Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Protein Tyrosine Phosphatases: An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.Tyrosine 3-Monooxygenase: An enzyme that catalyzes the conversion of L-tyrosine, tetrahydrobiopterin, and oxygen to 3,4-dihydroxy-L-phenylalanine, dihydrobiopterin, and water. EC 1.14.16.2.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Phosphotyrosine: An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.Signal Transduction: 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.Protein Tyrosine Phosphatase, Non-Receptor Type 11: A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.Receptor Protein-Tyrosine Kinases: A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.Protein Tyrosine Phosphatase, Non-Receptor Type 6: A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.Protein Tyrosine Phosphatase, Non-Receptor Type 1: A subtype of non-receptor protein tyrosine phosphatases that includes two distinctive targeting motifs; an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. This subtype includes a hydrophobic domain which localizes it to the ENDOPLASMIC RETICULUM.Molecular Sequence Data: 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.Enzyme Activation: 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.Amino Acid Sequence: 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.PhosphoproteinsLymphocyte Specific Protein Tyrosine Kinase p56(lck): This enzyme is a lymphoid-specific src family tyrosine kinase that is critical for T-cell development and activation. Lck is associated with the cytoplasmic domains of CD4, CD8 and the beta-chain of the IL-2 receptor, and is thought to be involved in the earliest steps of TCR-mediated T-cell activation.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Genistein: An isoflavonoid derived from soy products. It inhibits PROTEIN-TYROSINE KINASE and topoisomerase-II (DNA TOPOISOMERASES, TYPE II); activity and is used as an antineoplastic and antitumor agent. Experimentally, it has been shown to induce G2 PHASE arrest in human and murine cell lines and inhibits PROTEIN-TYROSINE KINASE.Vanadates: Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.src Homology Domains: Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.Proto-Oncogene Proteins: 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.Receptor, Epidermal Growth Factor: A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.Proto-Oncogene Proteins pp60(c-src): Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase.Proto-Oncogene Proteins c-fyn: Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Tyrosine Decarboxylase: A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC 4.1.1.25.Intracellular Signaling Peptides and Proteins: Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.Protein Kinase Inhibitors: Agents that inhibit PROTEIN KINASES.Tyrosine Phenol-Lyase: An enzyme that catalyzes the cleavage of tyrosine to phenol, pyruvate, and ammonia. It is a pyridoxal phosphate protein. The enzyme also forms pyruvate from D-tyrosine, L-cysteine, S-methyl-L-cysteine, L-serine, and D-serine, although at a slower rate. EC 4.1.99.2.Tyrphostins: A family of synthetic protein tyrosine kinase inhibitors. They selectively inhibit receptor autophosphorylation and are used to study receptor function.Cells, Cultured: 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.Proto-Oncogene Proteins c-abl: Non-receptor tyrosine kinases encoded by the C-ABL GENES. They are distributed in both the cytoplasm and the nucleus. c-Abl plays a role in normal HEMATOPOIESIS especially of the myeloid lineage. Oncogenic transformation of c-abl arises when specific N-terminal amino acids are deleted, releasing the kinase from negative regulation.Protein Binding: 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.SH2 Domain-Containing Protein Tyrosine Phosphatases: A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.Focal Adhesion Protein-Tyrosine Kinases: A family of non-receptor, PROLINE-rich protein-tyrosine kinases.Mutation: 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.Transfection: 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.Adaptor Proteins, Signal Transducing: A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymesPyrimidines: A family of 6-membered heterocyclic compounds occurring in nature in a wide variety of forms. They include several nucleic acid constituents (CYTOSINE; THYMINE; and URACIL) and form the basic structure of the barbiturates.Receptor-Like Protein Tyrosine Phosphatases, Class 3: A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.Paxillin: Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.Focal Adhesion Kinase 1: A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.Kinetics: The rate dynamics in chemical or physical systems.Protein Tyrosine Phosphatase, Non-Receptor Type 2: A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.Phospholipase C gamma: A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.3T3 Cells: 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.Focal Adhesion Kinase 2: A non-receptor protein-tyrosine kinase that is expressed primarily in the BRAIN; OSTEOBLASTS; and LYMPHOID CELLS. In the CENTRAL NERVOUS SYSTEM focal adhesion kinase 2 modulates ION CHANNEL function and MITOGEN-ACTIVATED PROTEIN KINASES activity.Receptor-Like Protein Tyrosine Phosphatases, Class 4: A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.fms-Like Tyrosine Kinase 3: A receptor tyrosine kinase that is involved in HEMATOPOIESIS. It is closely related to FMS PROTO-ONCOGENE PROTEIN and is commonly mutated in acute MYELOID LEUKEMIA.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Lactams, Macrocyclic: LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.Precipitin Tests: 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.GRB2 Adaptor Protein: A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).Quinones: Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.Benzoquinones: Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Protein Tyrosine Phosphatases, Non-Receptor: A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.Recombinant Fusion Proteins: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Janus Kinase 2: A Janus kinase subtype that is involved in signaling from GROWTH HORMONE RECEPTORS; PROLACTIN RECEPTORS; and a variety of CYTOKINE RECEPTORS such as ERYTHROPOIETIN RECEPTORS and INTERLEUKIN RECEPTORS. Dysregulation of Janus kinase 2 due to GENETIC TRANSLOCATIONS have been associated with a variety of MYELOPROLIFERATIVE DISORDERS.Tumor Cells, Cultured: 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.Receptor, Insulin: A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Phosphatidylinositol 3-Kinases: Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.Type C Phospholipases: A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.Protein Tyrosine Phosphatase, Non-Receptor Type 12: A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.Blotting, Western: 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.Epidermal Growth Factor: A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form.Benzamides: BENZOIC ACID amides.PiperazinesIsoflavones: 3-Phenylchromones. Isomeric form of FLAVONOIDS in which the benzene group is attached to the 3 position of the benzopyran ring instead of the 2 position.Mitogen-Activated Protein Kinases: A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).Receptor-Like Protein Tyrosine Phosphatases, Class 5: A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.Cell Division: The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Shc Signaling Adaptor Proteins: A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.Immunoblotting: 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.Tetranitromethane: Corrosive oxidant, explosive; additive to diesel and rocket fuels; causes skin and lung irritation; proposed war gas. A useful reagent for studying the modification of specific amino acids, particularly tyrosine residues in proteins. Has also been used for studying carbanion formation and for detecting the presence of double bonds in organic compounds.QuinazolinesSubstrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Calcium-Calmodulin-Dependent Protein Kinases: A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)Proto-Oncogene Proteins c-met: Cell surface protein-tyrosine kinase receptors for HEPATOCYTE GROWTH FACTOR. They consist of an extracellular alpha chain which is disulfide-linked to the transmembrane beta chain. The cytoplasmic portion contains the catalytic domain and sites critical for the regulation of kinase activity. Mutations of the gene for PROTO-ONCOGENE PROTEINS C-MET are associated with papillary renal carcinoma and other neoplasia.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Cell Line, Tumor: A cell line derived from cultured tumor cells.Receptors, Platelet-Derived Growth Factor: Specific receptors on cell membranes that react with PLATELET-DERIVED GROWTH FACTOR, its analogs, or antagonists. The alpha PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR ALPHA) and the beta PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR BETA) are the two principle types of PDGF receptors. Activation of the protein-tyrosine kinase activity of the receptors occurs by ligand-induced dimerization or heterodimerization of PDGF receptor types.Cytoskeletal Proteins: Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Proto-Oncogene Proteins c-kit: A protein-tyrosine kinase receptor that is specific for STEM CELL FACTOR. This interaction is crucial for the development of hematopoietic, gonadal, and pigment stem cells. Genetic mutations that disrupt the expression of PROTO-ONCOGENE PROTEINS C-KIT are associated with PIEBALDISM, while overexpression or constitutive activation of the c-kit protein-tyrosine kinase is associated with tumorigenesis.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Cell Adhesion: Adherence of cells to surfaces or to other cells.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.PhosphopeptidesIsoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Cell Adhesion Molecules: Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Crk-Associated Substrate Protein: Crk-associated substrate was originally identified as a highly phosphorylated 130 kDa protein that associates with ONCOGENE PROTEIN CRK and ONCOGENE PROTEIN SRC. It is a signal transducing adaptor protein that undergoes tyrosine PHOSPHORYLATION in signaling pathways that regulate CELL MIGRATION and CELL PROLIFERATION.RNA, Messenger: 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.Receptor Tyrosine Kinase-like Orphan Receptors: A family of cell surface receptors that were originally identified by their structural homology to neurotropic TYROSINE KINASES and referred to as orphan receptors because the associated ligand and signaling pathways were unknown. Evidence for the functionality of these proteins has been established by experiments showing that disruption of the orphan receptor genes results in developmental defects.Genes, src: Retrovirus-associated DNA sequences (src) originally isolated from the Rous sarcoma virus (RSV). The proto-oncogene src (c-src) codes for a protein that is a member of the tyrosine kinase family and was the first proto-oncogene identified in the human genome. The human c-src gene is located at 20q12-13 on the long arm of chromosome 20.Fusion Proteins, bcr-abl: Translation products of a fusion gene derived from CHROMOSOMAL TRANSLOCATION of C-ABL GENES to the genetic locus of the breakpoint cluster region gene on chromosome 22. Several different variants of the bcr-abl fusion proteins occur depending upon the precise location of the chromosomal breakpoint. These variants can be associated with distinct subtypes of leukemias such as PRECURSOR CELL LYMPHOBLASTIC LEUKEMIA-LYMPHOMA; LEUKEMIA, MYELOGENOUS, CHRONIC, BCR-ABL POSITIVE; and NEUTROPHILIC LEUKEMIA, CHRONIC.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Receptors, Cell Surface: Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.Janus Kinase 1: A Janus kinase subtype that is involved in signaling from a broad variety of CYTOKINE RECEPTORS.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.DNA-Binding Proteins: 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.Indoles: Benzopyrroles with the nitrogen at the number one carbon adjacent to the benzyl portion, in contrast to ISOINDOLES which have the nitrogen away from the six-membered ring.STAT3 Transcription Factor: A signal transducer and activator of transcription that mediates cellular responses to INTERLEUKIN-6 family members. STAT3 is constitutively activated in a variety of TUMORS and is a major downstream transducer for the CYTOKINE RECEPTOR GP130.Jurkat Cells: A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.Mitogen-Activated Protein Kinase 1: A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.Insulin Receptor Substrate Proteins: A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.Antineoplastic Agents: Substances that inhibit or prevent the proliferation of NEOPLASMS.STAT5 Transcription Factor: A signal transducer and activator of transcription that mediates cellular responses to a variety of CYTOKINES. Stat5 activation is associated with transcription of CELL CYCLE regulators such as CYCLIN KINASE INHIBITOR P21 and anti-apoptotic genes such as BCL-2 GENES. Stat5 is constitutively activated in many patients with acute MYELOID LEUKEMIA.Receptor, trkA: A protein-tyrosine kinase receptor that is specific for NERVE GROWTH FACTOR; NEUROTROPHIN 3; neurotrophin 4, neurotrophin 5. It plays a crucial role in pain sensation and thermoregulation in humans. Gene mutations that cause loss of receptor function are associated with CONGENITAL INSENSITIVITY TO PAIN WITH ANHIDROSIS, while gene rearrangements that activate the protein-tyrosine kinase function are associated with tumorigenesis.TYK2 Kinase: A Janus kinase subtype that is involved in signaling from a broad variety of CYTOKINE RECEPTORS. The TYK2 kinase is considered the founding member of the janus kinase family and was initially discovered as a signaling partner for the INTERFERON ALPHA-BETA RECEPTOR. The kinase has since been shown to signal from several INTERLEUKIN RECEPTORS.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Ligands: A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)Proto-Oncogene Proteins c-crk: Signal transducing adaptor proteins that contain SRC HOMOLOGY DOMAINS and play a role in CYTOSKELETON reorganization. c-crk protein is closely related to ONCOGENE PROTEIN V-CRK and includes several alternatively spliced isoforms.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Adaptor Proteins, Vesicular Transport: A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.Receptors, Antigen, B-Cell: IMMUNOGLOBULINS on the surface of B-LYMPHOCYTES. Their MESSENGER RNA contains an EXON with a membrane spanning sequence, producing immunoglobulins in the form of type I transmembrane proteins as opposed to secreted immunoglobulins (ANTIBODIES) which do not contain the membrane spanning segment.Immunoprecipitation: The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.Protein Tyrosine Phosphatase, Non-Receptor Type 13: A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing five different PDZ domains, and a carboxyl-terminal phosphatase domain. In addition to playing a role as a regulator of the FAS RECEPTOR activity this subtype interacts via its PDZ and FERM domains with a variety of INTRACELLULAR SIGNALING PROTEINS and CYTOSKELETAL PROTEINS.Oncogene Proteins v-abl: Transforming proteins encoded by the abl oncogenes. Oncogenic transformation of c-abl to v-abl occurs by insertional activation that results in deletions of specific N-terminal amino acids.Receptor, Platelet-Derived Growth Factor beta: A PDGF receptor that binds specifically to the PDGF-B chain. It contains a protein-tyrosine kinase activity that is involved in SIGNAL TRANSDUCTION.Platelet-Derived Growth Factor: Mitogenic peptide growth hormone carried in the alpha-granules of platelets. It is released when platelets adhere to traumatized tissues. Connective tissue cells near the traumatized region respond by initiating the process of replication.Molecular Weight: The sum of the weight of all the atoms in a molecule.Receptors, Antigen, T-Cell: Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (ANTIGENS, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains.Cell Transformation, Neoplastic: 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.Milk Proteins: The major protein constituents of milk are CASEINS and whey proteins such as LACTALBUMIN and LACTOGLOBULINS. IMMUNOGLOBULINS occur in high concentrations in COLOSTRUM and in relatively lower concentrations in milk. (Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p554)Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.T-Lymphocytes: Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Janus Kinase 3: A Janus kinase subtype that is predominantly expressed in hematopoietic cell. It is involved in signaling from a broad variety of CYTOKINE RECEPTORS including ones that utilize the INTERLEUKIN RECEPTOR COMMON GAMMA SUBUNIT.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Proto-Oncogene Proteins c-vav: Proto-oncogene proteins that are guanine nucleotide exchange factors for RHO GTPASES. They also function as signal transducing adaptor proteins.Receptor Aggregation: Chemically stimulated aggregation of cell surface receptors, which potentiates the action of the effector cell.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Proto-Oncogene Proteins c-hck: Members of the src-family tyrosine kinase family that are strongly expressed in MYELOID CELLS and B-LYMPHOCYTES.DNA Primers: 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.Proto-Oncogene Proteins c-ret: Receptor protein-tyrosine kinases involved in the signaling of GLIAL CELL-LINE DERIVED NEUROTROPHIC FACTOR ligands. They contain an extracellular cadherin domain and form a receptor complexes with GDNF RECEPTORS. Mutations in ret protein are responsible for HIRSCHSPRUNG DISEASE and MULTIPLE ENDOCRINE NEOPLASIA TYPE 2.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Mitogen-Activated Protein Kinase 3: A 44-kDa extracellular signal-regulated MAP kinase that may play a role the initiation and regulation of MEIOSIS; MITOSIS; and postmitotic functions in differentiated cells. It phosphorylates a number of TRANSCRIPTION FACTORS; and MICROTUBULE-ASSOCIATED PROTEINS.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.PC12 Cells: A CELL LINE derived from a PHEOCHROMOCYTOMA of the rat ADRENAL MEDULLA. PC12 cells stop dividing and undergo terminal differentiation when treated with NERVE GROWTH FACTOR, making the line a useful model system for NERVE CELL differentiation.Models, Biological: 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.Apoptosis: 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.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Down-Regulation: 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.Insulin: A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)STAT1 Transcription Factor: A signal transducer and activator of transcription that mediates cellular responses to INTERFERONS. Stat1 interacts with P53 TUMOR SUPPRESSOR PROTEIN and regulates expression of GENES involved in growth control and APOPTOSIS.Rats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Cortactin: A microfilament protein that interacts with F-ACTIN and regulates cortical actin assembly and organization. It is also an SH3 DOMAIN containing phosphoprotein, and it mediates tyrosine PHOSPHORYLATION based SIGNAL TRANSDUCTION by PROTO-ONCOGENE PROTEIN PP60(C-SRC).Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.Receptor, erbB-2: A cell surface protein-tyrosine kinase receptor that is overexpressed in a variety of ADENOCARCINOMAS. It has extensive homology to and heterodimerizes with the EGF RECEPTOR, the ERBB-3 RECEPTOR, and the ERBB-4 RECEPTOR. Activation of the erbB-2 receptor occurs through heterodimer formation with a ligand-bound erbB receptor family member.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Receptor, EphB2: An eph family receptor found widely expressed in embryonic and adult tissues. High levels of EphB2 receptor are observed in growing AXONS and NERVE FIBERS. Several isoforms of the protein exist due to multiple alternative mRNA splicing.Cell Proliferation: All of the processes involved in increasing CELL NUMBER including CELL DIVISION.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Cell Line, Transformed: Eukaryotic cell line obtained in a quiescent or stationary phase which undergoes conversion to a state of unregulated growth in culture, resembling an in vitro tumor. It occurs spontaneously or through interaction with viruses, oncogenes, radiation, or drugs/chemicals.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Mice, Inbred C57BLOncogene Proteins: Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).Dihydroxyphenylalanine: A beta-hydroxylated derivative of phenylalanine. The D-form of dihydroxyphenylalanine has less physiologic activity than the L-form and is commonly used experimentally to determine whether the pharmacological effects of LEVODOPA are stereospecific.Receptors, Growth Factor: Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.Gene Expression Regulation: 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.Leukemia, Myelogenous, Chronic, BCR-ABL Positive: Clonal hematopoetic disorder caused by an acquired genetic defect in PLURIPOTENT STEM CELLS. It starts in MYELOID CELLS of the bone marrow, invades the blood and then other organs. The condition progresses from a stable, more indolent, chronic phase (LEUKEMIA, MYELOID, CHRONIC PHASE) lasting up to 7 years, to an advanced phase composed of an accelerated phase (LEUKEMIA, MYELOID, ACCELERATED PHASE) and BLAST CRISIS.Antigens, CD: Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.MAP Kinase Signaling System: An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.Sperm Capacitation: The structural and functional changes by which SPERMATOZOA become capable of oocyte FERTILIZATION. It normally requires exposing the sperm to the female genital tract for a period of time to bring about increased SPERM MOTILITY and the ACROSOME REACTION before fertilization in the FALLOPIAN TUBES can take place.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Receptor-Like Protein Tyrosine Phosphatases, Class 7: A subclass of receptor-like protein tryosine phosphatases that contain a short extracellular domain, a cytosolic kinase-interaction domain, and single protein tyrosine kinase domain.Neurons: The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.Nitriles: Organic compounds containing the -CN radical. The concept is distinguished from CYANIDES, which denotes inorganic salts of HYDROGEN CYANIDE.Nerve Growth Factors: Factors which enhance the growth potentialities of sensory and sympathetic nerve cells.Nerve Tissue ProteinsAntibodies, Monoclonal: Antibodies produced by a single clone of cells.Dopamine: One of the catecholamine NEUROTRANSMITTERS in the brain. It is derived from TYROSINE and is the precursor to NOREPINEPHRINE and EPINEPHRINE. Dopamine is a major transmitter in the extrapyramidal system of the brain, and important in regulating movement. A family of receptors (RECEPTORS, DOPAMINE) mediate its action.Hepatocyte Growth Factor: Multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. Its receptor is PROTO-ONCOGENE PROTEINS C-MET.Proto-Oncogene Proteins c-akt: A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.Antigens, CD45: High-molecular weight glycoproteins uniquely expressed on the surface of LEUKOCYTES and their hemopoietic progenitors. They contain a cytoplasmic protein tyrosine phosphatase activity which plays a role in intracellular signaling from the CELL SURFACE RECEPTORS. The CD45 antigens occur as multiple isoforms that result from alternative mRNA splicing and differential usage of three exons.Receptor, trkB: A protein-tyrosine kinase receptor that is specific for BRAIN-DERIVED NEUROTROPHIC FACTOR; NEUROTROPHIN 3; neurotrophin 4 and neurotrophin 5. It is widely expressed in nervous tissue and plays a role in mediating the effects of neurotrophins on growth and differentiation of neuronal cells.Catechols: A group of 1,2-benzenediols that contain the general formula R-C6H5O2.Pyrroles: Azoles of one NITROGEN and two double bonds that have aromatic chemical properties.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. (1/13395)
BACKGROUND: The adaptor protein Gads is a Grb2-related protein originally identified on the basis of its interaction with the tyrosine-phosphorylated form of the docking protein Shc. Gads protein expression is restricted to hematopoietic tissues and cell lines. Gads contains a Src homology 2 (SH2) domain, which has previously been shown to have a similar binding specificity to that of Grb2. Gads also possesses two SH3 domains, but these have a distinct binding specificity to those of Grb2, as Gads does not bind to known Grb2 SH3 domain targets. Here, we investigated whether Gads is involved in T-cell signaling. RESULTS: We found that Gads is highly expressed in T cells and that the SLP-76 adaptor protein is a major Gads-associated protein in vivo. The constitutive interaction between Gads and SLP-76 was mediated by the carboxy-terminal SH3 domain of Gads and a 20 amino-acid proline-rich region in SLP-76. Gads also coimmunoprecipitated the tyrosine-phosphorylated form of the linker for activated T cells (LAT) adaptor protein following cross-linking of the T-cell receptor; this interaction was mediated by the Gads SH2 domain. Overexpression of Gads and SLP-76 resulted in a synergistic augmentation of T-cell signaling, as measured by activation of nuclear factor of activated T cells (NFAT), and this cooperation required a functional Gads SH2 domain. CONCLUSIONS: These results demonstrate that Gads plays an important role in T-cell signaling via its association with SLP-76 and LAT. Gads may promote cross-talk between the LAT and SLP-76 signaling complexes, thereby coupling membrane-proximal events to downstream signaling pathways. (+info)Tyrosine phosphorylation is required for actin-based motility of vaccinia but not Listeria or Shigella. (2/13395)
Studies of the actin-based motility of pathogens have provided important insights into the events occurring at the leading edge of motile cells [1] [2] [3]. To date, several actin-cytoskeleton-associated proteins have been implicated in the motility of Listeria or Shigella: vasodilator-stimulated phosphoprotein (VASP), vinculin and the actin-related protein complex of Arp2 and Arp3 [4] [5] [6] [7]. To further investigate the underlying mechanism of actin-tail assembly, we examined the localization of components of the actin cytoskeleton including Arp3, VASP, vinculin and zyxin during vaccinia, Listeria and Shigella infections. The most striking difference between the systems was that a phosphotyrosine signal was observed only at the site of vaccinia actin-tail assembly. Micro-injection experiments demonstrated that a phosphotyrosine protein plays an important role in vaccinia actin-tail formation. In addition, we observed a phosphotyrosine signal on clathrin-coated vesicles that have associated actin-tail-like structures and on endogenous vesicles in Xenopus egg extracts which are able to nucleate actin tails [8] [9]. Our observations indicate that a host phosphotyrosine protein is required for the nucleation of actin filaments by vaccinia and suggest that this phosphoprotein might be associated with cellular membranes that can nucleate actin. (+info)Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation. (3/13395)
Cbl-b, a mammalian homolog of Cbl, consists of an N-terminal region (Cbl-b-N) highly homologous to oncogenic v-Cbl, a Ring finger, and a C-terminal region containing multiple proline-rich stretches and potential tyrosine phosphorylation sites. In the present study, we demonstrate that upon engagement of the T cell receptor (TCR), endogenous Cbl-b becomes rapidly tyrosine-phosphorylated. In heterogeneous COS-1 cells, Cbl-b was phosphorylated on tyrosine residues by both Syk- (Syk/Zap-70) and Src- (Fyn/Lck) family kinases, with Syk kinase inducing the most prominent effect. Syk associates and phosphorylates Cbl-b in Jurkat T cells. A Tyr-316 Cbl-binding site in Syk was required for the association with and for the maximal tyrosine phosphorylation of Cbl-b. Mutation at a loss-of-function site (Gly-298) in Cbl-b-N disrupts its interaction with Syk. Cbl-b constitutively binds Grb2 and becomes associated with Crk-L upon TCR stimulation. The Grb2- and the Crk-L-binding regions were mapped to the C-terminus of Cbl-b. The Crk-L-binding sites were further determined to be Y655DVP and Y709KIP, with the latter being the primary binding site. Taken together, these results implicate that Cbl-b is involved in TCR-mediated intracellular signaling pathways. (+info)Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. (4/13395)
The protein tyrosine kinase PYK2 has been implicated in signaling pathways activated by G-protein-coupled receptors, intracellular calcium, and stress signals. Here we describe the molecular cloning and characterization of a novel family of PYK2-binding proteins designated Nirs (PYK2 N-terminal domain-interacting receptors). The three Nir proteins (Nir1, Nir2, and Nir3) bind to the amino-terminal domain of PYK2 via a conserved sequence motif located in the carboxy terminus. The primary structures of Nirs reveal six putative transmembrane domains, a region homologous to phosphatidylinositol (PI) transfer protein, and an acidic domain. The Nir proteins are the human homologues of the Drosophila retinal degeneration B protein (rdgB), a protein implicated in the visual transduction pathway in flies. We demonstrate that Nirs are calcium-binding proteins that exhibit PI transfer activity in vivo. Activation of PYK2 by agents that elevate intracellular calcium or by phorbol ester induce tyrosine phosphorylation of Nirs. Moreover, PYK2 and Nirs exhibit similar expression patterns in several regions of the brain and retina. In addition, PYK2-Nir complexes are detected in lysates prepared from cultured cells or from brain tissues. Finally, the Nir1-encoding gene is located at human chromosome 17p13.1, in proximity to a locus responsible for several human retinal diseases. We propose that the Nir and rdgB proteins represent a new family of evolutionarily conserved PYK2-binding proteins that play a role in the control of calcium and phosphoinositide metabolism downstream of G-protein-coupled receptors. (+info)Identification of a new Pyk2 target protein with Arf-GAP activity. (5/13395)
Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap. (+info)BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells. (6/13395)
Signaling through the B cell receptor (BCR) is essential for B cell function and development. Despite the key role of Syk in BCR signaling, little is known about the mechanism by which Syk transmits downstream effectors. BLNK (B cell LiNKer protein), a substrate for Syk, is now shown to be essential in activating phospholipase C (PLC)gamma 2 and JNK. The BCR-induced PLC gamma 2 activation, but not the JNK activation, was restored by introduction of PLC gamma 2 membrane-associated form into BLNK-deficient B cells. As JNK activation requires both Rac1 and PLC gamma 2, our results suggest that BLNK regulates the Rac1-JNK pathway, in addition to modulating PLC gamma 2 localization. (+info)Role of nitric oxide in lipopolysaccharide-induced hepatic injury in D-galactosamine-sensitized mice as an experimental endotoxic shock model. (7/13395)
The role of nitric oxide (NO) in lipopolysaccharide (LPS)-induced hepatic injury was studied in D-galactosamine (D-GalN)-sensitized mice. The inducible isoform of NO synthase (iNOS) was immunohistochemically detected on hepatocytes around blood vessels in livers of mice injected with D-GalN and LPS not on hepatocytes in mice injected with D-GalN or LPS alone, although mRNA for iNOS was found in those mice. Nitrotyrosine (NT) was also found in livers of mice injected with D-GalN and LPS. The localization of NT was consistent with that of iNOS, and the time courses of NT and iNOS expression were almost the same. Expression of iNOS and NT was detected exclusively in the hepatic lesions of mice injected with D-GalN and LPS. Anti-tumor necrosis factor alpha neutralizing antibody inhibited iNOS and NT expression and hepatic injury. The results suggested that NO from iNOS may play a role in LPS-induced hepatic injury on D-GalN-sensitized mice as an experimental endotoxic shock model. (+info)Yops of Yersinia enterocolitica inhibit receptor-dependent superoxide anion production by human granulocytes. (8/13395)
The virulence plasmid-borne genes encoding Yersinia adhesin A (YadA) and several Yersinia secreted proteins (Yops) are involved in the inhibition of phagocytosis and killing of Yersinia enterocolitica by human granulocytes. One of these Yops, YopH, dephosphorylates multiple tyrosine-phosphorylated proteins in eukaryotic cells and is involved in the inhibition of phagocytosis of Y. enterocolitica by human granulocytes. We investigated whether antibody- and complement-opsonized plasmid-bearing (pYV+) Y. enterocolitica inhibits O2- production by human granulocytes in response to various stimuli and whether YopH is involved. Granulocytes were preincubated with mutant strains unable to express YadA or to secrete Yops or YopH. O2- production by granulocytes during stimulation was assessed by measuring the reduction of ferricytochrome c. PYV+ Y. enterocolitica inhibited O2- production by granulocytes incubated with opsonized Y. enterocolitica or N-formyl-Met-Leu-Phe (f-MLP). This inhibitory effect mediated by pYV did not affect receptor-independent O2- production by granulocytes in response to phorbol myristate acetate, indicating that NADPH activity remained unaffected after activation of protein kinase C. The inhibition of f-MLP-induced O2- production by granulocytes depends on the secretion of Yops and not on the expression of YadA. Insertional inactivation of the yopH gene abrogated the inhibition of phagocytosis of antibody- and complement-opsonized Y. enterocolitica by human granulocytes but not of the f-MLP-induced O2- production by granulocytes or tyrosine phosphorylation of granulocyte proteins. These findings suggest that the specific targets for YopH are not present in f-MLP receptor-linked signal transduction and that other Yop-mediated mechanisms are involved. (+info)
Transforming gene product of Rous sarcoma virus phosphorylates tyrosine | PNAS
Tyrosine and tyrosinate fluorescence of pig intestinal Ca2+-binding protein | Biochemical Journal
A role for cholecystokinin-stimulated protein tyrosine phosphorylation in regulated secretion by the pancreatic acinar cell<...![Amino Acid and Protein Metabolism in Hospitalized Patients as Measured by l-[U-14C]Tyrosine and l-[1-14C]Leucine | Clinical...](data:image/png;base64,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)
Amino Acid and Protein Metabolism in Hospitalized Patients as Measured by l-[U-14C]Tyrosine and l-[1-14C]Leucine | Clinical...
Phosphorylation of Tyrosine Residues in the Kinase Domain and Juxtamembrane Region Regulates the Biological and Catalytic...Disease tropism of c-erbB: Effects of carboxyl-terminal tyrosine and internal mutations on tissue-specific transformation<...Vav in natural killer cells is tyrosine phosphorylated upon cross-linking of Fcγ RIIIA and is constitutively associated with a...
Association of tyrosine and serine kinases with the B cell surface antigen CD20. Induction via CD20 of tyrosine phosphorylation...
Injury and Trinucleotides Transactivate Specific Tyrosine Residues of the EGF Receptor Leading to Downstream Signaling | IOVS ...
Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. | Journal of...
ADHD treatments: Does Tyrosine for ADHD Actually Work as a Supplementation Strategy?(part 4)Mitochondria and regulated tyrosine nitration | Biochemical Society Transactions
Latching on to LAT | Science Signaling
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IJMS | Free Full-Text | CCR7 Sulfotyrosine Enhances CCL21 BindingT Cell Activation-Induced CrkII Binding to the Zap70 Protein Tyrosine Kinase Is Mediated by Lck-Dependent Phosphorylation of...Proteinuria and hypertension with tyrosine kinase inhibitors<...
VASCULAR INJURY CHANGE TYROSINE PHOSPHORYLATION OF FOCAL ADHESION PROTEINS | Heart
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.Download Resistance To Tyrosine Kinase Inhibitors 2016
Tyrosine phosphorylation of 3BP2 is indispensable for the interaction with VAV3 in chicken DT40 cells (Journal Article) |...
Role of tyrosine kinase signaling for b-cell replication and survival
Protein Tyrosine Kinase/RTK (Inhibitors Agonists Modulators Antagonists)-MedChemExpress.com
Receptor Tyrosine Protein Kinase ERBB 4 (Tyrosine Kinase Type Cell Surface Receptor HER4 or Proto Oncogene Like Protein c ErbB...
Anti-Nitrotyrosine AntibodiesStudies of Protein Metabolism in Man with Infusions of [14C]Tyrosine | Clinical Science | Portland Press
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The JAK‐binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop | The EMBO JournalDetecting Tyrosine-Phosphorylated Proteins by Western Blot Analysis - Current Protocols in Immunology - Sawasdikosol - Wiley...B for Biology: Signal Transduction Pathway - The JAK/STAT PathwaysTyrosine InformationBuy l tyrosine best brand - l tyrosine best brand on sale
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Tyrosine phosphorylation induced by EGF stimulation. Ce | Open-i
AgroParisTech - Serine/threonine/tyrosine phosphorylation regulates DNA binding of bacterial transcriptional regulatorsIdentification of tyrosine phosphorylation sites in human Gab-1 protein by EGF receptor kinase in vitro
ABL1 | SelfDecode | Genome AnalysisTyrosine phosphorylation of Syk after stimulation of NK | Open-i
Cross-linking of tyrosine-containing peptides by hydrogen peroxide-activated <em class="EmphasisTypeItalic">Coprinus Cinereus<...
Erratum: Mutagenesis of T cell antigen receptor ζ chain tyrosine residues. Effects on tyrosine phosphorylation and lymphokine...
Suppression of c-Cbl Tyrosine Phosphorylation Inhibits Neointimal Formation in Balloon-Injured Rat Arteries | Circulation
Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells | [email protected]Distinct tyrosine phosphorylation sites in JAK3 kinase domain positively and negatively regulate its enzymatic activity | PNAS
Hepatic tyrosine-phosphorylated proteins identified and localized following in vivo inhibition of protein tyrosine phosphatases...Association of the tyrosine phosphorylated epidermal growth factor receptor with a 55-kD tyrosine phosphorylated protein at the...Protein kinase C activation induces tyrosine phosphorylation of the NR2A and NR2B subunits of the NMDA receptor. - Department...Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS - CORE
Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells | Journal of Cell...
CSFR (human)Deficits in the Activation and Phosphorylation of Hippocampal Tyrosine Hydroxylase in the Aged Fischer 344 Rat Following...Identification of the src family kinases, Lck and Fgr in platelets: Their tyrosine phosphorylation status and subcellular...
Time-resolved Mass Spectrometry of Tyrosine Phosphorylation Sites in the Epidermal Growth Factor Receptor Signaling Network...Response to interferons and antibacterial innate immunity in the absence of tyrosine‐phosphorylated STAT1 | EMBO ReportsStructure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism | The EMBO JournalTyrosine phosphorylation controls Runx2-mediated subnuclear targeting of YAP to repress transcription<...Repression of SHP-1 expression by p53 leads to trkA tyrosine phosphorylation and suppression of breast cancer cell...
"High-Throughput Phosphotyrosine Profiling Using SH2 Domains" by Kazuya Machida, Christopher M. Thompson et al.
Tyrosine Protein Kinase SYK - Pipeline Review, H2 2020
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The coordinated action of protein tyrosine phosphatases and kinases in cell signaling - CSHL Scientific Digital RepositoryThrombospondin-1 induces tyrosine phosphorylation of adherens junction proteins and regulates an endothelial paracellular...l tyrosine buy - l tyrosine buy Manufacturer
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Leukocyte receptor tyrosine kinase - WikipediaRole of Src Homology 2-Containing Tyrosine Phosphatase 2 on Proliferation of Rat Smooth Muscle Cells | Arteriosclerosis,...
Importance of protein Ser/Thr/Tyr phosphorylation for bacterial pathogenesis
P130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading | IRIS Uni TorinoCyclolignans as Inhibitors of the Insulin-Like Growth Factor-1 Receptor and Malignant Cell Growth | Cancer Research
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tyrosine | InfopleaseTransforming gene product of Rous sarcoma virus phosphorylates tyrosine | PNAS
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Product information, instructions, health benefits, and usage for Tyrosine
TYROSINE KINASE INHIBITORS
Tyrosine hydroxylase deficiency: MedlinePlus Genetics
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- In contrast, eukaryotic tyrosine phosphorylation has long been considered a major tenet in signal transduction mechanisms, with a diverse array of tyrosine kinases and protein substrates ( 6 ). (asm.org)
- The topic of bacterial tyrosine kinases (BY-kinases) has been extensively reviewed by many groups ( 14 - 16 ), highlighting the diverse aspects of bacterial tyrosine kinase biology. (asm.org)
- Notably, most BY-kinases characterized to date reveal a structurally distinct class of proteins from the well-characterized "Hanks-type" eukaryotic tyrosine kinases ( 14 ). (asm.org)
- In this report, we have shown that Syk, but not Abl family protein-tyrosine kinases, is critical for BCR-mediated tyrosine phosphorylation of 3BP2 in chicken DT40 cells. (osti.gov)
- Protein-tyrosine kinases (PTKs) catalyze the transfer of the γ-phosphate of ATP to tyrosine residues of protein substrates, are critical components of signaling pathways that control cellular proliferation and differentiation. (medchemexpress.com)
- In addition, nonreceptor tyrosine kinases (NRTKs), which include Src, JAKs, and Abl, among others, are integral components of the signaling cascades triggered by RTKs and by other cell surface receptors such as GPCRs and receptors of the immune system. (medchemexpress.com)
- Tyrosine residues in enzymes have frequently been shown to be associated with active sites. (infoplease.com)
- Sulfation sites are have a tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues, a detailed description of the characteristics of the sulfation site is available from PROSITE (PROSITE pattern: PS00003). (bionity.com)
- Phosphorylated proteins are generally modified at one or more serine, threonine, or tyrosine residues. (asm.org)
- RTKs are transmembrane glycoproteins that are activated by the binding of their ligands, and they transduce the extracellular signal to the cytoplasm by phosphorylating tyrosine residues on the receptors themselves (autophosphorylation) and on downstream signaling proteins. (medchemexpress.com)
- tyrosine tī´rəsēn [ key ] , organic compound, one of the 20 amino acids commonly found in animal proteins. (infoplease.com)
- We infer from these observations that pp60 src is a novel protein kinase and that the modification of proteins via the phosphorylation of tyrosine is essential to the malignant transformation of cells by Rous sarcoma virus. (pnas.org)
- This is additional evidence of the functional similarity of these structurally related proteins and demonstrates that all uninfected vertebrate cells contain at least one protein kinase that phosphorylates tyrosine. (pnas.org)
- Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G-protein-coupled receptors, coagulation factors, serine protease inhibitors , extracellular matrix proteins, and hormones. (bionity.com)
- Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. (bionity.com)
- Tyrosine is an amino acid found in meat proteins. (memorialhealth.com)
- Within the last ten years, increasing numbers of global phosphoproteomic surveys of prokaryote species have revealed an abundance of tyrosine-phosphorylated proteins. (asm.org)
- Tyrosine phosphorylation of a small set of bacterial proteins was first linked to specialized cellular events, primarily with the synthesis and export of polysaccharides associated with lipopolysaccharide (LPS) and capsule biosynthesis ( 3 - 5 ). (asm.org)
- Tyrosine sulfation is a posttranslational modification where a sulfate group is added to a tyrosine residue of a protein molecule. (bionity.com)
- The reaction catalyzed by TPST is a transfer of sulfate from the universal sulfate donor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the side-chain hydroxyl group of a tyrosine residue. (bionity.com)
- In brief, a kinase acts to mediate transfer of a phosphate group (PO 4 ) to a protein substrate that has an accessible hydroxyl group on a tyrosine residue. (asm.org)
- The activated receptor is a tyrosine specific protein kinase, and tyrosine phosphorylation is one of the important mediators of EGF receptor (EGFR) signal transduction. (oregonstate.edu)
- By knock-out of TPST genes in mice, it may be observed that Tyrosine sulfation has effects on the growth of the mice, such as body weight, fecundity, and postnatal viability. (bionity.com)
- The protein kinase activity associated with pp60 src , the transforming protein of Rous sarcoma virus, was found to phosphorylate tyrosine when assayed in an immunoprecipitate. (pnas.org)
- This normal cellular protein, obtained from both chicken and human cells, also phosphorylated tyrosine when assayed in an immunoprecipitate. (pnas.org)
- Within a cellular context, several factors are required for a phosphate group to be covalently linked to tyrosine. (asm.org)
- When the enzyme that catalyzes the transformation of phenylalanine to tyrosine is not active because of a hereditary defect, the serious disease known as phenylketonuria (PKU) results. (infoplease.com)
- Tyrosine O-sulfate is a stable molecule and is excreted in urine in animals. (bionity.com)
- N-Acetyl Tyrosine supports brain function by improving the synthesis of the catecholamines norepinephrine and dopamine (neurotransmitters). (priceplow.com)
- Tyrosine O-sulfation is an irreversible process in vivo . (bionity.com)
- It uses material from the Wikipedia article "Tyrosine_sulfation" . (bionity.com)
- How should I take tyrosine? (uncmedicalcenter.org)
- No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. (bionity.com)
- Other defects in tyrosine metabolism include the rare hereditary disorder known as alkaptonuria, characterized by discharge of a urine which darkens on standing exposed to air. (infoplease.com)
- Tyrosine is a precursor of the adrenal hormones epinephrine and norepinephrine as well as of the thyroid hormones, including thyroxine . (infoplease.com)
- What we care about is that Tyrosine is a precursor to a variety of other natural substances that have been linked to having a profound impact on weight loss in human beings. (vaxxenlabs.com)
- However, within the last 10 years, detailed bacterial and archaeal phosphoproteomic studies have resulted in a fresh view that compares closely to the eukaryotic condition, where tyrosine phosphorylation is a central paradigm. (asm.org)
- Improved phosphotyrosine peptide enrichment techniques combined with highly sensitive mass spectrometry now reveal that tyrosine phosphorylation is indeed widespread across archaeal and bacterial proteomes ( 7 - 13 ). (asm.org)
- Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L -tyrosine to L -3,4-dihydroxyphenylalanine ( L -DOPA). (wikipedia.org)
- Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines . (wikipedia.org)
- In humans, tyrosine hydroxylase is encoded by the TH gene , and the enzyme is present in the central nervous system (CNS), peripheral sympathetic neurons and the adrenal medulla . (wikipedia.org)
- Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs). (wikipedia.org)
- Tyrosine hydroxylase catalyzes the reaction in which L -tyrosine is hydroxylated in the meta position to obtain L -3,4-dihydroxyphenylalanine ( L -DOPA). (wikipedia.org)
- Like the other aromatic amino acid hydroxylases (AAAHs), tyrosine hydroxylase use the cofactor tetrahydrobiopterin (BH 4 ) under normal conditions, although other similar molecules may also work as a cofactor for tyrosine hydroxylase. (wikipedia.org)
- Each of the four subunits in tyrosine hydroxylase is coordinated with an iron (II) atom presented in the active site. (wikipedia.org)
- Since L -DOPA is the precursor for the neurotransmitters dopamine, noradrenaline and adrenaline, tyrosine hydroxylase is therefore found in the cytosol of all cells containing these catecholamines . (wikipedia.org)
- This initial reaction catalyzed by tyrosine hydroxylase has been shown to be the rate limiting step in the production of catecholamines. (wikipedia.org)
- Tryptophan is a poor substrate for tyrosine hydroxylase, however it can hydroxylate L -phenylalanine to form L -tyrosine and small amounts of 3-hydroxyphenylalanine. (wikipedia.org)
- Tyrosine hydroxylase may also be involved in other reactions as well, such as oxidizing L -DOPA to form 5-S-cysteinyl-DOPA or other L -DOPA derivatives. (wikipedia.org)
- Tyrosine hydroxylase from rat showing two of its domains , the tetramerization domain (pink) and the catalytic domain (blue). (wikipedia.org)
- Tyrosine hydroxylase is a tetramer of four identical subunits ( homotetramer ). (wikipedia.org)
- In dopaminergic cells in the brain, tyrosine is converted to L-DOPA by the enzyme tyrosine hydroxylase (TH). (wikipedia.org)
- Tyrosine hydroxylase (TH) deficiency is a disorder that primarily affects movement, with symptoms that may range from mild to severe. (medlineplus.gov)
- The TH gene provides instructions for making the enzyme tyrosine hydroxylase, which is important for normal functioning of the nervous system. (medlineplus.gov)
- Tyrosine hydroxylase takes part in the pathway that produces a group of chemical messengers (hormones) called catecholamines. (medlineplus.gov)
- Tyrosine hydroxylase helps convert the protein building block (amino acid) tyrosine to a catecholamine called dopamine . (medlineplus.gov)
- Mutations in the TH gene result in reduced activity of the tyrosine hydroxylase enzyme. (medlineplus.gov)
- Furukawa Y, Kish S. Tyrosine Hydroxylase Deficiency. (medlineplus.gov)
- Furukawa Y, Kish SJ, Fahn S. Dopa-responsive dystonia due to mild tyrosine hydroxylase deficiency. (medlineplus.gov)
- Tyrosine Hydroxylase (phospho-Ser19) antibody detects endogenous levels of Tyrosine Hydroxylase only when phosphorylated at serine19. (abcam.com)
- Four Isoforms of Tyrosine Hydroxylase are Expressed in Human Brain. (abcam.com)
- Tyrosine Hydroxylase Activity in Parkinson's Disease. (rainbow.coop)
- Tyrosine hydroxylase is a BH4 (tetrahydrobiopterin) dependent enzyme which increases the conversion of tyrosine, an amino acid, to l-DOPA (l-dihydroxyphenylalanine. (rainbow.coop)
- The following antibody was used in this experiment: Tyrosine Hydroxylase Polyclonal Antibody from Thermo Fisher Scientific, catalog # P21962, RRID AB_2539844. (thermofisher.com)
- SDS-denatured rat tyrosine hydroxylase, purified from pheochromocytoma. (thermofisher.com)
- Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamine neurotransmitters (dopamine, epinephrine, and norepinephrine). (thermofisher.com)
- NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. (purdue.edu)
- Signals through Kit receptor tyrosine kinase are essential for development of erythrocytes, melanocytes, germ cells, mast cells and interstitial cells of Cajal (ICCs). (springer.com)
- Not long afterward, a group led by Stanley Cohen at Vanderbilt University reported that the transmembrane epidermal growth receptor protein, or EGFR, was also a tyrosine kinase. (asbmb.org)
- Proto-oncogene tyrosine-protein kinase Src, also known as proto-oncogene c-Src or simply c-Src , is a non-receptor tyrosine kinase protein that in humans is encoded by the SRC gene. (wikipedia.org)
- The Human Receptor Tyrosine Kinase (RTK) Pathways qBiomarker Somatic Mutation PCR Array is a translational research tool that allows rapid and accurate profiling of the somatic mutation status for. (qiagen.com)
- Here we report on the sequence analysis of members of the receptor tyrosine kinase (RTK) gene family in the genomes of glioblastoma brain tumors. (pnas.org)
- To find molecular targets, we have sequenced the coding exons for the kinase domains of 20 human receptor tyrosine kinase (RTK) genes in glioblastomas. (pnas.org)
- An isolated nucleic acid molecule encoding a novel human receptor type tyrosine kinase gene, KDR, is disclosed. (google.es)
- The present invention relates to an isolated nucleic acid molecule (polynucleotide) which encodes a human receptor tyrosine kinase, KDR, which is expressed on human endothelial cells. (google.es)
- An example is PDB 1IRK, the crystal structure of the tyrosine kinase domain of the human insulin receptor . (bionity.com)
- The first non-receptor tyrosine kinase identified was the v-src oncogenic protein. (bionity.com)
- The small molecule tyrosine kinase inhibitor (TKI) imatinib has revolutionized the treatment of chronic myeloid leukemia, and trastuzumab, the humanized monoclonal antibody against the ERBB2 receptor tyrosine kinase, has proved to have a high efficacy in 25% of breast cancers. (rti.org)
- A study published in Science Advances reveals the mechanism by which the receptor tyrosine kinase RET can increase neuronal survival in degenerative diseases. (phys.org)
- We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic inflammatory disorders, dephosphorylates NLRP3 upon inflammasome induction, allowing efficient NLRP3 activation and subsequent IL-1β release. (jci.org)
- Among the responsive sites, 20 were previously known to be tyrosine phosphorylated with insulin treatment, including sites on the insulin receptor and insulin receptor substrate-1. (diabetesjournals.org)
- Insulin binds to the insulin receptor at the cell surface and activates its tyrosine kinase activity, leading to autophosphorylation and phosphorylation of several receptor substrates. (diabetesjournals.org)
- Phosphorylation of selected tyrosine sites on receptor substrates is known to activate different pathways leading to increased glucose uptake, lipogenesis, and glycogen and protein synthesis, as well as to stimulation of cell growth ( 1 , 2 ). (diabetesjournals.org)
- For instance, serine phosphorylation on insulin receptor substrate (IRS)-1 induced by a variety of factors has been shown to interfere with the activating effects of tyrosine phosphorylation by decreasing binding to the insulin receptor or increasing degradation of IRS-1 ( 1 , 3 , 4 ). (diabetesjournals.org)
- Ser/Thr phosphorylation of the insulin receptor has also been shown to decrease tyrosine kinase activity ( 1 ). (diabetesjournals.org)
- Many of these factors are reflected in decreased amounts of the tyrosine-phosphorylated receptor and receptor substrates with concomitant reduction in downstream signaling. (diabetesjournals.org)
- Even though tyrosine phosphorylation plays a key role in insulin signaling, rather limited knowledge of specific phosphorylation sites, mainly focusing on tyrosine phosphorylation on the insulin receptor and IRS-1, is available so far. (diabetesjournals.org)
- Targeting Receptor-Type Protein Tyrosine Phosphatases with Biotherapeutics: Is Outside-in Better than Inside-Out? (mdpi.com)
- The Breast tumor kinase Brk is a prototypical non-myristoylated, non-receptor tyrosine kinase. (hu-berlin.de)
- I switched to Acetyl L-Tyrosine which has the same benefits but better pharmacological properties. (patientslikeme.com)
- I switched from taking L-Tyrosine to taking Acetyl L-Tyrosine because of better absorption and delivery of the Tyrosine across the blood brain barrier. (patientslikeme.com)
- After a few other experiences with supplements that supply nutrients in a form closer to the end products used by the body I decided to give the N-acetyl-L-Tyrosine form a try. (ei-resource.org)
- The positive effects on my mood and mental functioning I get with N-acetyl-L-Tyrosine last for around 3-4 hours so I need to take more than one dose per day to maintain them. (ei-resource.org)
- We are also actively investigating the regulation of Syk tyrosine kinase binding to membrane immune receptors and other signaling proteins. (purdue.edu)
- Tyrosine (Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. (wikipedia.org)
- We infer from these observations that pp60 src is a novel protein kinase and that the modification of proteins via the phosphorylation of tyrosine is essential to the malignant transformation of cells by Rous sarcoma virus. (pnas.org)
- This is additional evidence of the functional similarity of these structurally related proteins and demonstrates that all uninfected vertebrate cells contain at least one protein kinase that phosphorylates tyrosine. (pnas.org)
- Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G-protein-coupled receptors, coagulation factors, serine protease inhibitors , extracellular matrix proteins, and hormones. (bionity.com)
- Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. (bionity.com)
- To assess the physiological role of tyrosine nitration, it is crucial to identify the proteins that become nitrated. (nih.gov)
- Therefore, we treated lysates from RAW 264.7 cells with 1 mM peroxynitrite and immunoprecipitated tyrosine nitrated proteins. (nih.gov)
- Tyrosine is an amino acid found in meat proteins. (memorialhealth.com)
- Ligand binding stimulates the tyrosine kinase activity of the receptors, leading to recruitment of enzymes and adapter proteins that activate intracellular signaling pathways that control cell proliferation, differentiation, and numerous other biological processes. (cshlpress.com)
- It has resulted in the identification and relative temporal quantification of 122 tyrosine phosphorylation sites on 89 proteins. (diabetesjournals.org)
- These results show that insulin-elicited tyrosine phosphorylation is extensive and implicate a number of hitherto unrecognized proteins in insulin action. (diabetesjournals.org)
- We have recently developed a mass spectrometric methodology for the identification and quantification of tyrosine phosphorylation sites on many proteins ( 5 ). (diabetesjournals.org)
- Tyrosine is a conditionally essential amino acid derived from the essential amino acid phenylalanine which the body uses to synthesize proteins. (ei-resource.org)
- Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. (wikipedia.org)
- The present invention relates to compounds of the Formula I, the pharmaceutically acceptable salts and stereoisomers thereof, which inhibit, regulate and/or modulate tyrosine kinase signal transduction, compositions which contain these compounds, and methods of using them to treat tyrosine kinase-dependent. (google.com)
- Some scientific research has been conducted to understand the biological function and importance of tyrosine, a non-essential amino acid that, however, plays a pivotal role as a donor of phospho-tyrosine in signal transduction within the cells. (intechopen.com)
- QIAGEN provides a broad range of assay technologies for tyrosine kinase research that enable analysis of gene expression and regulation, epigenetic modification, and signal transduction pathway activation. (qiagen.com)
- BCR-ABL Tyrosine Kinase Inhibitors eg: Imatinib Mesylate, Dasatinib, and Nilotinib.2. (slideshare.net)
- S B Bhise, Abhijit D. Nalawade and Hitesh Wadhawa, Role of protein tyrosine kinase inhibitors in cancer therapeutics . (bionity.com)
- A new business intelligence report released by Up Market Research with title "Global Tyrosine Kinase Inhibitors Market Research Report 2019" that targets and provides comprehensive market analysis with future prospects to 2026. (openpr.com)
- Tyrosine Kinase Inhibitors Market research report delivers a close watch on leading competitors with strategic analysis, micro and macro market trend and scenarios, pricing analysis and a holistic overview of the market situations in the forecast period. (openpr.com)
- The report contains basic, secondary and advanced information pertaining to the Tyrosine Kinase Inhibitors Market global status and trend, market size, share, growth, trends analysis, segment and forecasts from 2019 - 2026. (openpr.com)
- The report for Tyrosine Kinase Inhibitors Market analysis & forecast 2019- 2026 is segmented into Product Segment, Application Segment & Major players. (openpr.com)
- Tyrosine Kinase Inhibitors Market Analysis and Forecast 2019- 2026" report helps the clients to take business decisions and to understand strategies of major players in the industry. (openpr.com)
- People taking MAO inhibitors that have been prescribed for depression need to strictly limit their intake of foods containing Tyrosine, and should not take any supplements containing this amino acid as it can lead to a sudden increase in blood pressure. (herbalremedies.com)
- Hendriks W, Bourgonje A, Leenders W, Pulido R. Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases. (mdpi.com)
- If I use 60mg of Armor thyroid per day, can I also use Tyrosine supplements of 500mg/3xday? (hubpages.com)
- This does not mean, however, that taking tyrosine supplements will avoid these particular circumstances. (healthyplace.com)
- Because tyrosine stimulates the production of serotonin, some experts speculate that L-tyrosine supplements may improve serotonin levels and decrease PMS symptoms. (healthyplace.com)
- Tyrosine is most commonly used in protein supplements to treat an inherited disorder called phenylketonuria (PKU). (webmd.com)
- Will L-Tyrosine Supplements Help My Erectile Dysfunction? (healthline.com)
- In the search for treatment options, L-tyrosine supplements are increasingly suggested to those with ED. Some research paints an optimistic picture, but how reliable is L-tyrosine? (healthline.com)
- Aside from high protein foods and ED supplements, it's also common to find tyrosine in other health supplements. (healthline.com)
- Before you take any tyrosine supplements, be sure to let your doctor know. (healthline.com)
- If you begin to experience side effects you didn't have prior to starting L-tyrosine, stop taking the supplements and contact your doctor immediately. (healthline.com)
- As of now, there don't appear to be too many major side effects associated with tyrosine supplements. (healthline.com)
- L-tyrosine supplements may trigger painful, long-lasting headaches called migraines in some people. (livestrong.com)
- Consult your doctor before trying tyrosine supplements. (livestrong.com)
- According to the University of Maryland Medical Center, or UMMC, studies have tested tyrosine as a treatment method for stress control, increased alertness and performance and for treating phenylketonuria, although the effectiveness of tyrosine supplements needs further research and studies to conclusively validate its health benefits. (livestrong.com)
- Tyrosine supplements are absorbed into your bloodstream and ultimately affect multiple systems in your body. (livestrong.com)
- Your doctor may prescribe tyrosine supplements in some cases, but inform him or her if you suffer from chronic headaches or migraines. (livestrong.com)
- Avoid taking tyrosine supplements if you take MAOIs, thyroid medication or medications used to treat Parkinson's disease. (livestrong.com)
- Stop taking L-tyrosine supplements immediately if you experience migraine symptoms, and consult your doctor. (livestrong.com)
- Your best bet is to avoid tyrosine supplements if you have frequent headaches or are taking an antidepressant categorized as an MAOI. (livestrong.com)
- As of 2011, more studies are needed to conclusively say L-tyrosine supplements are beneficial for athletic performance, alertness or to treat stress. (livestrong.com)
- Although you can take supplements of tyrosine, it is recommended to meet the needs of this amino acid through a balanced diet . (botanical-online.com)
- Long story short, I was reading in a natural therapy book about hypothyroidism and L-Tyrosine, B-complex, and Kelp were the top 3 recommended supplements to take. (healthboards.com)
- L-tyrosine is currently used as an ingredient in dietary supplements and health foods for its purported ability to relieve symptoms of stress, as well as in enteral nutritional products like medical foods. (nutraingredients.com)
- Amino acid supplements prefaced by the letter L, such as L-Tyrosine, are more similar to the amino acids in the body than those that start with the letter D, with the exception of D-L phenylalanine, which treats chronic pain. (herbalremedies.com)
- Tyrosine supplements should be taken at bedtime or with a high-carbohydrate meal so it does not compete for absorption with other amino acids. (herbalremedies.com)
- Often included in thermogenic or pre workout supplements to improve focus and mood, Tyrosine can play a major role in dealing with stress, intense training and sleep deprivation. (australiansportsnutrition.com.au)
- Try supplementing with L-Tyrosine throughout the day, simply in addition to your existing sports supplements or mixed with a glass of juice or water. (australiansportsnutrition.com.au)
- Protein tyrosine phosphatase-1B (PTP-1B) negatively regulates the signaling pathways of insulin and leptin, two hormones involved in the central regulation of energy balance ( 1 ). (diabetesjournals.org)
- In addition to activation of these pathways by tyrosine phosphorylation, several mechanisms of downregulating the response to insulin stimulation have also been identified. (diabetesjournals.org)
- The family of protein tyrosine phosphatases (PTPs) play critical roles in celluar signalling pathways and are recognised as potential drug targets in diabetes, cancer and cardiovascular disease. (soci.org)
- Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. (wikipedia.org)
- Structures of the three main molecules involved in chemical reaction catalyzed by the tyrosine aminotransferase enzyme are shown below: the amino acid tyrosine, the prosthetic group pyridoxal phosphate, and the resulting product 4-hydroxyphenylpyruvate. (wikipedia.org)
- Natural form of the amino acid " tyrosine " which leads to the production of norepinephrine , epinephrine ( adrenaline ), and thyroid hormone . (everything2.com)
- Scientists have been searching for it for decades: the enzyme that cuts the amino acid tyrosine off an important part of the cell's skeleton. (phys.org)
- The amino acid tyrosine is superior to synthetic T4/T3 combination in reducing TSH and improving mood in winter, whereas the T4/T3 combination worsens mood in the summer with no improvement in winter. (greenmedinfo.com)
- He and various colleagues then used PCR amplification and degenerate oligonucleotide probes that recognize the short sequence motifs to identify new tyrosine and serine kinase genes. (asbmb.org)
- Calculations reveal that the hydroxyl group of tyrosine is more suitable for the proton transfer than hydroxyl groups of other amino acids, such as serine and threonine. (nature.com)
- Although the role of tyrosine phosphorylation in this network is clear, only a limited number of insulin-induced tyrosine phosphorylation sites have been identified. (diabetesjournals.org)
- No studies to date have been done to determine the role of tyrosine in RLS. (clinicaltrials.gov)
- Low levels of tyrosine have been associated with low blood pressure, low body temperature, and an under active thyroid. (healthyplace.com)
- Because of this, people with PKU can have low levels of tyrosine in the body. (webmd.com)
- Good levels of tyrosine are required to help adapt to stress or anxiety or other problems such as headache because it also influences the synthesis of peptides like enkephalins. (botanical-online.com)
- Low plasma levels of Tyrosine have been linked with hypothyroidism. (herbalremedies.com)
- Human and animal research suggests that tyrosine acts as an adaptogen, helping the body adapt to and cope with the effects of physical or psychological stress by minimizing the symptoms brought on by stress. (healthyplace.com)
- Recent research suggests that tyrosine usage could help treat ED. (healthline.com)
- A double-blind, placebo-controlled study that enrolled 20 US Marines suggests that tyrosine can improve mental alertness during periods of sleep deprivation. (memorialhealth.com)
- Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate. (wikipedia.org)
- The Recommended Dietary Allowance (RDA) for phenylalanine and tyrosine is 33 mg per kilogram of body weight, or 15 mg per pound. (wikipedia.org)
- Conversion of phenylalanine and tyrosine to its biologically important derivatives. (wikipedia.org)
- Determination of Phenylalanine and Tyrosine by Liquid Chromatogra. (ingentaconnect.com)
- The body makes tyrosine from another amino acid called phenylalanine . (webmd.com)
- Phenylalanine, which in turn makes tyrosine, has been used successfully in combination with ultraviolet radiation therapy for darkening the whitened areas in those with vitiligo. (healthyplace.com)
- A deficiency of the enzyme in humans can result in what is known as Type II Tyrosinemia, wherein there is an abundance of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction to form 4-hydroxyphenylpyruvate. (wikipedia.org)
- The disease results from a deficiency in hepatic tyrosine aminotransferase. (wikipedia.org)
- Given that tyrosine is made from phenylalanine, restriction of this latter amino acid leads to deficiency of tyrosine. (healthyplace.com)
- Tyrosine deficiency is rare, according to the University of Maryland Medical Center. (livestrong.com)
- However, tyrosine plays a role in thyroid function, so tyrosine deficiency is linked to underactive thyroid. (livestrong.com)
- Tyrosine deficiency also can cause low blood pressure, low body temperature, and restless legs syndrome. (herbalremedies.com)
- A tyrosine deficiency therefore can contribute to fatigue, mood disorders, cognitive dysfunction, and pain disorders. (ei-resource.org)
- This is primarily due to the fact that tyrosine is a building block for norepinephine and epinephrine, the body's two main stress-related hormones. (healthyplace.com)
- In addition, because L-Tyrosine is necessary for the synthesis of thyroid hormone and epinephrine (adrenaline), L-Tyrosine supports healthy glandular function and stress response. (netrition.com)
- The thyroid hormones triiodothyronine (T3) and thyroxine (T4) in the colloid of the thyroid also are derived from tyrosine. (wikipedia.org)
- Can L-Tyrosine Restore Thyroid Function? (livestrong.com)
- Tyrosine influences other hormones such as thyroid , together with iodine, so it is beneficial in people with disorders of the thyroid gland, or alterations of estrogens, such as menopause . (botanical-online.com)
- Production of Thyroid Hormones - Tyrosine combines with iodine to form the thyroid hormones. (ei-resource.org)
- Protein tyrosine phosphatase-1B negatively regulates leptin and insulin signaling, potentially contributing to hormonal resistance. (diabetesjournals.org)
- Crystal structures of protein-tyrosine phosphatase 1B in complex with compounds bearing a novel isothiazolidinone (IZD) heterocyclic phosphonate mimetic reveal that the heterocycle is highly complementary to the catalytic pocket of the protein. (rcsb.org)
- By Hunter's recollection, he and his colleagues stumbled on tyrosine phosphorylation through their work on the polyoma DNA tumor virus. (asbmb.org)
- c-Src includes an SH2 domain, an SH3 domain, and a tyrosine kinase domain. (wikipedia.org)
- For example, the SRC-family kinase regulatory domain requires autophosphorylation for kinase domain activation, while most other intracellular tyrosine kinase families use different regulatory mechanisms. (qiagen.com)
- Tyrosine ammonia lyase (TAL) is an enzyme in the natural phenols biosynthesis pathway. (wikipedia.org)
- Plant biosynthesis of tyrosine from prephenate . (wikipedia.org)
- This book provides coverage, methodology, and laboratory protocols on the more essential aspects of protein tyrosine phosphatase (PTP) function and regulation, including the use of standardized in vitro functional assays, suitable cell systems, and animal and microorganism models. (springer.com)
- Studying tyrosine kinase expression and regulation in an experimental model system can yield new insights into their role in normal biological and pathophysiological processes. (qiagen.com)
- There is very limited evidence that the TPST genes are subject to transcriptional regulation and tyrosine O-sulfate is very stable and cannot be easily degraded by mammalian sulfatases. (bionity.com)
- Mechanistically, we found that direct phosphorylation of tyrosine 566 on NOX4 was critical for this FYN-mediated negative regulation. (jci.org)
- Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. (jci.org)
- Tyrosine also aids in the production of melanin (pigment responsible for hair and skin color) and in the function of organs in the body responsible for making and regulating hormones, including the adrenal, thryroid, and pituitary glands. (healthyplace.com)
- Given that tyrosine is involved in making melanin, it has been proposed that tyrosine may be a valuable aid in treating vitiligo. (healthyplace.com)
- Melanin is produced in melanosomes from tyrosine, and it is the substance responsible for the particular coloration of the skin, preventing its depigmentation. (botanical-online.com)
- Tyrosine is a component in the production of melanin, which is the pigment responsible for hair and skin color. (herbalremedies.com)
- Strategies for inducing dimerization by ligand binding are surprisingly diverse, as are mechanisms that couple this event to activation of the intracellular tyrosine kinase domains. (nih.gov)
- Dimerization of the extracellular regions of RTKs activates the intracellular tyrosine kinase domains (TKDs), which contain a C-lobe (light purple or yellow), N-lobe (dark purple or yellow in the inactive and active states), and an activation loop (dark purple or yellow in the inactive and active states, respectively). (nih.gov)
- Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and α-ketoglutarate. (wikipedia.org)
- This enzyme catalyzes the reaction causing the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine. (wikipedia.org)
- Therapies that target the TK enzymatic counterparts, the multi-enzyme family of protein tyrosine phosphatases (PTPs), are still lacking despite their undisputed involvement in human diseases. (mdpi.com)
- Learn about the usage, dosage, side-effects of Tyrosine. (healthyplace.com)
- The effects of tyrosine on cognitive performance during extended wakefulness. (memorialhealth.com)
- T-Cell Protein Tyrosine Phosphatase (TC PTP) is a phospho tyrosine-specific protein phosphatase. (neb.com)
- To meet their bodies' needs, supplemental tyrosine is given. (webmd.com)
- Supplemental Tyrosine can be used for reducing stress. (herbalremedies.com)
- Adding supplemental Tyrosine to the diet can also increase sex drive and eliminate headaches, and there is some evidence that suggests it can be helpful for those suffering from Parkinson s disease as well. (herbalremedies.com)
- Despite the fact that a protein kinase with this activity has not been described before, several observations suggest that pp60 src also phosphorylates tyrosine in vivo . (pnas.org)
- In a similar mechanism of aspartate transaminase, the lysine that forms the initial imine to PLP later acts as the base that attacks the tyrosine in transimination. (wikipedia.org)
- No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. (bionity.com)
- Together, our results identify tyrosine phosphorylation as an important regulatory mechanism for NLRP3 that prevents aberrant inflammasome activation. (jci.org)
- Tyrosine is essential to regulating mood, helping prevent depression and helping the body cope with the effects of physical or psychological stress. (healthyplace.com)
- Early research shows that taking a combination of tyrosine, 5-hydroxytryptophan (HTP), phosphatidylcholine, and L-glutamine, improves mood and the ability to sleep in men addicted to heroin. (webmd.com)
- Tyrosine: effects on catecholamine release. (springer.com)
- N-Acetyl Tyrosine is an acetylated derivative of the essential amino acid L-tyrosine. (patientslikeme.com)
- In the case of phenylketonuria, your health care provider will determine if you need a tyrosine-enriched diet and how much tyrosine is required. (healthyplace.com)
- However, for people with phenylketonuria tyrosine becomes an essential amino acid in the diet. (aminoz.com.au)
- According to UMMC, dosage guidelines may vary, but a common dosage for adults includes consuming 5 to 10 g of tyrosine three times per day. (livestrong.com)
- The typical therapeutic dosage of tyrosine used in studies ranges from 7 g to 30 g daily. (memorialhealth.com)
- Normally the level of cellular tyrosine kinase phosphorylation is tightly controlled by the antagonizing effect of tyrosine kinase and tyrosine phosphatases. (slideshare.net)
- Authoritative and practical, Protein Tyrosine Phosphatases: Methods and Protocols aims to aid researchers in better defining the common and individual features of the PTP family members and translating this knowledge into PTP-based therapy for human disease. (springer.com)
- By providing the raw material for the production of catecholamines, tyrosine may provide relief from stress and forms of depression where lack of motivation is prominent. (ei-resource.org)
- Humans often get tyrosine from foods high in protein. (healthline.com)
- Chapters covering state-of-the-art technical approaches suitable to decipher the physiologic roles of PTPs, and their involvement in tissue-specific functions, are also included, which will be of utility for both newcomers and experienced researchers in the field of tyrosine- and phosphoinositide- phosphorylation/dephosphorylation. (springer.com)
- The activation of c-Src causes the dephosphorylation of the tyrosine 527. (wikipedia.org)
- However, there simply aren't enough studies to conclusively prove that tyrosine is safe for everyone. (healthline.com)
