Tyrosine
Protein Tyrosine Phosphatases
Tyrosine 3-Monooxygenase
Phosphorylation
Phosphotyrosine
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
Receptor Protein-Tyrosine Kinases
Protein Tyrosine Phosphatase, Non-Receptor Type 6
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
Amino Acid Sequence
Lymphocyte 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.
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
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
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
Enzyme Inhibitors
Tyrosine Decarboxylase
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.
Tyrosine Phenol-Lyase
Tyrphostins
Cells, Cultured
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
SH2 Domain-Containing Protein Tyrosine Phosphatases
Focal Adhesion Protein-Tyrosine Kinases
Mutation
Transfection
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 enzymes
Pyrimidines
Receptor-Like Protein Tyrosine Phosphatases, Class 3
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.
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
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
Receptor-Like Protein Tyrosine Phosphatases, Class 4
fms-Like Tyrosine Kinase 3
Phenylalanine
Precipitin Tests
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
Benzoquinones
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
Binding Sites
Protein Tyrosine Phosphatases, Non-Receptor
Recombinant Fusion Proteins
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
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
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
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.
Isoflavones
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
Cell 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
Immunoblotting
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.
Substrate Specificity
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.
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
Membrane Proteins
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.
Sequence Homology, Amino Acid
Isoenzymes
Cell Adhesion Molecules
Protein Kinases
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
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
Cell Membrane
Cell Movement
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
Indoles
STAT3 Transcription Factor
Jurkat Cells
Mitogen-Activated Protein Kinase 1
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.
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
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
Structure-Activity Relationship
Dose-Response Relationship, Drug
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
Receptors, Antigen, B-Cell
Immunoprecipitation
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
Receptor, Platelet-Derived Growth Factor beta
Platelet-Derived Growth Factor
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
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
Electrophoresis, Polyacrylamide Gel
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
Amino Acids
Proto-Oncogene Proteins c-vav
Receptor Aggregation
Amino Acid Motifs
Gene Expression
Proto-Oncogene Proteins c-hck
DNA Primers
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
Mitogen-Activated Protein Kinase 3
Cricetinae
PC12 Cells
Models, Biological
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
Down-Regulation
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
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
STAT1 Transcription Factor
Rats, Sprague-Dawley
Cortactin
Fibroblasts
Point Mutation
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
Receptor, EphB2
DNA, Complementary
Cell Line, Transformed
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).
Oncogene Proteins
Dihydroxyphenylalanine
Receptors, Growth Factor
Gene Expression Regulation
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
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
Receptor-Like Protein Tyrosine Phosphatases, Class 7
Neurons
Nitriles
Nerve Growth Factors
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
Proto-Oncogene Proteins c-akt
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
Gene Expression Regulation, Enzymologic
Glutathione Transferase
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
Insulin phosphorylates tyrosine residue 464 of tub and translocates tubby into the nucleus in hircb cells<...
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...
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...
Cross-linking of ICAM-1 on T cells induces transient tyrosine phosphorylation and inactivation of cdc2 kinase. | The Journal of...
Receptor Tyrosine Protein Kinase ERBB 3 (Proto Oncogene Like Protein c ErbB 3 or Tyrosine Kinase Type Cell Surface Receptor...
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...
A new method for isolating tyrosine kinase substrates used to identify Fish, an SH3 and PX domain-containing protein, and Src...
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
Supplementary MaterialsSupplementary Document. phosphorylated at tyrosine 97 in the postischemic mind | The Critical Role of...
Phosphatidylinositol 3-kinase is a target for protein tyrosine nitration
IJMS | Free Full-Text | CCR7 Sulfotyrosine Enhances CCL21 Binding
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) |...
A conserved, N-terminal tyrosine signal directs Ras for inhibition by Rabex-5 - Ominy Science
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...
Ron is a heterodimeric tyrosine kinase receptor activated by the HGF homologue MSP<...
Anti-Nitrotyrosine Antibodies
Studies of Protein Metabolism in Man with Infusions of [14C]Tyrosine | Clinical Science | Portland Press
Plus it
The JAK‐binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop | The EMBO Journal
Receptor tyrosine kinases have an individual transmembrane (TM) section thats usually - Novel targets for Alzheimers disease...
Search Results | Journal of Cell Biology | Rockefeller University Press
Detecting Tyrosine-Phosphorylated Proteins by Western Blot Analysis - Current Protocols in Immunology - Sawasdikosol - Wiley...
Tyrosine Kinase JAK Inhibitors Market Analysis, Key Players, Industry Segments and Forecast to 2026 | Jul 9, 2018 - ReleaseWire
B for Biology: Signal Transduction Pathway - The JAK/STAT Pathways
Tyrosine Information
Receptor Tyrosine Protein Kinase ERBB 3 (Proto Oncogene Like Protein c ErbB 3 or Tyrosine Kinase Type Cell Surface Receptor...
Tyrosine Supplements | Tyrosine Products | Puritans Pride
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Sulfotyrosine Recognition as Marker for Druggable Sites in the Extracellular Space - topic of research paper in Biological...
Tyrosine sulfation
How Does Tyrosine Works | Mediologiest
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
A role for tyrosine phosphorylation in generation of inositol phosphates and prostacyclin production in endothelial cells
Hepatic tyrosine-phosphorylated proteins identified and localized following in vivo inhibition of protein tyrosine phosphatases...
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...
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 Reports
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Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism | The EMBO Journal
Identification and relative quantification of 3-nitrotyrosine residues in fibrinogen nitrated in vitro and fibrinogen from...
The tyrosine kinase activity of p56lck is increased in human T cells activated via CD2. - Immunology
Tyrosine 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
MLLT11/AF1q boosts oncogenic STAT3 activity through Src-PDGFR tyrosine kinase signaling - Semantic Scholar
Src, Autophosphorylation Site, Tyrosine Kinase Substrate substrate product blog
The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain. |...
The coordinated action of protein tyrosine phosphatases and kinases in cell signaling - CSHL Scientific Digital Repository
Thrombospondin-1 induces tyrosine phosphorylation of adherens junction proteins and regulates an endothelial paracellular...
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Impaired tyrosine phosphorylation of membrane type 1-matrix metalloproteinase reduces tumor cell proliferation in three...
Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor | Science
Leukocyte receptor tyrosine kinase - Wikipedia
Role 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 Torino
Cyclolignans as Inhibitors of the Insulin-Like Growth Factor-1 Receptor and Malignant Cell Growth | Cancer Research
MOLECULAR DOCKING AND ADMET STUDIES OF BIOACTIVE COMPOUNDS OF RHIZOPORA MUCORNATA AGAINST BACTERIAL ENZYME PROTEIN TYROSINE...
Tyrosine hydroxylase | Article about tyrosine hydroxylase by The Free Dictionary
ADHD treatments: Does Tyrosine for ADHD Actually Work as a Supplementation Strategy? (part 3)
Histone
Serine/threonine/tyrosine phosphorylation[edit]. Addition of a negatively charged phosphate group can lead to major changes in ...
Talk:Tubulin-tyrosine ligase
Retrieved from "https://en.wikipedia.org/w/index.php?title=Talk:Tubulin-tyrosine_ligase&oldid=420266952" ...
Philadelphia chromosome
Tyrosine kinase inhibitors[edit]. Crystal structure of Abl kinase domain (blue) in complex with 2nd generation tyrosine kinase ... The ABL tyrosine kinase activity of BCR-Abl is elevated relative to wild-type ABL.[11] Since ABL activates a number of cell ... Tyrosine kinase inhibitors specific to such domains as CC, Y177, and Rho (such as imatinib and sunitinib) are important drugs ... The activity of tyrosine kinases is typically regulated in an auto-inhibitory fashion, but the BCR-Abl fusion gene codes for a ...
Amino acid synthesis
Erythrose 4-phosphate and phosphoenolpyruvate: phenylalanine, tyrosine, and tryptophan[edit]. Phenylalanine, tyrosine, and ... Tyrosine can also be inhibited at the transcriptional level by the TyrR repressor. TyrR binds to the TyrR boxes on the operon ... In addition, the amino acids arginine, cysteine, glycine, glutamine, histidine, proline, serine, and tyrosine are considered ... Tyrosine is synthesized by the hydroxylation of phenylalanine, an essential amino acid. The pathways for the biosynthesis of ...
Chicken as food
Tyrosine. 0.796 g. Valine. 1.199 g. Arginine. 1.545 g. Histidine. 0.726 g. ...
Hickory
Tyrosine. 0.454 g. Valine. 0.730 g. Arginine. 2.086 g. Histidine. 0.389 g. ...
Almond
Tyrosine. 0.452 g. Valine. 0.817 g. Arginine. 2.446 g. Histidine. 0.557 g. ...
Canarium ovatum
Tyrosine. 0.381 g. Valine. 0.701 g. Arginine. 1.516 g. Histidine. 0.255 g. ...
Hemp
Tyrosine. 1.263 g. Valine. 1.777 g. Arginine. 4.550 g. Histidine. 0.969 g. ...
Protein quality
Tyrosine*. 5.369 g. 2.267 g 3.745 g. 3.409 g. 3.677 g. 2.658 g. 3.675 g. 4.496 g. 2.8 g. 2.500 g. N/A. 4.193 g ...
Egg as food
Tyrosine. 0.513 g. Valine. 0.767 g. Arginine. 0.755 g. Histidine. 0.298 g. ...
Spirulina (dietary supplement)
Tyrosine. 2.584 g. Valine. 3.512 g. Arginine. 4.147 g. Histidine. 1.085 g. ...
Naturally occurring phenols
Acetophenones, Tyrosine derivatives, Phenylacetic acids 3-Acetyl-6-methoxybenzaldehyde, Tyrosol, p-Hydroxyphenylacetic acid, ...
Castanea sativa
Tyrosine. 0.067 g. Valine. 0.135 g. Arginine. 0.173 g. Histidine. 0.067 g. ...
Yolk
Tyrosine. 0.678 g. Valine. 0.949 g. Arginine. 1.099 g. Histidine. 0.416 g. ...
Coconut
Tyrosine. 0.103 g. Valine. 0.202 g. Arginine. 0.546 g. Histidine. 0.077 g. ...
Amaranth
Tyrosine. 0.329 g. Valine. 0.679 g. Arginine. 1.060 g. Histidine. 0.389 g. ...
Human mitochondrial genetics
Tyrosine Tyr Y MT-TY 5,826-5,891 H Valine Val V MT-TV 1,602-1,670 L ...
Competitive inhibition
In competitive inhibition, an inhibitor that resembles the normal substrate binds to the enzyme, usually at the active site, and prevents the substrate from binding.[8] At any given moment, the enzyme may be bound to the inhibitor, the substrate, or neither, but it cannot bind both at the same time. During competitive inhibition, the inhibitor and substrate compete for the active site. The active site is a region on an enzyme which a particular protein or substrate can bind to. The active site will only allow one of the two complexes to bind to the site therefore either allowing for a reaction to occur or yielding it. In competitive inhibition the inhibitor resembles the substrate therefore taking its place and binding to the active site of an enzyme. Increasing the substrate concentration would diminish the "competition" for the substrate to properly bind to the active site and allow a reaction to occur.[3] When the substrate is of higher concentration than that of the competitive inhibitor, it ...
D-Amino acid
Two enzymes convert L-amino acids to D-amino acids. D-Amino-acid racemase, a PLP-dependent enzyme, racemizes amino acids via the formation of the alpha-iminoacids, where the stereogenic center is lost. L-amino-acid oxidases convert L-amino acids to the alpha-ketoacids, which are susceptible to reductive amination. Some amino acids are prone to racemization, one example being lysine, which racemizes via formation pipecolic acid. In peptides, L-amino acid residues slowly racemize, resulting in the formation of some D-amino acid residues. Racemization occurs via deprotonation of the methyne that is alpha to the amido group. Rates increase with pH. Many D-amino acids found in higher organisms are derived from microbial sources. The D-alanine in peptidoglycans that comprise bacterial cell walls helps its host resist attack by proteolytic enzymes. Several antibiotics, e.g. bacitracin, contain D-amino acid residues.[1] ...
Cysteine
Their hydrophobic tendency was equivalent to that of known nonpolar amino acids such as methionine and tyrosine (tyrosine is ...
COX-2 inhibitor
The COX-2 enzyme was discovered in 1988 by Daniel Simmons, a Brigham Young University researcher.[23] The mouse COX-2 gene was cloned by UCLA scientist Dr. Harvey Herschman, a finding published in 1991.[24]. The basic research leading to the discovery of COX-2 inhibitors has been the subject of at least two lawsuits. Brigham Young University has sued Pfizer, alleging breach of contract from relations BYU had with the company at the time of Dr. Simmons's work.[25][26] A settlement was reached in April 2012 in which Pfizer agreed to pay $450 million.[27][28] The other litigation is based on United States Pat. No. 6,048,850[29] owned by University of Rochester, which claimed a method to treat pain without causing gastro-intestinal distress by selectively inhibiting COX-2. When the patent issued, the university sued Searle (later Pfizer) in a case called, University of Rochester v. G.D. Searle & Co., 358 F.3d 916 (Fed. Cir. 2004). The court ruled in favor of Searle in 2004, holding in essence that ...
Glycine
... (symbol Gly or G;[5] /ˈɡlaɪsiːn/)[6] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest amino acid (since carbamic acid is unstable), with the chemical formula NH2‐CH2‐COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is the most abundant amino acid in collagen triple-helices. Glycine is also an inhibitory neurotransmitter - interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction. Glycine is a colorless, sweet-tasting crystalline solid. It is the only achiral proteinogenic amino acid. It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. The acyl radical is glycyl. ...
5α-Reductase inhibitor
A 2017 population-based, matched-cohort study of 93,197 men aged 66 years and older with BPH found that finasteride and dutasteride were associated with a significantly increased risk of depression (HR, 1.94; 95% CI, 1.73-2.16) and self-harm (HR, 1.88; 95% CI, 1.34-2.64) during the first 18 months of treatment, but were not associated with an increased risk of suicide (HR, 0.88; 95% CI, 0.53-1.45).[31][32][33][21] After the initial 18 months of therapy, the risk of self-harm was no longer heightened, whereas the elevation in risk of depression lessened but remained marginally increased (HR, 1.22; 95% CI, 1.08-1.37).[31][32][21] The absolute increase in the rate of depression was 247 per 100,000 patient-years and of self-harm was 17 per 100,000 patient-years.[21][34] As such, on the basis of these findings, it has been stated that cases of depression in patients that are attributable to 5-ARIs will be encountered on occasion, while cases of self-harm attributable to 5-ARIs will be encountered ...
Ribonuclease inhibitor
valine, isoleucine, methionine, tyrosine, and phenylalanine. Contents. *1 Structure. *2 Binding to ribonucleases ...
5α-Reductase inhibitor
Beyond being a catalyst in the rate-limiting step in testosterone reduction, 5α-reductase isoforms I and II reduce progesterone to 5α-dihydroprogesterone (5α-DHP) and deoxycorticosterone to dihydrodeoxycorticosterone (DHDOC). In vitro and animal models suggest subsequent 3α-reduction of DHT, 5α-DHP and DHDOC lead to neurosteroid metabolites with effect on cerebral function. These neurosteroids, which include allopregnanolone, tetrahydrodeoxycorticosterone (THDOC), and 3α-androstanediol, act as potent positive allosteric modulators of GABAA receptors, and have antidepressant, anxiolytic, prosexual, and anticonvulsant effects.[33] 5α-Dihydrocortisol is present in the aqueous humor of the eye, is synthesized in the lens, and might help make the aqueous humor itself.[34] 5α-Dihydroaldosterone is a potent antinatriuretic agent, although different from aldosterone. Its formation in the kidney is enhanced by restriction of dietary salt, suggesting it may help retain sodium.[35] 5α-DHP is a ...
Histidine
When both imidazole ring nitrogens are protonated, their 15N chemical shifts are similar (about 200 ppm, relative to nitric acid on the sigma scale, on which increased shielding corresponds to increased chemical shift). NMR shows that the chemical shift of N1-H drops slightly, whereas the chemical shift of N3-H drops considerably (about 190 vs. 145 ppm). This indicates that the N1-H tautomer is preferred, it is presumed due to hydrogen bonding to the neighboring ammonium. The shielding at N3 is substantially reduced due to the second-order paramagnetic effect, which involves a symmetry-allowed interaction between the nitrogen lone pair and the excited π* states of the aromatic ring. As the pH rises above 9, the chemical shifts of N1 and N3 become approximately 185 and 170 ppm. An entirely deprotonated form of the imidazole ring, the imidazolate ion, would be formed only above a pH of 14, and is therefore not physiologically relevant. This change in chemical shifts can be explained by the ...
Amino acid neurotransmitter
An amino acid neurotransmitter is an amino acid which is able to transmit a nerve message across a synapse. Neurotransmitters (chemicals) are packaged into vesicles that cluster beneath the axon terminal membrane on the presynaptic side of a synapse in a process called endocytosis.[1]. Amino acid neurotransmitter release (exocytosis) is dependent upon calcium Ca2+ and is a presynaptic response. There are inhibitory amino acids (IAA) or excitatory amino acids (EAA). Some EAA are L-Glutamate, L-Aspartate, L-Cysteine, and L-Homocysteine.[2] These neurotransmitter systems will activate post-synaptic cells.[3] Some IAA include GABA, Glycine, β-Alanine, and Taurine.[2] The IAA depress the activity of post-synaptic cells.[3]. ...
Branched-chain amino acid
While most amino acids are oxidized in the liver, BCAAs are primarily oxidized in the skeletal muscle and other peripheral tissues.[4] The effects of BCAA administration on muscle growth in rat diaphragm was tested, and concluded that not only does a mixture of BCAAs alone have the same effect on growth as a complete mixture of amino acids, but an amino acid mixture with all but BCAAs has no effect on rat diaphragm muscle growth.[16] Administration of either isoleucine or valine alone had no effect on muscle growth, although administration of leucine alone appears to be nearly as effective as the complete mixture of BCAAs. Leucine indirectly activates p70 S6 kinase as well as stimulates assembly of the eIF4F complex, which are essential for mRNA binding in translational initiation.[16] P70 S6 kinase is part of the mammalian target of rapamycin complex (mTOR) signaling pathway, and has been shown to allow adaptive hypertrophy and recovery of rat muscle.[17] At rest protein infusion stimulates ...
Statin
The role of cholesterol in the development of cardiovascular disease was elucidated in the second half of the 20th century.[138] This lipid hypothesis prompted attempts to reduce cardiovascular disease burden by lowering cholesterol. Treatment consisted mainly of dietary measures, such as a low-fat diet, and poorly tolerated medicines, such as clofibrate, cholestyramine, and nicotinic acid. Cholesterol researcher Daniel Steinberg writes that while the Coronary Primary Prevention Trial of 1984 demonstrated cholesterol lowering could significantly reduce the risk of heart attacks and angina, physicians, including cardiologists, remained largely unconvinced.[139] Scientists in academic settings and the pharmaceutical industry began trying to develop a drug to reduce cholesterol more effectively. There were several potential targets, with 30 steps in the synthesis of cholesterol from acetyl-coenzyme A.[140] In 1971, Akira Endo, a Japanese biochemist working for the pharmaceutical company Sankyo, ...
Tyrosine hydroxylase - Wikipedia
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L- ... Tyrosine hydroxylase catalyzes the reaction in which L-tyrosine is hydroxylated in the meta position to obtain L-3,4- ... Tyrosine hydroxylase can be inhibited by the drug α-methyl-para-tyrosine (metirosine). This inhibition can lead to a depletion ... Tyrosine hydroxylase catalyzes conversion of tyrosine to L-DOPA using Fe2+, O2 and BH4 ...
Bruton's tyrosine kinase - Wikipedia
Brutons tyrosine kinase (abbreviated Btk or BTK), also known as tyrosine-protein kinase BTK, is an enzyme that in humans is ... non-membrane spanning protein tyrosine kinase activity. • ATP binding. • protein binding. • protein tyrosine kinase activity. ... Brutons tyrosine kinase was discovered in 1993 and is named for Ogden Bruton, who first described XLA in 1952.[5] ... peptidyl-tyrosine autophosphorylation. • B cell activation. • positive regulation of NF-kappaB transcription factor activity. • ...
Tyrosine - MeSH - NCBI
L Tyrosine. All MeSH CategoriesChemicals and Drugs CategoryAmino Acids, Peptides, and ProteinsAmino AcidsAmino Acids, Cyclic ... Tyrosine. A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE ... Amino Acids, AromaticTyrosineBetalainsBetacyaninsDihydroxyphenylalanineCysteinyldopaLevodopaMethyldopaDiiodotyrosineMelanins ...
TYROSINE KINASE INHIBITORS
... PRESENTED BY: Y.VIJAY FINAL YEAR POST GRADUATEDEPARTMENT OF PHARMACOLOGY OSMANIA MEDICAL COLLEGE ... 5. TYPES OF TYROSINE KINASES• Tyrosine kinases can be further subdivided into1. Receptor tyrosine kinases eg: EGFR, PDGFR, ... TYROSINE KINASE INHIBITORS * 1. TYROSINE KINASE INHIBITORS PRESENTED BY: Y.VIJAY FINAL YEAR POST GRADUATEDEPARTMENT OF ... 9. TYROSINE KINASE INIBITORS1. BCR-ABL Tyrosine Kinase Inhibitors eg: Imatinib Mesylate, Dasatinib, and Nilotinib.2. Epidermal ...
L-tyrosine (CHEBI:17895)
... is enantiomer of D-tyrosine (CHEBI:28479) L-tyrosine (CHEBI:17895) is tautomer of L-tyrosine ... L-tyrosine (CHEBI:17895). L-tyrosin-O4-yl group (CHEBI:32768) is substituent group from L-tyrosine (CHEBI:17895). L-tyrosine ... L-tyrosine (CHEBI:17895) is a proteinogenic amino acid (CHEBI:83813) L-tyrosine (CHEBI:17895) is a tyrosine (CHEBI:18186) L- ... L-tyrosine (CHEBI:17895) has role nutraceutical (CHEBI:50733) L-tyrosine (CHEBI:17895) is a L-α-amino acid (CHEBI:15705) L- ...
Tyrosine hydroxylase deficiency: MedlinePlus Genetics
Tyrosine hydroxylase (TH) deficiency is a disorder that primarily affects movement, with symptoms that may range from mild to ... Tyrosine hydroxylase helps convert the protein building block (amino acid) tyrosine to a catecholamine called dopamine. . ... Tyrosine hydroxylase (TH) deficiency is a disorder that primarily affects movement, with symptoms that may range from mild to ... Mutations in the TH gene result in reduced activity of the tyrosine hydroxylase enzyme. As a result, the body produces less ...
Oncogenic protein tyrosine kinases | SpringerLink
tyrosine kinase inhibitor (CHEBI:38637)
1-NA-PP1 (CHEBI:52310) has role tyrosine kinase inhibitor (CHEBI:38637). 1-NM-PP1 (CHEBI:52309) has role tyrosine kinase ... BE-23372M (CHEBI:65473) has role tyrosine kinase inhibitor (CHEBI:38637). biochanin A (CHEBI:17574) has role tyrosine kinase ... bosutinib hydrate (CHEBI:68533) has role tyrosine kinase inhibitor (CHEBI:38637). butein (CHEBI:3237) has role tyrosine kinase ... masitinib (CHEBI:63450) has role tyrosine kinase inhibitor (CHEBI:38637). melemeleone B (CHEBI:66690) has role tyrosine kinase ...
Tyrosine - Healthy.net
Tyrosine is easily made in the body from phenylalanine and is very important to general metabolism, as it is a direct precursor ... of L-tyrosine can be taken two or three times during the day. Since tyrosine has a more stimulating antidepressant effect, ... L-tyrosine has also been used, usually in a dose of 1-2 grams a day, for low sex drive, Parkinsons disease, and in programs ... Tyrosine is easily made in the body from phenylalanine and is very important to general metabolism, as it is a direct precursor ...
L-Tyrosine - Everything2.com
... tyrosine which leads to the production of norepinephrine, epinephrine (adrenaline), and thyroid hormone. The ... ... Tyrosine. Saint Johns wort. A medical explanation of the effects of ecstasy on your body. Sleep cycle strategies. ... The human body also uses l-tyrosine to make serotonin and dopamine, two important neurotransmitters. Some reported effects of ... Natural form of the amino acid "tyrosine" which leads to the production of norepinephrine, epinephrine (adrenaline), and ...
Tyrosine | HealthyPlace
Learn about the usage, dosage, side-effects of Tyrosine. ... Tyrosine is essential to regulating mood, helping prevent ... Tyrosine for Stress. Human and animal research suggests that tyrosine acts as an adaptogen, helping the body adapt to and cope ... Given that tyrosine is involved in making melanin, it has been proposed that tyrosine may be a valuable aid in treating ... How to Take Tyrosine. Tyrosine supplements should be taken at least 30 minutes before meals, divided into three daily doses. ...
TYROSINE DETERMINATION | Science
L-Tyrosine - iHerb
Tyrosine Hydroxylase | ALZFORUM
L-Tyrosine - iHerb
Food for creativity: tyrosine promotes deep thinking | SpringerLink
Elevation of plasma tyrosine after a single oral dose of l-tyrosine. Life Sciences, 25, 265-271. doi: 10.1016/0024-3205(79) ... Deijen, J. B. (2005). Tyrosine. In: Lieberman, Kanarek & Prasad, Nutrition brain and behavior (pp. 363-381).Google Scholar ... 2007). Tyrosine supplementation mitigates memory decrements during cold exposure. Physiology and Behavior, 92(4), 575-582. ... During, M. J., Acworth, I. N., & Wurtman, R. J. (1988). Effects of systemic l-tyrosine on dopamine release from rat corpus ...
Cell signaling by receptor tyrosine kinases. - PubMed - NCBI
Cell signaling by receptor tyrosine kinases.. Lemmon MA1, Schlessinger J.. Author information. 1. Department of Biochemistry ... RTK-mediated tyrosine phosphorylation of PLCγ leads to intramolecular binding of the C-terminal SH2 domain to phosphotyrosine ... On the other hand, H2O2 inhibits protein tyrosine phosphatases (PTPs) and thus, prolongs or increases activity of EGFR by a ... Human receptor tyrosine kinases (RTKs) contain 20 subfamilies, shown here schematically with the family members listed beneath ...
Patent US7585866 - Protein tyrosine kinase inhibitors - Google Patents
... and methods of using them to treat tyrosine kinase-dependent diseases and conditions in mammals: wherein n is an integer, ... regulate and/or modulate tyrosine kinase signal transduction, compositions which contain these compounds, ... Tyrosine kinases can be categorized as receptor type or non-receptor type. Receptor type tyrosine kinases have an extracellular ... For example, the Bcr-Abl tyrosine kinase is the constitutive abnormal tyrosine kinase created by the Philadelphia chromosome ...
Tyrosine: Uses, Side Effects, Interactions, Dosage, and Warning
Learn more about Tyrosine uses, effectiveness, possible side effects, interactions, dosage, user ratings and products that ... Acétyl-L-Tyrosine, L-Tyrosine, N-Acetyl L-Tyrosine, N-Acetyl-L-Tyrosine, N-Acétyl L-Tyrosine, N-Acetyl-Tyrosine, N-Acétyl- ... As a result they cant make tyrosine. To meet their bodies needs, supplemental tyrosine is given.. Tyrosine is also commonly ... Tyrosine can also be found in dairy products, meats, fish, eggs, nuts, beans, oats, and wheat.. Tyrosine is most commonly used ...
A legacy of tyrosine
Tyrosine and tumors. By Hunters recollection, he and his colleagues stumbled on tyrosine phosphorylation through their work on ... was also a tyrosine kinase. This led Hunter to generate sequence alignments of the viral tyrosine kinase proteins, as well as ... A legacy of tyrosine. Tony Hunter, the Salk Institute biochemist who discovered this amino acids phosphorylation, was ... Today, 40 tyrosine kinase inhibitors have been approved by the Food and Drug Administration as cancer therapies. ...
Template:Tyrosine kinases - Wikipedia
Tyrosine kinases,state=autocollapse}}. *shows the template collapsed to the title bar if there is a {{navbar}}. , a {{sidebar}} ... Tyrosine kinases,state=collapsed}}. to show the template collapsed, i.e., hidden apart from its title bar ... Tyrosine kinases,state=expanded}}. to show the template expanded, i.e., fully visible ... Retrieved from "https://en.wikipedia.org/w/index.php?title=Template:Tyrosine_kinases&oldid=737502993" ...
Tyrosine - Wikipedia
Tyrosine residues may also be modified by the addition of a sulfate group, a process known as tyrosine sulfation.[7] Tyrosine ... namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2- ... It transforms L-tyrosine into p-coumaric acid. Precursor to pigmentsEdit. Tyrosine is also the precursor to the pigment melanin ... Ortho- and meta-tyrosineEdit. Enzymatic oxidation of tyrosine by phenylalanine hydroxylase (top) and non-enyzmatic oxidation by ...
Tyrosine | IntechOpen
p, 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 ... in 1960s and thereafter has uncovered an involvement of tyrosine phosphorylation and dephosphorylation as a key feature in on- ... This book will cover several aspects of biological as well as physicochemical features of tyrosine in all related scientific ...
Protein Tyrosine Phosphatases - Methods and Protocols | Rafael Pulido | Springer
... and laboratory protocols on the more essential aspects of protein tyrosine phosphatase (PTP) function and regulation, including ... Protein Tyrosine Phosphatases. Book Subtitle. Methods and Protocols. Editors. * Rafael Pulido Series Title. Methods in ... Authoritative and practical, Protein Tyrosine Phosphatases: Methods and Protocols aims to aid researchers in better defining ... Tailor-Made Protein Tyrosine Phosphatases: In Vitro Site-Directed Mutagenesis of PTEN and PTPRZ-B ...
tyrosine - Symptoms, Treatments and Resources for tyrosine
Treatments and Tools for tyrosine. Find tyrosine information, treatments for tyrosine and tyrosine symptoms. ... tyrosine - MedHelps tyrosine Center for Information, Symptoms, Resources, ... I was taking l-tyrosine and 5-htp for some anxiety issues i have.It was working great but t... ... L-Tyrosine and the Thomas Recipe, how much - Addiction: Substance Abuse Community ...
Tyrosine Side Effects in Detail - Drugs.com
Learn about the potential side effects of tyrosine. Includes common and rare side effects information for consumers and ... Applies to tyrosine: oral capsule, oral powder. Get emergency medical help if you have signs of an allergic reaction: hives; ... Although not all side effects are known, tyrosine is thought to be likely safe in most adults when taken for up to 3 months. ...
DailyMed - APPFORMIN - metformin hydrochloride, tyrosine
APPFORMIN - metformin hydrochloride, tyrosine To receive this label RSS feed. Copy the URL below and paste it into your RSS ... In addition, tyrosine deficiencies have been reported in the medical literature in obese and morbidly obese patients. Thus, ... Products containing L-tyrosine are contraindicated in those with the inborn errors of metabolism alkaptonuria and tyrosinemia ... Products containing tyrosine are also contraindicated in patients taking non-selective monoamine oxidase (MAO) inhibitors. ...
Electrochemically clicking on tyrosine | Science
A reactive N=N species generated in the five-membered ring reacts with the C-H bonds adjacent to the tyrosine OH group. ... Alvarez-Dorta et al. show that tyrosine residues on proteins, including insulin and bovine serum albumin, can be targeted by ... For example, for electron-rich tyrosine, click methods have been developed based on cyclic diazodicarboxyamide anchors, but ...
Tyrosine Kinases - QIAGEN
Tyrosine Kinases RT2 Profiler PCR Array The Rat Tyrosine Kinases RT2 Profiler PCR Array profiles the expression of 84 receptor ... Tyrosine Kinases RT2 Profiler PCR Array The Human Tyrosine Kinases RT2 Profiler PCR Array profiles the expression of 84 ... Tyrosine Kinases RT2 Profiler PCR Array The Mouse Tyrosine Kinases RT2 Profiler PCR Array profiles the expression of 84 ... Receptor Tyrosine Kinase (Panel II) qBiomarker Somatic Mutation PCR Array The Human Receptor Tyrosine Kinase (RTK) Pathways ...
Transforming gene product of Rous sarcoma virus phosphorylates tyrosine | PNAS
We have found that viral pp60src and the endogenous pp60sarc of birds and of mammals catalyze the phosphorylation of a tyrosine ... It has been shown recently that a tyrosine in both the 60,000-dalton tumor antigen of polyoma virus (20) and p120 of Abelson ... We favor the idea that the phosphorylation of tyrosine carried out by pp60src is an end-state protein modification that is ... Phosphorylated tyrosines are rare in uninfected cells and significantly more abundant in cells transformed by RSV. It is ...
KinasesReceptorResiduesProteinsHydroxylaseInhibitorsResidueDopamineSignal transductionPATHWAYSAcetyl-L-TyrosineNeurotransmittersPrecursorGeneAmino acid tyrosineSupplementsRole of tyrosineLevels of tyrosineSuggests that tyrosineConversion of tyrosineBody makes tyrosine from anotherMakes tyrosineSerineDeficiencyThyroidSulfationProtein tyrosine phospStumbled on tyrosine phosphorylationMelaninRegulationKinase domainPhosphatasesIntracellular tyrosine kinaseEpinephrineHydroxyl groupEnzymeEffects of tyrosinePhenylalanine and tyrosineMoleculeBiosynthesisCapsulePhospho-tyrosineSupplemental tyrosinePhosphorylate tyrosineAdrenalPhosphorylatesMechanismCatecholaminePTPsSubstancesDerivativeCatecholaminesHumansDephosphorylation
Kinases44
- Kinases that specifically phosphorylate tyrosine residues2. (slideshare.net)
- Tyrosine kinases can be further subdivided into1. (slideshare.net)
- Receptor tyrosine kinases eg: EGFR, PDGFR, FGFR2. (slideshare.net)
- The molecular basis of phospho-tyrosyl-regulation of Src-family and Syk-family protein tyrosine kinases in signaling pathways is a current focus of the lab. (purdue.edu)
- Cell signaling by receptor tyrosine kinases. (nih.gov)
- Recent structural studies of receptor tyrosine kinases (RTKs) have revealed unexpected diversity in the mechanisms of their activation by growth factor ligands. (nih.gov)
- Human receptor tyrosine kinases (RTKs) contain 20 subfamilies, shown here schematically with the family members listed beneath each receptor. (nih.gov)
- Top: In general, receptor tyrosine kinases (RTKs) associate into dimers when ligand (red) binds to their extracellular regions. (nih.gov)
- His discovery that the activity of tyrosine kinases drives the growth of cancerous cells ultimately led to the development of tyrosine kinase inhibitors and the groundbreaking leukemia therapy Gleevec, as well as an entire subfield of biochemical regulation. (asbmb.org)
- According to Hunter, this provided an immediate hint that cells might also have tyrosine kinases. (asbmb.org)
- This led Hunter to generate sequence alignments of the viral tyrosine kinase proteins, as well as protein kinases that phosphorylate serine and threonine, which revealed that the catalytic domain of tyrosine kinase has a series of conserved short sequence motifs that are essential for transferring phosphate. (asbmb.org)
- When those genes were combined with analysis of the human genome sequence, the researchers ultimately wound up discovering nearly 500 human kinases, about 90 of which are tyrosine kinases. (asbmb.org)
- Some of the tyrosine residues can be tagged (at the hydroxyl group) with a phosphate group ( phosphorylated ) by protein kinases . (wikipedia.org)
- His research interest is the role played by protein-tyrosine kinases in transmembrane signal transduction mechanisms such as in the cancer cells and the fertilized eggs. (intechopen.com)
- The protein tyrosine kinase superfamily includes roughly 60 receptor tyrosine kinases (RTKs) and about 30 intracellular tyrosine kinases. (qiagen.com)
- Upon activation, RTKs dimerize and autophosphorylate their intracellular domains, initiating downstream signaling that often includes non-receptor tyrosine kinases. (qiagen.com)
- Non-receptor tyrosine kinases include a catalytic domain and a regulatory domain, which vary for each family. (qiagen.com)
- Tyrosine kinases and their downstream signaling pathways are involved in many basic biological processes, such as growth, proliferation, and differentiation. (qiagen.com)
- These processes are commonly dysregulated during oncogenesis, often due to frequent mutations of key tyrosine kinases or regulators. (qiagen.com)
- These oncogenic processes make the tyrosine kinase superfamily members attractive drug targets, and there are several chemotherapeutics targeting tyrosine kinases already on the market (e.g., imatinib mesylate). (qiagen.com)
- The Human Tyrosine Kinases RT 2 Profiler PCR Array profiles the expression of 84 receptor and non-receptor tyrosine kinase genes. (qiagen.com)
- The recognition motif for phosphorylation by Abl is I/V/L Y XXP/F. Abl, like many cytosolic protein tyrosine kinases, preferentially phosphorylates sites recognized by its own SH2 domain, selects substrates with large hydrophobic amino acids at the +3 position and β-branched amino acids at the -1 position (4). (neb.com)
- It is now clear that tyrosine kinases represent attractive targets for therapeutic intervention in cancer. (pnas.org)
- Recent successful development of targeted intervention agents has been based on the use of small molecules and antibodies directed to disregulated tyrosine kinases ( 2 , 3 ). (pnas.org)
- Tyrosine kinases are a subgroup of the larger class of protein kinases . (bionity.com)
- There are over 100 3D structures of tyrosine kinases available at the Protein Data Bank . (bionity.com)
- Most tyrosine kinases have an associated protein tyrosine phosphatase. (bionity.com)
- Approximately 2000 kinases are known and more than 90 Protein Tyrosine Kinases (PTKs) have been found in the human genome. (bionity.com)
- At present, 58 receptor tyrosine kinases (RTKs) are known, grouped into 20 subfamilies. (bionity.com)
- In humans, there are 32 cytoplasmic protein tyrosine kinases ( EC 2.7.10.2). (bionity.com)
- Most animal cells contain one or more members of the Src family of tyrosine kinases. (bionity.com)
- A mutation that causes certain tyrosine kinases to be constitutively active has been associated with several cancers. (bionity.com)
- Imatinib (brand names Gleevec and Glivec) is a drug able to bind the catalytic cleft of these tyrosine kinases, inhibiting its activity. (bionity.com)
- The development of the so-called "targeted therapies", particularly those drugs that inhibit the activity of tyrosine kinases, has become a remarkable progress in the treatment of neoplastic diseases. (rti.org)
- Here we summarize what is known up to date about the cardiotoxicity of drugs targeting the tyrosine kinases. (rti.org)
- Therefore, tyrosine phosphorylation-dependent signaling involving receptor tyrosine kinases, mitogen-activated protein kinases, Abl, Src, and Pyk2 is known to be initiated or amplified by reactive oxidants. (sciencemag.org)
- Receptor tyrosine kinases are a large family of cell-surface receptors that respond to a variety of intercellular signals, including insulin, growth factors such as epidermal growth factor (EGF) and fibroblast growth factor (FGF), and molecules involved in neuronal guidance. (cshlpress.com)
- Written and edited by experts in the field, Signaling by Receptor Tyrosine Kinases from Cold Spring Harbor Perspectives in Biology discusses the mechanisms underlying receptor tyrosine kinase signaling, including ligand processing, receptor dimerization, receptor trafficking, and the roles of adapters. (cshlpress.com)
- However, development of therapeutics targeting the family of protein tyrosine phosphatases has lagged far behind that of kinases. (soci.org)
- Attempts to normalize aberrant tyrosine phosphorylation levels in disease states currently involve either the application of small compounds that inhibit tyrosine kinases (TKs) or the addition of growth factors or their mimetics to boost receptor-type TK activity. (mdpi.com)
- Tyrosine kinases are enzymes capable of phosphorylating tyrosine residues within proteins. (novusbio.com)
- c-Src phosphorylates specific tyrosine residues in other tyrosine kinases. (wikipedia.org)
- c-Src can be activated by many transmembrane proteins that include: adhesion receptors, receptor tyrosine kinases, G-protein coupled receptors and cytokine receptors. (wikipedia.org)
- Most studies have looked at the receptor tyrosine kinases and examples of these are platelet derived growth factor receptor (PDGFR) pathway and epidermal growth factor receptor (EGFR). (wikipedia.org)
Receptor22
- 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)
- 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)
- pronounced "sarc", as it is short for sarcoma), is a non-receptor tyrosine kinase protein that in humans is encoded by the SRC gene. (wikipedia.org)
Residues9
- Tyrosine residues may also be modified by the addition of a sulfate group, a process known as tyrosine sulfation . (wikipedia.org)
- For example, for electron-rich tyrosine, click methods have been developed based on cyclic diazodicarboxyamide anchors, but activation with chemical oxidants can also modify lysine residues or create products with limited aqueous stability. (sciencemag.org)
- show that tyrosine residues on proteins, including insulin and bovine serum albumin, can be targeted by electrochemically oxidizing phenyl urazoles without affecting amine or thiol groups of other amino acids. (sciencemag.org)
- Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. (uniprot.org)
- 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)[1]. (bionity.com)
- A major mechanism of injury associated with the production of nitric oxide (NO*) in vivo is due to its diffusion-limited reaction with superoxide to form peroxynitrite, which in turn may cause nitration of protein tyrosine residues. (nih.gov)
- It is a truncated form of the human T-Cell protein tyrosine phosphatase (residues 1-317) which lacks a C-terminal regulatory domain (1,2). (neb.com)
- Protein phosphatase exclusively specific to phospho-tyrosine residues in proteins. (neb.com)
- TC PTP can be used to release phosphate groups specifically from phospho-tyrosine residues in proteins. (neb.com)
Proteins14
- We are also actively investigating the regulation of Syk tyrosine kinase binding to membrane immune receptors and other signaling proteins. (purdue.edu)
- Tyrosine (symbol Tyr or Y ) [1] 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)
Hydroxylase25
- 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 , [6] and the enzyme is present in the central nervous system (CNS), peripheral sympathetic neurons and the adrenal medulla . (wikipedia.org)
- [6] 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)
- [8] Each of the four subunits in tyrosine hydroxylase is coordinated with an iron (II) atom presented in the active site. (wikipedia.org)
- [11] 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)
- 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)
- In dopaminergic cells in the brain, tyrosine is converted to L-DOPA by the enzyme tyrosine hydroxylase (TH). (wikipedia.org)
- 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)
Inhibitors11
- 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)
- What is the role of tyrosine kinase inhibitors in the etiology of macrocytosis? (medscape.com)
- The tyrosine kinase inhibitors sunitinib and imatinib have been shown to induce macrocytosis in patients with a variety of cancers, including renal cell carcinomas (RCCs), gastrointestinal stromal tumors (GISTs), and breast cancer. (medscape.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)
Residue7
- A tyrosine residue also plays an important role in photosynthesis . (wikipedia.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)
- A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to a tyrosine residue in a protein . (bionity.com)
- Because protein tyrosine phosphatases (PTPs) all harbor an absolutely conserved catalytic cysteine residue, oxidation of this residue inactivates PTPs, rendering tyrosine kinase signaling pathways highly sensitive to the local redox environment. (sciencemag.org)
- Each side of the dimer protein includes pyridoxal phosphate (PLP) bonded to the Lys280 residue of the tyrosine aminotransferase molecule. (wikipedia.org)
- This induces long-range allostery via protein domain dynamics, causing the structure to be destabilized, resulting in the opening up of the SH3, SH2 and kinase domains and the autophosphorylation of the residue tyrosine 416. (wikipedia.org)
Dopamine18
- Tyrosine is easily made in the body from phenylalanine and is very important to general metabolism, as it is a direct precursor of both adrenaline (as well as norepinephrine and dopamine) and thyroid hormones, all stimulants to metabolism and the nervous system. (healthy.net)
- The human body also uses l-tyrosine to make serotonin and dopamine , two important neurotransmitter s. (everything2.com)
- As a building block for several important brain chemicals, tyrosine is needed to make epinephrine, norepinephrine, serotonin, and dopamine, all of which work to regulate mood. (healthyplace.com)
- Finally, in the mid 1980s some researchers speculated that tyrosine may be useful for treating Parkinson's because this amino acid can increase dopamine levels. (healthyplace.com)
- In this study, we investigated whether creativity in convergent- and divergent-thinking tasks is promoted by the food supplement l -Tyrosine (TYR)-a biochemical precursor of dopamine, which is assumed to drive cognitive control and creativity. (springer.com)
- Tyrosine influences pigment production and the development of dopamine in the brain. (healthline.com)
- Take tyrosine for instance, your body uses this amino acid to produce epinephrine, norepinephrine, and dopamine, brain chemicals that influence mood. (livestrong.com)
- Besides being necessary for normal growth and development, tyrosine serves as a precursor to the neurotransmitters dopamine, norepinephrine and epinephrine. (ralphs.com)
- Tyrosine improves clinical signs of dopamine-dependent depression. (greenmedinfo.com)
- Tyrosine is a precursor of adrenaline and the neurotransmitters norepinephrine and dopamine, which stimulates metabolism and the nervous system, and regulates mood. (herbalremedies.com)
- L-Tyrosine, a constituent of dietary protein, is a substrate or precursor to the catecholamine neurotransmitters norepinephrine, epinephrine and dopamine, the levels of which can be affected by the amount of tyrosine consumed. (jarrow.com)
- N-Acetyl Tyrosine supports brain function by improving the synthesis of the catecholamines norepinephrine and dopamine (neurotransmitters). (patientslikeme.com)
- NOW L-Tyrosine is a non-essential amino acid that plays an important role in the production of neurotransmitters dopamine and norepinephrine. (netrition.com)
- dopamine from L-tyrosine: step 1/2. (abcam.com)
- Production of Catecholamines - Tyrosine is the basic building block of this important group of neurotransmitters which include dopamine, adrenaline/epinephrine, and noradrenaline/norepinephrine have an energizing effect on the brain. (ei-resource.org)
- Since tyrosine is the amino acid building block of the energizing catecholamine neurotransmitters such as dopamine and noradrenaline/norepinephrine I thought it would be well worth trying it to see if it alleviated my symptoms. (ei-resource.org)
- This quality free-form amino acid supplement supplies 500 mg of L-tyrosine which is a precursor to the neurotransmitter dopamine, as well as to the adrenal hormones norepinephrine and epinephrine which may help to heighten mental alertness, offset physical and mental fatigue. (prosource.net)
- N-Acetyl Tyrosine supports brain function by supporting the synthesis of the catecholamines norepinephrine and dopamine (neurotransmitters). (jarrow.com)
Signal transduction4
- 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)
- Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. (wikipedia.org)
- 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)
PATHWAYS4
- 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)
- We describe a nonradioisotopic method that discriminates between reduced and oxidatively modified tyrosine phosphatases, thus facilitating studies that may mechanistically link oxidant activity with specific signaling pathways. (sciencemag.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)
Acetyl-L-Tyrosine4
- 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)
Neurotransmitters1
- Tyrosine is an important precursor for neurotransmitters in the body. (aminoz.com.au)
Precursor2
- Tyrosine is also the precursor to the pigment melanin. (wikipedia.org)
- Tyrosine (or its precursor phenylalanine) is needed to synthesize the benzoquinone structure which forms part of coenzyme Q10. (wikipedia.org)
Gene2
- Bruton's tyrosine kinase (abbreviated Btk or BTK ), also known as tyrosine-protein kinase BTK , is an enzyme that in humans is encoded by the BTK gene . (wikipedia.org)
- L-tyrosine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } 4-hydroxyphenylpyruvate + L-glutamate In humans, the tyrosine aminotransferase protein is encoded by the TAT gene. (wikipedia.org)
Amino acid tyrosine5
- Natural form of the amino acid " tyrosine " which leads to the production of norepinephrine , epinephrine ( adrenaline ), and thyroid hormone . (everything2.com)
- Aside from being a proteinogenic amino acid , tyrosine has a special role by virtue of the phenol functionality. (wikipedia.org)
- 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)
- 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)
Supplements15
- 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)
- 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)
Role of tyrosine1
- 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)
Levels of tyrosine4
- 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)
Suggests that tyrosine3
- 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)
Conversion of tyrosine1
- Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate. (wikipedia.org)
Body makes tyrosine from another1
- The body makes tyrosine from another amino acid called phenylalanine . (webmd.com)
Makes tyrosine1
- 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)
Serine3
- 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)
- N-Benzoyl-L-tyrosine p-nitroanilide (BTPNA) is used as a substrate to identify, differentiate and characterize serine carboxypeptidase(s) and various proteases. (sigmaaldrich.com)
Deficiency7
- 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 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)
- A tyrosine deficiency therefore can contribute to fatigue, mood disorders, cognitive dysfunction, and pain disorders. (ei-resource.org)
Thyroid7
- L-tyrosine is an amino acid that is purported to help boost flagging energy levels or reduce fatigue-related memory problems, often attributed to hormonal insufficiencies due to adrenal fatigue or poor thyroid function. (livestrong.com)
- L-tyrosine is recommended for its beneficial effect on both adrenal and thyroid hormone production in cases of chronic stress, says 'The Stress Effect' author Richard Weinstein. (livestrong.com)
- 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)
- The thyroid hormones triiodothyronine (T3) and thyroxine (T4) in the colloid of the thyroid are also derived from tyrosine. (wikipedia.org)
- 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)
- Production of Thyroid Hormones - Tyrosine combines with iodine to form the thyroid hormones. (ei-resource.org)
Sulfation4
- [7] Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST). (wikipedia.org)
- 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)
- Tyrosine O-sulfation is an irreversible process in vivo . (bionity.com)
- It uses material from the Wikipedia article "Tyrosine_sulfation" . (bionity.com)
Protein tyrosine phosp2
- 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)
Stumbled on tyrosine phosphorylation1
- By Hunter's recollection, he and his colleagues stumbled on tyrosine phosphorylation through their work on the polyoma DNA tumor virus. (asbmb.org)
Melanin5
- Folic acid, niacin, vitamin C, and copper are needed to support tyrosine metabolism into these and other important substances, which also include melanin, estrogen molecules, and the enkephalins (natural pain relievers). (healthy.net)
- 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)
Regulation5
- 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)
Kinase domain2
- 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)
- It includes an SH2 domain, an SH3 domain and a tyrosine kinase domain. (wikipedia.org)
Phosphatases3
- 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)
- 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)
Intracellular tyrosine kinase2
- 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)
Epinephrine1
- 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)
Hydroxyl group2
- 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)
Enzyme1
- citation needed] Tyrosine ammonia lyase (TAL) is an enzyme in the natural phenols biosynthesis pathway. (wikipedia.org)
Effects of tyrosine2
- Learn about the usage, dosage, side-effects of Tyrosine. (healthyplace.com)
- The effects of tyrosine on cognitive performance during extended wakefulness. (memorialhealth.com)
Phenylalanine and tyrosine3
- The Dietary Reference Intake (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)
Molecule2
- One of the oxygen atoms in O 2 is used to hydroxylate the tyrosine molecule to obtain L -DOPA and the other one is used to hydroxylate the cofactor. (wikipedia.org)
- Tyrosine O-sulfate is a stable molecule and is excreted in urine in animals. (bionity.com)
Biosynthesis1
- Plant biosynthesis of tyrosine from prephenate . (wikipedia.org)
Capsule1
- You will find L-tyrosine in tablet, capsule and pill forms. (livestrong.com)
Phospho-tyrosine1
- T-Cell Protein Tyrosine Phosphatase (TC PTP) is a phospho tyrosine-specific protein phosphatase. (neb.com)
Supplemental tyrosine3
- 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)
Phosphorylate tyrosine1
- 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)
Adrenal2
- Supplemental L-tyrosine helps you if you are suffering from adrenal fatigue with symptoms such as cold hands and feet and depression, Weinstein says. (livestrong.com)
- MayoClinic.com endocrinologist Todd B. Nippoldt cautions against using unproven remedies such as L-tyrosine to alleviate adrenal fatigue or hormone imbalances. (livestrong.com)
Phosphorylates1
- 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)
Mechanism3
- 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)
- 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)
Catecholamine1
- Tyrosine: effects on catecholamine release. (springer.com)
PTPs1
- 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)
Substances1
- Tyrosine is also involved in the synthesis of enkephalins, substances that have pain-relieving effects in the body. (healthyplace.com)
Derivative1
- N-Acetyl Tyrosine is an acetylated derivative of the essential amino acid L-tyrosine. (patientslikeme.com)
Catecholamines1
- 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)
Humans1
- Humans often get tyrosine from foods high in protein. (healthline.com)
Dephosphorylation1
- The activation of c-Src causes the dephosphorylation of the tyrosine 527. (wikipedia.org)