and not all these cyclins alter in ...
cyclin-dependent kinase inhibitor. cyclin-dependent kinase interacting protein 2. cyclin-dependent kinase interactor 1. kinase- ... CDKN3 cyclin dependent kinase inhibitor 3 [Homo sapiens] CDKN3 cyclin dependent kinase inhibitor 3 [Homo sapiens]. Gene ID:1033 ... cyclin dependent kinase inhibitor 3provided by HGNC. Primary source. HGNC:HGNC:1791 See related. Ensembl:ENSG00000100526 MIM: ... cyclin-dependent kinase inhibitor 3. Names. CDK2-associated dual specificity phosphatase. Cdk-associated protein phosphatase. ...
Cyclin E/CDK2 or cyclin A/CDK2 cannot phosphorylate the mutant in vitro. Using the technique of fluorescence recovery after ... The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation Mol Cell Biol. 2003 Dec;23(23):8626-36. doi: ... in which the five cyclin-dependent kinase phosphorylation consensus sites were mutated from serine or threonine residues into ...
Cyclin A regulates kinetochore microtubules to promote faithful chromosome segregation.. 60. 15601848. 2005. Cyclin-dependent ... Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm.. 54. ... Cyclin A2 regulates nuclear-envelope breakdown and the nuclear accumulation of cyclin B1.. 64. ... Cyclins and cyclin-dependent kinases: comparative study of hepatocellular carcinoma versus cirrhosis.. 51. ...
Compare Cyclin T1 ELISA Kits and find the right product on antibodies-online.com. ... Order Cyclin T1 ELISA Kits for many Reactivities. ... Cyclin T1 ELISA Kits. (Cyclin T1 (CCNT1)). This gene encodes a ... Aliase für Cyclin T1 ELISA Kits. Cyclin T (CycT) ELISA Kits. cyclin T1 (CCNT1) ELISA Kits. cyclin T1 (ccnt1) ELISA Kits. cyclin ... Hier sind Cyclin T1 ELISA Kits für eine Vielzahl von Species wie anti-Chicken Cyclin T1, anti-Cow Cyclin T1, anti-Dog Cyclin T1 ...
From the Cyclin Portugal Centre of Tábua, six routes with different levels of difficulty are available, along which you will ...
Cyclin I is an atypical cyclin because it is most abundant in postmitotic cells. We previously showed that cyclin I does not ... Cyclin I: a new cyclin encoded by a gene isolated from human brain. Exp. Cell Res. 221:534-542. View this article via: CrossRef ... HEK293 cells were cotransfected with cyclin I alone, cyclin I and Cdk5, or cyclin I and a dominant negative Cdk5 (D145N-Cdk5). ... Proof that these differences were indeed due to cyclin I was confirmed by infecting cyclin I-null cells with myc-tagged cyclin ...
1996). Both cyclin A and cyclin E have S-phase promoting (SPF) activity in Xenopus egg extracts. J. Cell Sci. 109, 1555-1563. ... 2012). Interaction of Cyclin-Dependent Kinase 12/CrkRS with Cyclin K1 Is Required for the Phosphorylation of the C-Terminal ... Here we show that the cyclin-dependent kinase G2 (CDKG2), together with its cognate cyclin, CYCLYN L1 (CYCL1) affects the ... It has been previously shown that the CDKG group of kinases and their cognate cyclin, CYCLIN L1 (CYCL1), are important ...
Techniques: Tool compounds for probing cyclin dependent kinase 8 (CDK8)- and cyclin dependent kinase 19 (CDK19; CDC2L6)- ...
Among the major cyclin-dependent kinases (Cdks), Cdk1 is most abundantly expressed in IDG-SW3 cells, and its expression is down ... Among the major cyclin-dependent kinases (Cdks), Cdk1 is most abundantly expressed in IDG-SW3 cells, and its expression is down ... Among the major cyclin-dependent kinases (Cdks), Cdk1 is most abundantly expressed in IDG-SW3 cells, and its expression is down ... Regulation of osteoblast to osteocyte differentiation by cyclin-dependent kinase-1. *Mark ...
Cyclin around and around again targeting transcriptional CDKs in lymphoid malignancy. *Gregory, G. (Organiser) ...
Cyclin-dependent kinases (CDKs) are protein kinases characterized by needing a …Cyclin-dependent kinase 2. Cyclin-dependent ... The encoded protein binds to and inhibits the activity of cyclin-cyclin-dependent kinase2 or -cyclin-dependent kinase4 ... Cyclin-dependent kinase 1 also known as CDK1 or cell division cycle protein 2 homolog …Cyclin-dependent kinase 2. Cyclin- ... Cyclins and cyclin-dependent kinases control when cells divide, making them important targets for cancer therapy. Cyclin A ( ...
A cyclin subtype that is found associated with CYCLIN-DEPENDENT KINASE 5; cyclin G associated kinase, and PROTEIN PHOSPHATASE 2 ... "Cyclin G" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject Headings ... This graph shows the total number of publications written about "Cyclin G" by people in this website by year, and whether " ... Below are the most recent publications written about "Cyclin G" by people in Profiles. ...
Cyclin D3 ELISA Kit for Measurement of Mouse Cyclin D3 in Cell Culture Supernatant, Plasma, Serum... ... Cyclin D3ELISA Kit详情. (hide) 抗原 See all Cyclin D3 (CCND3) ELISA试剂盒 Cyclin D3 (CCND3) 适用 All reactivities for Cyclin D3 ELISA试剂盒 ... Cyclin D3目标详情. (hide) 抗原 See all Cyclin D3 (CCND3) ELISA试剂盒 Cyclin D3 (CCND3) Abstract CCND3 产品 途径 Cell Division Cycle, Mitotic ... Cyclin D3 (CCND3) ELISA Kit CCND3 适用: 大鼠 Colorimetric Sandwich ELISA 31.25 pg/mL - 2000 pg/mL Plasma, Serum, Tissue
IHC of Cyclin B1 on an FFPE Cervical Cancer Tissue ... Cyclin B1-Cdk1 is involved in the early events of mitosis, such ... Cyclin B1 is a regulatory protein involved with mitosis. It complexes with p34(cdc2) to form the maturation-promoting factor ( ... Before mitosis almost all cyclin B1 in the cell is located in the cytoplasm, but in late prophase it relocates to the nucleus. ... Cyclin B1 is a rabbit monoclonal antibody derived from cell culture supernatant that is concentrated, dialyzed, filter ...
Cyclin B1 Antibody detects endogenous levels of total Cyclin B1. Immunogen: A synthesized peptide derived from human Cyclin B1 ... Cyclin B1 Antibody detects endogenous levels of total Cyclin B1.. Immunogen: A synthesized peptide derived from human Cyclin B1 ...
Laden Sie das herunter und installieren Sie es Cyclin Schrift kostenlos von FFonts.net. ✔️ Diese Schriftart wurde ... Schriftart / Dekorative / Cyclin / Cyclin Herunterladen Dein Download beginnt in 20 Sekunden… Wenn nicht, die folgenden ...
Cyclin-dependent kinase control of the initiation-to-elongation switch of RNA polymerase II. Nat Struct Mol Biol. 2012 Nov; 19( ... Shiozaki Y, Okamura K, Kohno S, Keenan AL, Williams K, Zhao X, Chick WS, Miyazaki-Anzai S, Miyazaki M. The CDK9-cyclin T1 ... "Cyclin-Dependent Kinase 9" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Cyclin-Dependent Kinase 9" by people in this website by year, ...
Cyclin-Dependent Kinase Inhibitor Proteins [D12.776.624.776.355]. *Cyclin-Dependent Kinase Inhibitor p19 [D12.776.624.776. ... "Cyclin-Dependent Kinase Inhibitor p19" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, ... An INK4 cyclin-dependent kinase inhibitor containing five ANKYRIN REPEATS. Aberrant expression of this protein has been ... This graph shows the total number of publications written about "Cyclin-Dependent Kinase Inhibitor p19" by people in UAMS ...
Comparison of the structure of the unbound cyclin with the structure of cyclin A complexed with CDK2 reveals that cyclin A does ... cyclin A-3, corresponding to residues 171-432 of human cyclin A. The cyclin box has an or-helical fold comprising five a ... Cyclins exhibit diverse sequences but all share homology over a region of approximately 100 amino acids, termed the cyclin box ... The structural results indicate a role for the cyclin-box fold both as a template for the cyclin family and as a generalised ...
Home keyboard_arrow_right Publications keyboard_arrow_right Loss of Cyclin C or CDK8 provides ATR inhibitor resistance by ... Loss of Cyclin C or CDK8 provides ATR inhibitor resistance by suppressing transcription-associated replication stress ...
Cyclin E. A, Cyclin A. R, restriction point.NATURE COMMUNICATIONS , 7:12991 , DOI: ten.1038/ncomms12991 , www.nature.com/ ... D, Cyclin D. E, Cyclin E. A, Cyclin A. R, restriction point.NATURE COMMUNICATIONS , 7:12991 , DOI: ten.1038/ncomms12991 , www. ... p53 p21 Cyclin D1 Cyclin E2 Cyclin A2 GAPDHNATURE COMMUNICATIONS , DOI: 10.1038/ncommsARTICLErequirement of higher doses to ... D, Cyclin. Post date. March 2, 2024. Post last updated dateUpdated March 2, 2024. Post read time. 2 min read Post author. ...
Cyclin. 0.16. 0.24. 0.40. 0.18. 0.19. 0.33. 0.36. 0.61. 0.34. 0.34. KW-0251. Elongation factor. 0.08. 0.11. 0.45. 0.08. 0.09. ... Cyclin. GO:0061575. 89.34. 98.92. 98.89. 0.44. 97.96. 99.78. 99.78. 0.60. 89.80. 99.84. 99.83. 0.62. 75.51. 99.63. 99.53. 0.39 ...
Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which ... Potentiates the transcriptional activity of ATF5.,similarity:Belongs to the cyclin family.,similarity:Belongs to the cyclin ... This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activtiy is required for cell ... Cyclin D subfamily.,subunit:Interacts with the CDK4 and CDK6 protein kinases to form a serine/threonine kinase holoenzyme ...
... as nuclear-targeted cyclin B1 was degraded at twice the rate of wild-type cyclin B1. We propose a simple spatial model of G2 ... Spatial regulation of APCCdh1-induced cyclin B1 degradation maintains G2 arrest in mouse oocytes. Creator Holt, Janet E.; ... G2 arrest, however, also requires control in the concentrations of the Cdk1-binding partner cyclin B1, a process achieved by ... However, it remains unresolved how cyclin B1 levels are suppressed sufficiently to maintain arrest but not so low that they ...
CDKN1C: cyclin dependent kinase inhibitor 1C. *CDKN1B: cyclin dependent kinase inhibitor 1B ...
Cyclin D1 plays a key role in cell cycle regulation and progression of cells from G1 phase to S phase by activation of cyclin- ... as well as an overexpression of cyclin D1. [11] Chen et al noted that the association with cyclin D1 overexpression in hairy ... Cyclin D1 is overexpressed. Immunophenotyping helps differentiate MCL from other small B-cell lymphomas (see the Table, below). ... 11] Chen et al assessed expression of sox11 and evaluated its association with t(11;14) and overexpression of cyclin D1 in 211 ...
Targeting cyclin D-CDK4/6 sensitizes immune-refractory cancer by blocking the SCP3-NANOG axis. ... Dive into the research topics of Targeting cyclin D-CDK4/6 sensitizes immune-refractory cancer by blocking the SCP3-NANOG axis ...
MiR-1271 Inhibits Ovarian Cancer Growth by Targeting Cyclin G1 Xiaogang Liu, Lihong Ma, [...] Qinhua Rao, Yuhui Mao, Yuhong Xin ... Cyclin-Dependent Kinase 1 (CDK1) is Co-Expressed with CDCA5: Their Functions in Gastric Cancer Cell Line MGC-803 Zhigang Huang ...
  • Cyclins, when bound with the dependent kinases, such as the p34/cdc2/cdk1 protein, form the maturation-promoting factor. (wikipedia.org)
  • Cyclins and cyclin-dependent kinases: comparative study of hepatocellular carcinoma versus cirrhosis. (atlasgeneticsoncology.org)
  • Among the major cyclin-dependent kinases (Cdks), Cdk1 is most abundantly expressed in IDG-SW3 cells, and its expression is down-regulated during differentiation into osteocytes. (lu.se)
  • This Screening Library contains drug-like screening compounds targeting cyclin-dependent kinases CDK2 and CDK7 for anticancer drug discovery.Damage to the heart, brain or skeletal muscles causes elevated creatine kinase levels, according to Better Medicine. (dsimanifesto.eu)
  • Cyclin-dependent kinases (CDKs) are members of the serine/threonine …Jun 6, 2020 · Ino H, Chiba T (2001) Cyclin-dependent kinase 4 and cyclin D1 are required for excitotoxin-induced neuronal cell death in vivo. (dsimanifesto.eu)
  • Cyclin-dependent kinases (CDKs), cyclins, and CDK inhibitors (CKIs) are valuable members of this system and their equilibrium guarantees the proper progression of the cell cycle. (dsimanifesto.eu)
  • The protein encoded by this gene is a member of the cyclin-dependent kinase (CDK) …Cyclin-dependent kinases (CDKs) lie at the heart of eukaryotic cell cycle …This Screening Library contains drug-like screening compounds targeting cyclin-dependent kinases CDK2 and CDK7 for anticancer drug discovery.Function. (dsimanifesto.eu)
  • 3] Feb 11, 2021 · Introduction: The cell cycle cyclin-dependent kinases (CDKs) play a critical role in controlling the transition between cell cycle phases, as well as cellular transcription. (dsimanifesto.eu)
  • https://usmleqa.com/?p=7728 Question: What are Cyclin-dependent kinases? (dsimanifesto.eu)
  • Background: Eukaryotic cell cycle progression is regulated by cyclin dependent protein kinases (CDKs) whose activity is regulated by association with cyclins and by reversible phosphorylation. (ncl.ac.uk)
  • Cyclins function as regulators of CDK kinases. (immunoway.com)
  • Protein kinases that control cell cycle progression in all eukaryotes and require physical association with CYCLINS to achieve full enzymatic activity. (bvsalud.org)
  • Cyclin-dependent kinases are regulated by phosphorylation and dephosphorylation events. (bvsalud.org)
  • Cyclins themselves have no enzymatic activity but have binding sites for some substrates and target the Cdks to specific subcellular locations. (wikipedia.org)
  • Cyclins also determine the subcellular location and substrate specificity of CDKs. (ncl.ac.uk)
  • There are several different cyclins that are active in different parts of the cell cycle and that cause the Cdk to phosphorylate different substrates. (wikipedia.org)
  • In humans, there are multiple forms of positive transcription elongation factor b, which may include one of several different cyclins along with cyclin-dependent kinase 9. (antikoerper-online.de)
  • Specificity: Cyclin B1 Antibody detects endogenous levels of total Cyclin B1. (afsbio.com)
  • The cyclin subunit imparts substrate specificity to the complex. (immunoway.com)
  • It was identified as a cyclin-dependent kinase inhibitor, and has been shown to interact with, and dephosphorylate CDK2 kinase, thus prevent the activation of CDK2 kinase. (nih.gov)
  • Cyclin E/CDK2 or cyclin A/CDK2 cannot phosphorylate the mutant in vitro. (nih.gov)
  • Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyclin A/Cdk2 as a progesterone receptor coactivator. (atlasgeneticsoncology.org)
  • Conclusions: Analysis of residues that are conserved throughout the A, B, and E cyclins identifies two exposed clusters of residues, one of which has recently been shown to be involved in the association with human CDK2. (ncl.ac.uk)
  • Comparison of the structure of the unbound cyclin with the structure of cyclin A complexed with CDK2 reveals that cyclin A does not undergo any significant conformational changes on complex formation. (ncl.ac.uk)
  • This gene encodes a member of the highly conserved cyclin C subfamily. (antikoerper-online.de)
  • The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. (immunoway.com)
  • Cyclin is a family of proteins that controls the progression of a cell through the cell cycle by activating cyclin-dependent kinase (CDK) enzymes or group of enzymes required for synthesis of cell cycle. (wikipedia.org)
  • For example, the amino-terminal regions of S and M cyclins contain short destruction-box motifs that target these proteins for proteolysis in mitosis. (wikipedia.org)
  • Threading analysis shows that the cyclin-box fold is consistent with the sequences of the transcription factor TFIIB and other functionally related proteins. (ncl.ac.uk)
  • Here, we examined spatial control of this process by determining the intracellular location of the proteins involved and using nuclear-targeted cyclin B1. (edu.au)
  • A cyclin forms a complex with Cdk, which begins to activate but the complete activation requires phosphorylation, as well. (wikipedia.org)
  • To analyze the effect of H1 tail phosphorylation on the modulation of the histone's nuclear dynamics, we generated a mutant histone H1, referred to as M1-5, in which the five cyclin-dependent kinase phosphorylation consensus sites were mutated from serine or threonine residues into alanines. (nih.gov)
  • This cyclin and its kinase partner are also involved in triggering transcript elongation through phosphorylation of the carboxy-terminal domain of the largest RNA polymerase II subunit. (antikoerper-online.de)
  • Phosphorylation by Cyclin-dependent kinase 1 (CDK1) at two conserved sites in this region destabilizes binding to Mis18α:Mis18β, limiting complex formation to the G1 phase of the cell cycle. (elifesciences.org)
  • Cyclin-dependent kinase 2, also known as cell division …Cyclin-dependent kinase 1 also known as CDK1 or cell division cycle protein 2 homolog …Cyclin-dependent kinase 2. (dsimanifesto.eu)
  • Jan 3, 2024 · CDK1 (Cyclin Dependent Kinase 1) is a Protein Coding gene. (dsimanifesto.eu)
  • Its activation is well regulated, and positive feedback loops ensure that once the cyclin B1-Cdk1 complex is activated it is not deactivated. (affordableihcinstruments.com)
  • Cyclin B1-Cdk1 is involved in the early events of mitosis, such as chromosome condensation, nuclear envelope breakdown, and spindle pole assembly. (affordableihcinstruments.com)
  • G2 arrest, however, also requires control in the concentrations of the Cdk1-binding partner cyclin B1, a process achieved by anaphase-promoting complex (APC Cdh1 ) activity, which ubiquitylates and so targets cyclin B1 for degradation. (edu.au)
  • Cyclin-dependent kinase inhibitor 1C is a tight-binding inhibitor of several G1 cyclin/Cdk complexes and a negative regulator of cell proliferation. (dsimanifesto.eu)
  • Cyclin D3 Monoclonal Antibody detects endogenous levels of Cyclin D3 protein. (immunoway.com)
  • Identification of cell cycle-associated and -unassociated regulators for expression of a hepatocellular carcinoma oncogene cyclin-dependent kinase inhibitor 3. (nih.gov)
  • Expression and alternative splicing of the cyclin-dependent kinase inhibitor-3 gene in human cancer. (nih.gov)
  • The encoded protein tightly associates with cyclin-dependent kinase 9, and is a major subunit of positive transcription elongation factor b (p-TEFb). (antikoerper-online.de)
  • The complex containing the encoded cyclin and cyclin-dependent kinase 9 acts as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and is both necessary and sufficient for full activation of viral transcription. (antikoerper-online.de)
  • Here we show that the cyclin-dependent kinase G2 (CDKG2), together with its cognate cyclin, CYCLYN L1 (CYCL1) affects the alternative splicing of FLM , balancing the levels of FLM-β and FLM-δ across the ambient temperature range. (frontiersin.org)
  • Cyclin dependent kinase - Taking care of your elderly parents might be your duty, but it can be costly. (dsimanifesto.eu)
  • Article CAS PubMed PubMed Central Google Scholar Cyclin-dependent kinase 2. (dsimanifesto.eu)
  • Nov 23, 2023 · This gene encodes a member of the cyclin-dependent protein kinase family. (dsimanifesto.eu)
  • CDKN1A cyclin dependent kinase inhibitor 1A [ (human)] , updated on 5-Feb-2024. (dsimanifesto.eu)
  • This gene encodes a potent cyclin-dependent kinase inhibitor. (dsimanifesto.eu)
  • The encoded protein binds to and inhibits the activity of cyclin-cyclin-dependent kinase2 or -cyclin-dependent kinase4 complexes, and thus functions as a regulator of cell cycle progression at G1. (dsimanifesto.eu)
  • Cyclin-Dependent Kinase (CDK) Inhibitors in Drug Development CDK …Oct 28, 2023 · The Cyclin-dependent kinase 1, as a serine/threonine protein kinase, is more than a cell cycle regulator as it was originally identified. (dsimanifesto.eu)
  • CDKL5 (cyclin-dependent kinase-like 5) deficiency disorder is a rare neurodevelopmental condition caused by pathogenic variants in the CDKL5 gene. (dsimanifesto.eu)
  • Cyclin-Dependent Kinase 12 and Programmed Death 1 (PD-1) Inhibition - a Conceptual Model. (dsimanifesto.eu)
  • Cyclin-Dependent Kinase 9" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • This graph shows the total number of publications written about "Cyclin-Dependent Kinase 9" by people in this website by year, and whether "Cyclin-Dependent Kinase 9" was a major or minor topic of these publications. (ucdenver.edu)
  • Below are the most recent publications written about "Cyclin-Dependent Kinase 9" by people in Profiles. (ucdenver.edu)
  • An INK4 cyclin-dependent kinase inhibitor containing five ANKYRIN REPEATS. (uams.edu)
  • DHA-enriched fish oil upregulates cyclin-dependent kinase inhibitor 2A (P16 INK ) expression and downregulates telomerase activity without modulating effects of PPARγ Pro12Ala polymorphism in type 2 diabetic patients: A randomized, double-blind, placebo-controlled clinical trial. (bvsalud.org)
  • Results: We have solved the crystal structure, at 2.0 Angstrom resolution, of an active recombinant fragment of bovine cyclin A, cyclin A-3, corresponding to residues 171-432 of human cyclin A. The cyclin box has an or-helical fold comprising five a helices. (ncl.ac.uk)
  • Purified recombinant fragment of human Cyclin D3 expressed in E. Coli. (immunoway.com)
  • Kaposi sarcoma herpesvirus (KSHV) encodes a D-type cyclin (ORF72) that binds CDK6 and is likely to contribute to KSHV-related cancers. (wikipedia.org)
  • Cyclin B1 is a rabbit monoclonal antibody derived from cell culture supernatant that is concentrated, dialyzed, filter sterilized and diluted in buffer pH 7.5, containing BSA and sodium azide as a preservative. (affordableihcinstruments.com)
  • Western Blot analysis using Cyclin D3 Monoclonal Antibody against NIH/3T3 (1) and Jurkat (2) cell lysate. (immunoway.com)
  • The levels of S cyclins remain high, not only throughout S phase, but through G2 and early mitosis as well to promote early events in mitosis. (wikipedia.org)
  • M cyclin concentrations rise as the cell begins to enter mitosis and the concentrations peak at metaphase. (wikipedia.org)
  • The destruction of M cyclins during metaphase and anaphase, after the Spindle Assembly Checkpoint is satisfied, causes the exit of mitosis and cytokinesis. (wikipedia.org)
  • Cyclin B1 is a regulatory protein involved with mitosis. (affordableihcinstruments.com)
  • Cyclin B1 contributes to the switch-like all or none behavior of the cell in deciding to commit mitosis. (affordableihcinstruments.com)
  • Before mitosis almost all cyclin B1 in the cell is located in the cytoplasm, but in late prophase it relocates to the nucleus. (affordableihcinstruments.com)
  • At the end of mitosis, cyclin B1 is targeted for degradation by the APC through its APC localization sequence, permitting the cell to exit mitosis. (affordableihcinstruments.com)
  • The CDK4 activity associated with this cyclin was reported to be necessary for cell cycle progression through G2 phase into mitosis after UV radiation. (immunoway.com)
  • Cell changes in the cell cycle like the assembly of mitotic spindles and alignment of sister-chromatids along the spindles are induced by M cyclin- Cdk complexes. (wikipedia.org)
  • Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm. (atlasgeneticsoncology.org)
  • Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. (immunoway.com)
  • Thus, APC Cdh1 activity prevents precocious meiotic entry by promoting cyclin B1 degradation. (edu.au)
  • Hier sind Cyclin T1 ELISA Kits für eine Vielzahl von Species wie anti-Chicken Cyclin T1, anti-Cow Cyclin T1, anti-Dog Cyclin T1 zu finden. (antikoerper-online.de)
  • Hier sind Cyclin T1 ELISA Kits mit einem spezifischen Detektionsmethode zu finden. (antikoerper-online.de)
  • This ELISA kit is a solid phase ELISA designed for quantitative determination of Cyclin D3 (CCND3). (antibodies-online.cn)
  • The oscillations of the cyclins, namely fluctuations in cyclin gene expression and destruction by the ubiquitin mediated proteasome pathway, induce oscillations in Cdk activity to drive the cell cycle. (wikipedia.org)
  • Expression of cyclins detected immunocytochemically in individual cells in relation to cellular DNA content (cell cycle phase), or in relation to initiation and termination of DNA replication during S-phase, can be measured by flow cytometry. (wikipedia.org)
  • Shiozaki Y, Okamura K, Kohno S, Keenan AL, Williams K, Zhao X, Chick WS, Miyazaki-Anzai S, Miyazaki M. The CDK9-cyclin T1 complex mediates saturated fatty acid-induced vascular calcification by inducing expression of the transcription factor CHOP. (ucdenver.edu)
  • The mechanism by which MSLN contributes to these more aggressive behaviors was investigated by using ingenuity pathway analysis, which predicted that increased MSLN could induce cyclin E expression. (cdc.gov)
  • Epstein-Barr virus latent membrane protein expression and cyclin DI cell cyase protein expression in malignant and normal oesophageal tissues to see whether any variation in their expression in these tissues could be of diagnostic or prognostic value. (bvsalud.org)
  • EBV-LMPI protein expression and cyclin DI expression were studied immunohisto chemically in these tissue sections. (bvsalud.org)
  • This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activtiy is required for cell cycle G1/S transition. (immunoway.com)
  • The Cdk- G1/S cyclin complex begins to induce the initial processes of DNA replication, primarily by arresting systems that prevent S phase Cdk activity in G1. (wikipedia.org)
  • Immunogen: A synthesized peptide derived from human Cyclin B1, corresponding to a region within the internal amino acids. (afsbio.com)
  • G1 cyclins do not behave like the other cyclins, in that the concentrations increase gradually (with no oscillation), throughout the cell cycle based on cell growth and the external growth-regulatory signals. (wikipedia.org)
  • We found that raising nuclear cyclin B1 concentrations, an event normally observed in the minutes before nuclear envelope breakdown, was a very effective method of inducing the G2/M transition. (edu.au)
  • Cyclins are generally very different from each other in primary structure, or amino acid sequence. (wikipedia.org)
  • However, all members of the cyclin family are similar in 100 amino acids that make up the cyclin box. (wikipedia.org)
  • Cyclins exhibit diverse sequences but all share homology over a region of approximately 100 amino acids, termed the cyclin box. (ncl.ac.uk)
  • Furthermore, APC Cdh1 activity appeared higher in the nucleus, as nuclear-targeted cyclin B1 was degraded at twice the rate of wild-type cyclin B1. (edu.au)
  • We propose a simple spatial model of G2 arrest in which nuclear APC Cdh1 -proteasomal activity guards against any cyclin B1 accumulation mediated by nuclear import. (edu.au)
  • We previously showed that cyclin I does not regulate proliferation, but rather controls survival of podocytes, terminally differentiated epithelial cells that are essential for the structural and functional integrity of kidney glomeruli. (jci.org)
  • We found that BSW shMSLN cells had decreased cyclin E, and their proliferation rate was reverted to nearly that of untransformed cells. (cdc.gov)
  • The cyclins also promote other activities to progress the cell cycle, such as centrosome duplication in vertebrates or spindle pole body in yeast. (wikipedia.org)
  • Cdc20 and Cks direct the spindle checkpoint-independent destruction of cyclin A. (atlasgeneticsoncology.org)
  • p53 mutation and cyclin D1 amplification correlate with cisplatin sensitivity in xenografted human squamous cell carcinomas from head and neck. (lu.se)
  • From the determination of the structure of cyclin A, together with results from biochemical and genetic analyses, we can identify which parts of the cyclin molecule may contribute to cyclin A structure and function. (ncl.ac.uk)
  • From the Cyclin' Portugal Centre of Tábua, six routes with different levels of difficulty are available, along which you will cross magnificent landscapes with the Serra da Estrela in the background. (aldeiasdoxisto.pt)
  • However, it remains unresolved how cyclin B1 levels are suppressed sufficiently to maintain arrest but not so low that they make oocytes hormonally insensitive. (edu.au)
  • Cyclins were originally discovered by R. Timothy Hunt in 1982 while studying the cell cycle of sea urchins. (wikipedia.org)
  • R. Timothy Hunt: "By the way, the name cyclin, which I coined, was really a joke, it's because I liked cycling so much at the time, but they did come and go in the cell. (wikipedia.org)
  • Cyclins were originally named because their concentration varies in a cyclical fashion during the cell cycle. (wikipedia.org)
  • Note that the cyclins are now classified according to their conserved cyclin box structure, and not all these cyclins alter in level through the cell cycle. (wikipedia.org)
  • Cyclins can be divided into four classes based on their behaviour in the cell cycle of vertebrate somatic cells and yeast cells: G1 cyclins, G1/S cyclins, S cyclins, and M cyclins. (wikipedia.org)
  • This division is useful when talking about most cell cycles, but it is not universal as some cyclins have different functions or timing in different cell types. (wikipedia.org)
  • The presence of G cyclins coordinate cell growth with the entry to a new cell cycle. (wikipedia.org)
  • A novel function for Cyclin A2: control of cell invasion via RhoA signaling. (atlasgeneticsoncology.org)
  • Cyclins contain two domains of a similar all-α fold, the first located at the N-terminus and the second at the C-terminus. (wikipedia.org)
  • This fold is repeated in the C-terminal region, although this region shares negligible sequence similarity with the cyclin box. (ncl.ac.uk)
  • The structural results indicate a role for the cyclin-box fold both as a template for the cyclin family and as a generalised adaptor molecule in the regulation of transcription. (ncl.ac.uk)
  • S cyclins bind to Cdk and the complex directly induces DNA replication. (wikipedia.org)