Protein tyrosine phosphatases. Medical search

An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.

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.

A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.

A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.

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.

A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.

A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.

A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.

A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.

A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.

A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.

A subcategory of protein tyrosine phosphatases that are bound to the cell membrane. They contain cytoplasmic tyrosine phosphatase domains and extracellular protein domains that may play a role in cell-cell interactions by interacting with EXTRACELLULAR MATRIX components. They are considered receptor-like proteins in that they appear to lack specific ligands.

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.

A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

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.

Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.

A subclass of receptor-like protein tryosine phosphatases that contain a short extracellular domain, a cytosolic kinase-interaction domain, and single protein tyrosine kinase domain.

A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an N-terminal catalytic domain and a C-terminal PROLINE-rich domain. The phosphatase subtype is predominantly expressed in LYMPHOCYTES and plays a key role in the inhibition of downstream T-LYMPHOCYTE activation. Polymorphisms in the gene that encodes this phosphatase subtype are associated with a variety of AUTOIMMUNE DISEASES.

A subclass of receptor-like protein tryosine phosphatases that contain an extracellular RDGS-adhesion recognition motif and a single cytosolic protein tyrosine phosphate domain.

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.

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. Expression of this phosphatase subtype has been observed in BONE MARROW; fetal LIVER; LYMPH NODES; and T LYMPHOCYTES.

An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.

Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.

A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.

Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.

A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.

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.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

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.

An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.

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.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Established cell cultures that have the potential to propagate indefinitely.

A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. The subtype was originally identified in a cell line derived from MEGAKARYOCYTES.

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.

A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.

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.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

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.

The rate dynamics in chemical or physical systems.

A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

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.

Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.

Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

Proteins prepared by recombinant DNA technology.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

An enzyme that catalyzes the conversion of L-tyrosine, tetrahydrobiopterin, and oxygen to 3,4-dihydroxy-L-phenylalanine, dihydrobiopterin, and water. EC 1.14.16.2.

Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.

A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.

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.

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).

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).)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)

A 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

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.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

A family of synthetic protein tyrosine kinase inhibitors. They selectively inhibit receptor autophosphorylation and are used to study receptor function.

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.

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.

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.

A family of non-receptor, PROLINE-rich protein-tyrosine kinases.

A Janus kinase subtype that is involved in signaling from GROWTH HORMONE RECEPTORS; PROLACTIN RECEPTORS; and a variety of CYTOKINE RECEPTORS such as ERYTHROPOIETIN RECEPTORS and INTERLEUKIN RECEPTORS. Dysregulation of Janus kinase 2 due to GENETIC TRANSLOCATIONS have been associated with a variety of MYELOPROLIFERATIVE DISORDERS.

A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.

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.

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.

A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.

Adherence of cells to surfaces or to other cells.

A signal transducer and activator of transcription that mediates cellular responses to INTERLEUKIN-6 family members. STAT3 is constitutively activated in a variety of TUMORS and is a major downstream transducer for the CYTOKINE RECEPTOR GP130.

A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.

A 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).

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.

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.

The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.

Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.

A genetically heterogeneous, multifaceted disorder characterized by short stature, webbed neck, ptosis, skeletal malformations, hypertelorism, hormonal imbalance, CRYPTORCHIDISM, multiple cardiac abnormalities (most commonly including PULMONARY VALVE STENOSIS), and some degree of INTELLECTUAL DISABILITY. The phenotype bears similarities to that of TURNER SYNDROME that occurs only in females and has its basis in a 45, X karyotype abnormality. Noonan syndrome occurs in both males and females with a normal karyotype (46,XX and 46,XY). Mutations in a several genes (PTPN11, KRAS, SOS1, NF1 and RAF1) have been associated the the NS phenotype. Mutations in PTPN11 are the most common. LEOPARD SYNDROME, a disorder that has clinical features overlapping those of Noonan Syndrome, is also due to mutations in PTPN11. In addition, there is overlap with the syndrome called neurofibromatosis-Noonan syndrome due to mutations in NF1.

Inorganic or organic compounds that contain arsenic.

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.

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.

A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.

A contactin subtype that is predominantly expressed in the CEREBELLUM; HIPPOCAMPUS; NEOCORTEX; and HYPOTHALAMUS.

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.

A Janus kinase subtype that is involved in signaling from a broad variety of CYTOKINE RECEPTORS.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

A subclass of receptor-like protein tryosine phosphatases that contain heavily glycosylated and cysteine-rich extracellular regions that include fibronectin type III-like domains.

The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.

A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES.

Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.

Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.

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.

The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.

A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.

A cell line derived from cultured tumor cells.

A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES and JNK MITOGEN-ACTIVATED PROTEIN KINASES.

LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.

Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.

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)

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A non-receptor protein-tyrosine kinase that is expressed primarily in the BRAIN; OSTEOBLASTS; and LYMPHOID CELLS. In the CENTRAL NERVOUS SYSTEM focal adhesion kinase 2 modulates ION CHANNEL function and MITOGEN-ACTIVATED PROTEIN KINASES activity.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

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.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

An autosomal dominant disorder with an acronym of its seven features (LENTIGO; ELECTROCARDIOGRAM abnormalities; ocular HYPERTELORISM; PULMONARY STENOSIS; abnormal genitalia; retardation of growth; and DEAFNESS or SENSORINEURAL HEARING LOSS). This syndrome is caused by mutations of PTPN11 gene encoding the non-receptor PROTEIN TYROSINE PHOSPHATASE, type 11, and is an allelic to NOONAN SYNDROME. Features of LEOPARD syndrome overlap with those of NEUROFIBROMATOSIS 1 which is caused by mutations in the NEUROFIBROMATOSIS 1 GENES.

Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.

The sum of the weight of all the atoms in a molecule.

A 44-kDa extracellular signal-regulated MAP kinase that may play a role the initiation and regulation of MEIOSIS; MITOSIS; and postmitotic functions in differentiated cells. It phosphorylates a number of TRANSCRIPTION FACTORS; and MICROTUBULE-ASSOCIATED PROTEINS.

Inorganic compounds that contain vanadium as an integral part of the molecule.

A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A ubiquitously expressed membrane glycoprotein. It interacts with a variety of INTEGRINS and mediates responses to EXTRACELLULAR MATRIX PROTEINS.

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.

A member of the immunoglobulin superfamily of neuronal cell adhesion molecules that is required for proper nervous system development. Neural cell adhesion molecule L1 consists of six Ig domains, five fibronectin domains, a transmembrane region and an intracellular domain. Two splicing variants are known: a neuronal form that contains a four-amino acid RSLE sequence in the cytoplasmic domain, and a non-neuronal form that lacks the RSLE sequence. Mutations in the L1 gene result in L1 disease. Neural cell adhesion molecule L1 is predominantly expressed during development in neurons and Schwann cells; involved in cell adhesion, neuronal migration, axonal growth and pathfinding, and myelination.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

A genus of gram-negative, facultatively anaerobic rod- to coccobacillus-shaped bacteria that occurs in a broad spectrum of habitats.

Antibodies directed against immunogen-coupled phosphorylated PEPTIDES corresponding to amino acids surrounding the PHOSPHORYLATION site. They are used to study proteins involved in SIGNAL TRANSDUCTION pathways. (From Methods Mol Biol 2000; 99:177-89)

A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.

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.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

Agents that inhibit PROTEIN KINASES.

Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.

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.

Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.

Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.

Transport proteins that carry specific substances in the blood or across cell membranes.

The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)

3-Phenylchromones. Isomeric form of FLAVONOIDS in which the benzene group is attached to the 3 position of the benzopyran ring instead of the 2 position.

A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.

A protein tyrosine kinase that is required for T-CELL development and T-CELL ANTIGEN RECEPTOR function.

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).

IMMUNOGLOBULINS on the surface of B-LYMPHOCYTES. Their MESSENGER RNA contains an EXON with a membrane spanning sequence, producing immunoglobulins in the form of type I transmembrane proteins as opposed to secreted immunoglobulins (ANTIBODIES) which do not contain the membrane spanning segment.

A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.

The relationship between the dose of an administered drug and the response of the organism to the drug.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

A signal transducer and activator of transcription that mediates cellular responses to INTERFERONS. Stat1 interacts with P53 TUMOR SUPPRESSOR PROTEIN and regulates expression of GENES involved in growth control and APOPTOSIS.

Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

All of the processes involved in increasing CELL NUMBER including CELL DIVISION.

Physiologically inactive substances that can be converted to active enzymes.

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

Elements of limited time intervals, contributing to particular results or situations.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

A family of immunoglobulin-related cell adhesion molecules that are involved in NERVOUS SYSTEM patterning.

The artificial induction of GENE SILENCING by the use of RNA INTERFERENCE to reduce the expression of a specific gene. It includes the use of DOUBLE-STRANDED RNA, such as SMALL INTERFERING RNA and RNA containing HAIRPIN LOOP SEQUENCE, and ANTI-SENSE OLIGONUCLEOTIDES.

The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.

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.

Antigens expressed primarily on the membranes of living cells during sequential stages of maturation and differentiation. As immunologic markers they have high organ and tissue specificity and are useful as probes in studies of normal cell development as well as neoplastic transformation.

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)

A mitogen-activated protein kinase subfamily that is widely expressed and plays a role in regulation of MEIOSIS; MITOSIS; and post mitotic functions in differentiated cells. The extracellular signal regulated MAP kinases are regulated by a broad variety of CELL SURFACE RECEPTORS and can be activated by certain CARCINOGENS.

Mice bearing mutant genes which are phenotypically expressed in the animals.

A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.

Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

An 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.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.

The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.

A lipid phosphatase that acts on phosphatidylinositol-3,4,5-trisphosphate to regulate various SIGNAL TRANSDUCTION PATHWAYS. It modulates CELL GROWTH PROCESSES; CELL MIGRATION; and APOPTOSIS. Mutations in PTEN are associated with COWDEN DISEASE and PROTEUS SYNDROME as well as NEOPLASTIC CELL TRANSFORMATION.

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.

Chemically stimulated aggregation of cell surface receptors, which potentiates the action of the effector cell.

A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.

A negative regulator of the CELL CYCLE that undergoes PHOSPHORYLATION by CYCLIN-DEPENDENT KINASES. RBL2 contains a conserved pocket region that binds E2F4 TRANSCRIPTION FACTOR and E2F5 TRANSCRIPTION FACTOR. RBL2 also interacts with viral ONCOPROTEINS such as POLYOMAVIRUS TUMOR ANTIGENS; ADENOVIRUS E1A PROTEINS; and PAPILLOMAVIRUS E7 PROTEINS.

Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.

Compounds of the general formula R-O-R arranged in a ring or crown formation.

In tissue culture, hairlike projections of neurons stimulated by growth factors and other molecules. These projections may go on to form a branched tree of dendrites or a single axon or they may be reabsorbed at a later stage of development. "Neurite" may refer to any filamentous or pointed outgrowth of an embryonal or tissue-culture neural cell.

A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.

The phosphoric acid ester of serine.

Morphologic alteration of small B LYMPHOCYTES or T LYMPHOCYTES in culture into large blast-like cells able to synthesize DNA and RNA and to divide mitotically. It is induced by INTERLEUKINS; MITOGENS such as PHYTOHEMAGGLUTININS, and by specific ANTIGENS. It may also occur in vivo as in GRAFT REJECTION.

A group of antigens that includes both the major and minor histocompatibility antigens. The former are genetically determined by the major histocompatibility complex. They determine tissue type for transplantation and cause allograft rejections. The latter are systems of allelic alloantigens that can cause weak transplant rejection.

In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.

A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.

An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.

Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.

Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.

Eukaryotic cell line obtained in a quiescent or stationary phase which undergoes conversion to a state of unregulated growth in culture, resembling an in vitro tumor. It occurs spontaneously or through interaction with viruses, oncogenes, radiation, or drugs/chemicals.

Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. (1/4408)

Elevated levels of Src kinase activity have been reported in a number of human cancers, including colon and breast cancer. We have analysed four human breast tumor cell lines that exhibit high levels of Src kinase activity, and have determined that these cell lines also exhibit a high level of a phosphotyrosine phosphatase activity that recognizes the Src carboxy-terminal P-Tyr530 negative regulatory site. Total Src kinase activity in these cell lines is elevated as much as 30-fold over activity in normal control cells and specific activity is elevated as much as 5.6-fold. When the breast tumor cells were grown in the presence of the tyrosine phosphatase inhibitor vanadate, Src kinase activity was reduced in all four breast tumor cell lines, suggesting that Src was being activated by a phosphatase which could recognize the Tyr530 negative regulatory site. In fractionated cell extracts from the breast tumor cells, we found elevated levels of a membrane associated tyrosine phosphatase activity that preferentially dephosphorylated a Src family carboxy-terminal phosphopeptide containing the regulatory tyrosine 530 site. Src was hypophosphorylated in vivo at tyrosine 530 in at least two of the tumor cell lines, further suggesting that Src was being activated by a phosphatase in these cells. In preliminary immunoprecipitation and antibody depletion experiments, we were unable to correlate the major portion of this phosphatase activity with several known phosphatases. (+info)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (2/4408)

Jun N-terminal kinases (JNKs) are serine-threonine kinases that play a critical role in the regulation of cell growth and differentiation. We previously observed that JNK activity is suppressed by all-trans-retinoic acid (t-RA), a ligand for retinoic acid nuclear receptors (RARs), in normal human bronchial epithelial cells, which are growth inhibited by t-RA. In this study, we investigated the mechanism by which t-RA inhibits JNK and the possibility that this signaling event is blocked in non-small cell lung cancer (NSCLC) cells. Virtually all NSCLC cell lines are resistant to the growth-inhibitory effects of t-RA, and a subset of them have a transcriptional defect specific to retinoid nuclear receptors. We found that in NSCLC cells expressing functional retinoid receptors, serum-induced JNK phosphorylation and activity were inhibited by t-RA in a bimodal pattern, transiently within 30 min and in a sustained fashion beginning at 12 h. Retinoid receptor transcriptional activation was required for the late, but not the early, suppression of JNK activity. t-RA inhibited serum-induced JNK activity by blocking mitogen-activated protein (MAP) kinase kinase 4-induced signaling events. This effect of t-RA was phosphatase dependent and involved an increase in the expression of the dual-specificity MAP kinase phosphatase 1 (MKP-1). t-RA did not activate MKP-1 expression or inhibit JNK activity in a NSCLC cell line with retinoid receptors that are refractory to ligand-induced transcriptional activation. These findings provide the first evidence that t-RA suppresses JNK activity by inhibiting JNK phosphorylation. Retinoid receptor transcriptional activation was necessary for the sustained inhibition of JNK activity by t-RA, and this signaling event was disrupted in NSCLC cells with retinoid receptors that are refractory to ligand-induced transcriptional activation. (+info)

Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway. (3/4408)

Shp-2 is an SH2 domain-containing protein tyrosine phosphatase. Although the mechanism remains to be defined, substantial experimental data suggest that Shp-2 is primarily a positive regulator in cell growth and development. We present evidence here that Shp-2, while acting to promote mitogenic signals, also functions as a negative effector in interferon (IFN)-induced growth-inhibitory and apoptotic pathways. Treatment of mouse fibroblast cells lacking a functional Shp-2 with IFN-alpha or IFN-gamma resulted in an augmented suppression of cell viability compared to that of wild-type cells. To dissect the molecular mechanism, we examined IFN-induced activation of signal transducers and activators of transcription (STATs) by electrophoretic mobility shift assay, using a specific DNA probe (hSIE). The amounts of STAT proteins bound to hSIE upon IFN-alpha or IFN-gamma stimulation were significantly increased in Shp-2(-/-) cells. Consistently, tyrosine phosphorylation levels of Stat1 upon IFN-gamma treatment and, to a lesser extent, upon IFN-alpha stimulation were markedly elevated in mutant cells. Furthermore, IFN-gamma induced a higher level of caspase 1 expression in Shp-2(-/-) cells than in wild-type cells. Reintroduction of wild-type Shp-2 protein reversed the hypersensitivity of Shp-2(-/-) fibroblasts to the cytotoxic effect of IFN-alpha and IFN-gamma. Excessive activation of STATs by IFNs was also diminished in mutant cells in which Shp-2 had been reintroduced. Together, these results establish that Shp-2 functions as a negative regulator of the Jak/STAT pathway. We propose that Shp-2 acts to promote cell growth and survival through two mechanisms, i.e., the stimulation of growth factor-initiated mitogenic pathways and the suppression of cytotoxic effect elicited by cytokines, such as IFNs. (+info)

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor. (4/4408)

Tumor necrosis factor (TNF)-induced apoptosis can be inhibited by overexpression of specific tyrosine kinases or activation of tyrosine kinase cascades, suggesting potential antagonism between apoptotic and tyrosine kinase signaling processes. In this report, the effects of TNF on EGF receptor tyrosine phosphorylation in ME-180 cell variants selected for apoptotic sensitivity (Sen) or resistance (Res) to TNF, previously shown to differentially express EGFr, were examined. Prior to the onset of apoptosis, TNF caused a significant reduction in the level of EGFr tyrosine phosphorylation in Sen cells but mediated only limited suppression of EGFr tyrosine phosphorylation in apoptotically resistant Res cells. In vitro incubation of cellular membranes with TNF derived from Sen cells stimulated a resident protein tyrosine phosphatase (PTP) activity which was able to dephosphorylate EGFr or tyrosine phosphopeptides mimicking an EGFr autophosphorylation site. In membrane preparations, PTPIB complexed with tyrosine phosphorylated EGFr and this association was disrupted by TNF through an apparent stimulation of PTP activity and turnover of phosphotyrosine. Intrinsic enzymatic activity of PTP1B was 2-3-fold higher in Sen versus Res cell lysates and a family of PTP1B-related proteins with altered C-termini was found to be highly expressed in Sen cells but absent or expressed at reduced levels in Res cells. Cytoplasmic extracts of Sen cells contained PTP1B-like proteins and TNF incubation resulted in the time dependent accumulation of PTP1B-like proteins in Sen cells but did not effect these proteins in Res cells. Together, these results suggest that specific changes in expression and subcellular distribution of phosphotyrosine modulatory proteins may play a role in conveying intrinsic apoptotic sensitivity to TNF in some tumor cell types. (+info)

gp49B1 inhibits IgE-initiated mast cell activation through both immunoreceptor tyrosine-based inhibitory motifs, recruitment of src homology 2 domain-containing phosphatase-1, and suppression of early and late calcium mobilization. (5/4408)

We define by molecular, pharmacologic, and physiologic approaches the proximal mechanism by which the immunoglobulin superfamily member gp49B1 inhibits mast cell activation mediated by the high affinity Fc receptor for IgE (FcepsilonRI). In rat basophilic leukemia-2H3 cells expressing transfected mouse gp49B1, mutation of tyrosine to phenylalanine in either of the two immunoreceptor tyrosine-based inhibitory motifs of the gp49B1 cytoplasmic domain partially suppressed gp49B1-mediated inhibition of exocytosis, whereas mutation of both abolished inhibitory capacity. Sodium pervanadate elicited tyrosine phosphorylation of native gp49B1 and association of the tyrosine phosphatases src homology 2 domain-containing phosphatase-1 (SHP-1) and SHP-2 in mouse bone marrow-derived mast cells (mBMMCs). SHP-1 associated transiently with gp49B1 within 1 min after coligation of gp49B1 with cross-linked FcepsilonRI in mBMMCs. SHP-1-deficient mBMMCs exhibited a partial loss of gp49B1-mediated inhibition of FcepsilonRI-induced exocytosis at concentrations of IgE providing optimal exocytosis, revealing a central, but not exclusive, SHP-1 requirement in the counter-regulatory pathway. Coligation of gp49B1 with cross-linked FcepsilonRI on mBMMCs inhibited early release of calcium from intracellular stores and subsequent influx of extracellular calcium, consistent with SHP-1 participation. Because exocytosis is complete within 2 min in mBMMCs, our studies establish a role for SHP-1 in the initial counter-regulatory cellular responses whereby gp49B1 immunoreceptor tyrosine-based inhibition motifs rapidly transmit inhibition of FcepsilonRI-mediated exocytosis. (+info)

Involvement of tyrosine phosphorylation in HMG-CoA reductase inhibitor-induced cell death in L6 myoblasts. (6/4408)

Our previous studies have shown that the HMG-CoA reductase (HCR) inhibitor (HCRI), simvastatin, causes myopathy in rabbits and kills L6 myoblasts. The present study was designed to elucidate the molecular mechanism of HCRI-induced cell death. We have demonstrated that simvastatin induces the tyrosine phosphorylation of several cellular proteins within 10 min. These phosphorylations were followed by apoptosis, as evidenced by the occurrence of internucleosomal DNA fragmentation and by morphological changes detected with Nomarski optics. Simvastatin-induced cell death was prevented by tyrosine kinase inhibitors. The MTT assay revealed that the addition of mevalonic acid into the culture medium partially inhibited simvastatin-induced cell death. Thus, these results suggested that protein tyrosine phosphorylation might play an important role in the intracellular signal transduction pathway mediating the HCRI-induced death of myoblasts. (+info)

Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (7/4408)

Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction. (+info)

Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. (8/4408)

Protein tyrosine phosphatase-1B (PTP-1B) has been implicated in the negative regulation of insulin signaling. Disruption of the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP-1B+/+ littermates. The enhanced insulin sensitivity of the PTP-1B-/- mice was also evident in glucose and insulin tolerance tests. The PTP-1B-/- mice showed increased phosphorylation of the insulin receptor in liver and muscle tissue after insulin injection in comparison to PTP-1B+/+ mice. On a high-fat diet, the PTP-1B-/- and PTP-1B+/- mice were resistant to weight gain and remained insulin sensitive, whereas the PTP-1B+/+ mice rapidly gained weight and became insulin resistant. These results demonstrate that PTP-1B has a major role in modulating both insulin sensitivity and fuel metabolism, thereby establishing it as a potential therapeutic target in the treatment of type 2 diabetes and obesity. (+info)

The symptoms of Noonan syndrome can vary widely among individuals, but typically include:

* Short stature and short arms and legs
* Concave chest (pectus excavatum)
* Mild to moderate intellectual disability
* Delayed development of speech and language skills
* Distinctive facial features such as a long, narrow face, low-set ears, and a prominent forehead
* Heart defects, particularly pulmonary valve stenosis or atrial septal defect
* Eye problems, including crossed eyes (strabismus) or double vision (diplopia)
* Hearing loss
* Skeletal abnormalities such as curved spine (scoliosis) or missing or deformed ribs

Noonan syndrome is usually diagnosed based on a combination of clinical features and genetic testing. Treatment for the disorder typically focuses on managing any associated medical problems, such as heart defects or hearing loss, and providing support for intellectual and developmental delays. In some cases, medications may be prescribed to help manage symptoms such as high blood pressure or hyperthyroidism.

While there is no cure for Noonan syndrome, early diagnosis and intervention can help improve outcomes for individuals with the disorder. With appropriate support and resources, many people with Noonan syndrome are able to lead fulfilling lives and achieve their goals.

* Skin changes, such as freckles-like spots (lentigines) on the skin, hair, and eyes
* Electrocardiographic abnormalities, such as arrhythmias and prolonged QT interval
* Oculocutaneous albinism, which affects the pigmentation of the skin, hair, and eyes
* Pulmonary stenosis, a narrowing of the pulmonary valve that can lead to heart problems
* Abnormal genitalia in males
* Deafness or hearing loss

Leopard syndrome is typically diagnosed based on a combination of clinical findings and genetic testing. Treatment for the disorder is focused on managing the individual symptoms, such as cardiovascular problems, hearing loss, and vision issues. The prognosis for individuals with leopard syndrome varies depending on the severity of the symptoms and the presence of any additional health problems. With appropriate management, many individuals with leopard syndrome can lead active and productive lives.

Explanation: Neoplastic cell transformation is a complex process that involves multiple steps and can occur as a result of genetic mutations, environmental factors, or a combination of both. The process typically begins with a series of subtle changes in the DNA of individual cells, which can lead to the loss of normal cellular functions and the acquisition of abnormal growth and reproduction patterns.

Over time, these transformed cells can accumulate further mutations that allow them to survive and proliferate despite adverse conditions. As the transformed cells continue to divide and grow, they can eventually form a tumor, which is a mass of abnormal cells that can invade and damage surrounding tissues.

In some cases, cancer cells can also break away from the primary tumor and travel through the bloodstream or lymphatic system to other parts of the body, where they can establish new tumors. This process, known as metastasis, is a major cause of death in many types of cancer.

It's worth noting that not all transformed cells will become cancerous. Some forms of cellular transformation, such as those that occur during embryonic development or tissue regeneration, are normal and necessary for the proper functioning of the body. However, when these transformations occur in adult tissues, they can be a sign of cancer.

See also: Cancer, Tumor

Word count: 190

... a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate Protein tyrosine (pTyr) phosphorylation is a common post ... Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes ... "The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1". Protein Sci. 15 (6): 1500- ... Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine ...

https://en.wikipedia.org/wiki/Protein_tyrosine_phosphatase

Receptor tyrosine phosphatases are enzyme-linked receptor phosphatases, a sub-class of protein tyrosine phosphatases. Types ... v t e (Protein pages needing a picture, Transmembrane receptors, Single-pass transmembrane proteins, All stub articles, Enzyme ...

https://en.wikipedia.org/wiki/Receptor_tyrosine_phosphatase

Zhang ZY (2002). "Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development". ... The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. ... A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its ... Knobler, Hilla; Elson, Ari (May 2014). "Metabolic regulation by protein tyrosine phosphatases". Journal of Biomedical Research ...

https://en.wikipedia.org/wiki/Protein_phosphatase

... purple acid phosphatases (PAPs), and most recently, protein tyrosine phosphatase-like phytases (PTP-like phytases). Most of the ... "Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase". Protein Science ... Zhang ZY (2003). Mechanistic studies on protein tyrosine phosphatases. Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic ... Puhl A, Greiner R, Selinger LB (2008). "A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ...

https://en.wikipedia.org/wiki/Phytase

Cho H (2013). "Protein tyrosine phosphatase 1B (PTP1B) and obesity". Vitamins and Hormones. 91: 405-24. doi:10.1016/B978-0-12- ... similar to squalamine that is an allosteric inhibitor of protein-tyrosine phosphatase 1B (PTP1B). It was isolated from the ...

https://en.wikipedia.org/wiki/Trodusquemine

"Protein tyrosine phosphatases in the human genome". Cell. 117 (6): 699-711. doi:10.1016/j.cell.2004.05.018. PMID 15186772. ... Myotubularin related protein 14 also known as MTMR14 is a protein which in humans is encoded by the MTMR14 gene. Expression of ... MTMR14 is a phosphatidylinositol-3-phosphatase that dephosphorylates the same substrates as myotubularin, PtdIns(3)P and PtdIns ... 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287- ...

https://en.wikipedia.org/wiki/MTMR14

June 2004). "Protein tyrosine phosphatases in the human genome". Cell. 117 (6): 699-711. doi:10.1016/j.cell.2004.05.018. PMID ... The FA proteins play an elaborate role with FAN1 to remove these ICLs. The pathway consists of 15 known proteins. Three of them ... It is a structure dependent endonuclease and a member of the myotubularin-related class 1 cysteine-based protein tyrosine ... This is present in proteins that bind to ubiquitinated proteins, and is highly conserved across eukaryotes. This Zinc finger is ...

https://en.wikipedia.org/wiki/FAN1

Protein Tyrosine Phosphatase; Rab11a: Member RAS Oncogene Family; RGS2: Regulator Of G-Protein Signaling 2; RyR1: Ryanodine ... "TRPV6 protein expression summary". The Human Protein Atlas. Retrieved 2020-08-01. Lehen'kyi V, Raphaël M, Prevarskaya N (March ... Shin YC, Shin SY, So I, Kwon D, Jeon JH (January 2011). "TRIP Database: a manually curated database of protein-protein ... of proteins. The TRP family is a group of channel proteins critical for ionic homeostasis and the perception of various ...

https://en.wikipedia.org/wiki/TRPV6

Lorenz, Ulrike (2017-05-07). "Protein Tyrosine Phosphatase Assays". Current Protocols in Immunology. 91 (1): 11.7.1-12. doi: ... This property can be used to determine the activity of various phosphatases including alkaline phosphatase (AP) and protein ... tyrosine phosphatase (PTP). The substance is sensitive to light, and thus should be stored protected from light. This is also ... Phosphatases catalyze the hydrolysis of pNPP liberating inorganic phosphate and the conjugate base of para-nitrophenol (pNP). ...

https://en.wikipedia.org/wiki/Para-Nitrophenylphosphate

Takagi T, Moore CR, Diehn F, Buratowski S (June 1997). "An RNA 5′-triphosphatase related to the protein tyrosine phosphatases ... Wen Y, Yue Z, Shatkin AJ (October 1998). "Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism". ... Deshpande T, Takagi T, Hao L, Buratowski S, Charbonneau H (June 1999). "Human PIR1 of the protein-tyrosine phosphatase ... These enzymes are very much similar to protein tyrosine phosphatases in their structure and mechanism. This family includes ...

https://en.wikipedia.org/wiki/Polynucleotide_5'-phosphatase

It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family ... dual-specificity protein tyrosine phosphatases". Molecules and Cells. 8 (1): 2-11. PMID 9571625. Keyse SM (Apr 1998). "Protein ... Keyse SM, Emslie EA (Oct 1992). "Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase". ... "The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase". Proceedings of the National ...

https://en.wikipedia.org/wiki/DUSP1

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. Protein tyrosine phosphatases ... "Receptor protein tyrosine phosphatases, cell adhesion and signal transduction". Advances in Protein Phosphatases. 8: 241-71. ... "Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine ... Rosdahl JA, Mourton TL, Brady-Kalnay SM (2002). "Protein kinase C delta (PKCdelta) is required for protein tyrosine phosphatase ...

https://en.wikipedia.org/wiki/PTPRM

"SHP1 and SHP2 Protein-tyrosine Phosphatases Associate with βc after Interleukin-3-induced Receptor Tyrosine Phosphorylation". ... Xu, Dan; Qu, Cheng-Kui (2008). "Protein tyrosine phosphatases in the JAK/STAT pathway". Frontiers in Bioscience. 13 (1): 4925- ... Yi, T L; Cleveland, J L; Ihle, J N (1992). "Protein tyrosine phosphatase containing SH2 domains: characterization, preferential ... Signal transducing adaptor protein, a helper protein used by major proteins in signalling pathways. Aaronson DS, Horvath CM ( ...

https://en.wikipedia.org/wiki/JAK-STAT_signaling_pathway

... and opposing the action of the tyrosine kinases were 108 protein phosphatases that can remove phosphate from P.Tyr in proteins ... Two important classes of tyrosine kinase in tyrosine phosphorylation are receptor tyrosine kinase and nonreceptor tyrosine ... whereas protein tyrosine phosphatases (PTPs) remove the phosphate group from phosphotyrosine. Tyrosine phosphorylation of ... 2004). "Protein tyrosine phosphatases in the human genome". Cell. 117 (6): 699-711. doi:10.1016/j.cell.2004.05.018. PMID ...

https://en.wikipedia.org/wiki/Tyrosine_phosphorylation

Martell KJ, Angelotti T, Ullrich A (1998). "The "VH1-like" dual-specificity protein tyrosine phosphatases". Mol. Cells. 8 (1): ... Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene. Dual specificity protein ... Tanoue, T; Yamamoto T; Maeda R; Nishida E (Jul 2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 ... Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha ...

https://en.wikipedia.org/wiki/DUSP10

Liu F, Hill DE, Chernoff J (1996). "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src ... a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877-85. doi:10.1038/sj.onc.1201279 ... "Fyn and Lck tyrosine kinases regulate tyrosine phosphorylation of p105CasL, a member of the p130Cas docking protein family, in ... novel SH2-containing protein family), and other proteins such as the Id family of helix-loop-helix proteins. In terms of post- ...

https://en.wikipedia.org/wiki/NEDD9

Receptor-type tyrosine-protein phosphatase F is an enzyme that in humans is encoded by the PTPRF gene. The protein encoded by ... "Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin ... "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". ... "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". ...

https://en.wikipedia.org/wiki/PTPRF

This causes severe truncation and loss of function in the gene's protein product, tyrosine phosphatase SHP-2. SHP-2 plays an ... "OMIM Entry * 176876 - PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 11; PTPN11". omim.org. Retrieved 23 March 2022. Yang, ... Gonzalez-Quevedo, Rosa (31 January 2005). "Receptor tyrosine phosphatase-dependent cytoskeletal remodeling by the hedgehog- ... Given that the mutation causes a loss of protein function and displays a dominant inheritance pattern, it is hypothesized that ...

https://en.wikipedia.org/wiki/Metachondromatosis

Tonks, Nicholas K. (2006). "Protein tyrosine phosphatases: from genes, to function, to disease". Nature Reviews Molecular Cell ... A protein phosphatase is an enzyme that dephosphorylates an amino acid residue of its protein substrate. Whereas protein ... Acid phosphatase Alkaline phosphatase Endonuclease/Exonuclease/phosphatase family Kinase Phosphatome Phosphotransferase Protein ... Similarly, dual-specificity tyrosine phosphatases can dephosphorylate not only tyrosine residues, but also serine residues. ...

https://en.wikipedia.org/wiki/Phosphatase

Protein tyrosine phosphatases (PTPs) restore nRTKs to their basal state of activity. In some cases PTPs positively regulate ... to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that ... nRTKs also possess domains that mediate protein-protein, protein-lipid, and protein-DNA interactions. One of the protein- ... Tonks NK, Neel BG (November 1996). "From form to function: signaling by protein tyrosine phosphatases". Cell. 87 (3): 365-8. ...

https://en.wikipedia.org/wiki/Non-receptor_tyrosine_kinase

Tiganis T (January 2002). "Protein tyrosine phosphatases: dephosphorylating the epidermal growth factor receptor". IUBMB Life. ... Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function". Molecular and Cellular ... "Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. ... "Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and ...

https://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor

2012), showed that McsB and YwlE are a protein arginine kinase and phosphatase, rather than a tyrosine kinase and phosphatase ... and YwlE is a phosphatase-arginine-phosphatase (PAP). Many proteins rely on protein phosphatase activity for regulating their ... YwIE was thought to be a protein-tyrosine-phosphatase, and McsB a tyrosine-kinase, however in 2012 Elsholz et al. showed that ... YwIE is a member of the low-molecular-weight protein tyrosine phosphatase (LMW-PTP). It is the only active PAP present in B. ...

https://en.wikipedia.org/wiki/Protein_arginine_phosphatase

CagA then allosterically activates protein tyrosine phosphatase/protooncogene Shp2. Pathogenic strains of H. pylori have been ... Once inside the cell, the CagA protein is phosphorylated on tyrosine residues by a host cell membrane-associated tyrosine ... The latter provide information of how proteins interact with each other, e.g. in stable protein complexes or in more dynamic, ... Furthermore, the interactome of H. pylori has been systematically studied and more than 3000 protein-protein interactions have ...

https://en.wikipedia.org/wiki/Helicobacter_pylori

His research is mainly focused on studying the function and regulation of protein tyrosine phosphatases. He did his ... Tonks, Nicholas K. (2006). "Protein tyrosine phosphatases: from genes, to function, to disease". Nature Reviews Molecular Cell ... After graduation, he joined Sir Philip Cohen lab in University of Dundee for his PhD study in protein phosphatase from 1982- ... "MRC Protein Phosphorylation Unit :: Research :: Philip Cohen :: Profiles for Past Lab Members". Ppu.mrc.ac.uk. Retrieved 5 May ...

https://en.wikipedia.org/wiki/Nicholas_Kester_Tonks

A 170 amino acid domain, the so-called MAM (meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu) domain, has been ... a developmentally-regulated cell surface protein; Xenopus nrp1; P28824); and receptor-like tyrosine protein phosphatase. The ... expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase". FEBS Lett. 290 (1): 123- ... Protein domains, Single-pass transmembrane proteins, All stub articles, Membrane protein stubs). ...

https://en.wikipedia.org/wiki/MAM_domain

The function of protein tyrosine kinases and protein-tyrosine phosphatase counterbalances the level of phosphotyrosine on any ... The malfunctioning of specific chains of protein tyrosine kinases and protein tyrosine phosphatase has been linked to multiple ... and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the ... In the late 1980s and early 1990s, the first protein tyrosine phosphatase (PTP1B) was purified and the discovery, as well as, ...

https://en.wikipedia.org/wiki/Protein_phosphorylation

Imai discovered three kinds of protein tyrosine phosphatase (PTP) genes having the function of controlling the signal ... "Mammalian SH2-containing protein tyrosine phosphatase". Cell. 85 (1): 15. doi:10.1016/s0092-8674(00)81077-6. PMID 8620532. ... similarity in genomic organization within protein-tyrosine phosphatasegenes". Oncogene. 9 (10): 3031-3035. PMID 8084610. Adachi ...

https://en.wikipedia.org/wiki/Kohzoh_Imai

PTPLAD2 is a protein tyrosine phosphatase. The exact function of KIAA1797 is not yet understood by the scientific community. It ... KIAA1797 is a protein that in humans is encoded by the KIAA1797 gene. A specific single-nucleotide polymorphism rs7875153 in ... KIAA1797 is a protein-coding gene in Homo sapiens. Alternate names for the gene are FLJ20375, OTTHUMP00000069845, and ... The main isoform of the human protein is 1801 amino acids long, a total of 200,072 Da. Two distinct domains of unknown function ...

https://en.wikipedia.org/wiki/KIAA1797

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene. ... "Entrez Gene: PTPN7 protein tyrosine phosphatase, non-receptor type 7". Pettiford SM, Herbst R (February 2000). "The MAP-kinase ... Adachi M, Sekiya M, Arimura Y, Takekawa M, Itoh F, Hinoda Y, Imai K, Yachi A (1992). "Protein-tyrosine phosphatase expression ...

https://en.wikipedia.org/wiki/PTPN7

Kwak SP, Dixon JE (Jan 1995). "Multiple dual specificity protein tyrosine phosphatases are expressed and regulated ... The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases ... "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases". Genomics. 22 (2): 462-4. doi:10.1006/geno. ... a dual specificity MAP kinase protein phosphatase". Proteins. 66 (1): 253-8. doi:10.1002/prot.21224. PMID 17078075. S2CID ...

https://en.wikipedia.org/wiki/DUSP5

... which contains multiple binding sites for the initiator protein DnaA (a highly homologous protein amongst bacterial kingdom). ... This pocket has a tyrosine residue that is able to form van der Waals interactions with the correctly paired nucleotide. In ... by inorganic phosphatase) into two phosphates. This hydrolysis drives DNA synthesis to completion. Furthermore, DNA polymerase ... In E. coli these proteins include DiaA, SeqA, IciA, HU, and ArcA-P, but they vary across other bacterial species. A few other ...

https://en.wikipedia.org/wiki/Prokaryotic_DNA_replication

"The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase ... Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B (2002). "The transmembrane receptor protein tyrosine phosphatase DEP1 ... Ren Y, Busch RK, Perlaky L, Busch H (May 1998). "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts with ... Ren Y, Busch RK, Perlaky L, Busch H (1998). "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts with ...

https://en.wikipedia.org/wiki/NOL1

The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of ... by a human protein-tyrosine phosphatase". Science. 250 (4987): 1573-6. Bibcode:1990Sci...250.1573G. doi:10.1126/science.1703321 ... Galaktionov K, Beach D (1992). "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple ... Draetta G, Eckstein J (1997). "Cdc25 protein phosphatases in cell proliferation". Biochim. Biophys. Acta. 1332 (2): M53-63. doi ...

https://en.wikipedia.org/wiki/CDC25C

"Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl ... Tyrosine-protein kinase ABL1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL ... "A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle". ... Cao C, Leng Y, Li C, Kufe D (April 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the ...

https://en.wikipedia.org/wiki/ABL_(gene)

Srinivasan S, Mahowald AP, Fuller MT (April 2012). "The receptor tyrosine phosphatase Lar regulates adhesion between Drosophila ... Mahowald was concerned as to why organisms have multiple, very similar, genes that encode for the same proteins with only a few ... In Drosophila testicles, the Leukocyte-antigen-related (LAR) receptor tyrosine phosphatase targets selection and synapse ... these amino acid substitutions in Act5C and Act42A did not occur in regions of the actin molecule where actin binding proteins ...

https://en.wikipedia.org/wiki/Anthony_Mahowald

... the heat shock protein 70 (hsp70) and the protein FKBP4 (FK506-binding protein 4). The endogenous glucocorticoid hormone ... the role of tyrosine 735". Molecular Endocrinology. 17 (5): 845-859. doi:10.1210/me.2002-0320. PMID 12569182. Schulz M, Eggert ... "Glucocorticoid regulation of alkaline phosphatase, osteocalcin, and proto-oncogenes in normal human osteoblast-like cells". ... Hulkko SM, Wakui H, Zilliacus J (August 2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the ...

https://en.wikipedia.org/wiki/Glucocorticoid_receptor

"Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha". Cancer Research. 62 (22): 6357-61. PMID ... of phosphoinositides are ubiquitous second messengers that function downstream of many G protein-coupled receptors and tyrosine ... This enzyme is an integral membrane protein localized to two subcellular domains, the matrix side of the inner mitochondrial ... kinases regulating cell growth, calcium metabolism, and protein kinase C activity. This gene encodes an enzyme which regulates ...

https://en.wikipedia.org/wiki/CDS1_(gene)

The algal toxin microcystin is also a peptide and is an inhibitor of protein phosphatases. This toxin can contaminate water ... A notable class of kinase drug targets is the receptor tyrosine kinases which are essential enzymes that regulate cell growth; ... which bind to ribonucleases in one of the tightest known protein-protein interactions. A special case of protein enzyme ... "Molecular enzymology underlying regulation of protein phosphatase-1 by natural toxins". Current Medicinal Chemistry. 9 (22): ...

https://en.wikipedia.org/wiki/Enzyme_inhibitor

Angers-Loustau A, Côté JF, Charest A, Dowbenko D, Spencer S, Lasky LA, Tremblay ML (1999). "Protein tyrosine phosphatase-PEST ... Garton AJ, Tonks NK (1999). "Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST". J. Biol. Chem. ... Adapter molecule crk is a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. This ... "P130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading". Mol. Biol. Cell. 15 ...

https://en.wikipedia.org/wiki/Adapter_molecule_crk

"Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of ... Highly conserved phosphatase domain is in central part of the protein. This catalytic domain is flanked on the N-terminal side ... "Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of ... SHIP1 is a 145 kDa large protein and member of the inositol polyphosphate-5-phosphatase (INPP5) family. Alternate ...

https://en.wikipedia.org/wiki/INPP5D

1994). "Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45". J. ... 1995). "Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation ... 1995). "Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the ... 1994). "Activation and serine phosphorylation of the p56lck protein tyrosine kinase in response to antigen receptor cross- ...

https://en.wikipedia.org/wiki/CD79B

April 2016). "Low-Molecular-Weight Protein Tyrosine Phosphatase Predicts Prostate Cancer Outcome by Increasing the Metastatic ... The most important of these might be the tyrosine phosphatase ACP1 of which the expression might outperform the Gleason grading ... Alkaline phosphatase is more elevated in metastatic than non-metastatic cells. High levels of alkaline phosphatase is ... Transport protein ZIP1 is responsible for the transport of zinc into prostate cells. One of zinc's important roles is to change ...

https://en.wikipedia.org/wiki/Prostate_cancer

... protein synthesis - protein targeting - protein translocation - protein-tyrosine kinase - protein-tyrosine-phosphatase - ... protein - protein biosynthesis - Protein Data Bank - protein design - protein expression - protein folding - protein isoform - ... protein nuclear magnetic resonance spectroscopy - protein P16 - protein P34cdc2 - protein precursor - protein structure ... receptor protein-tyrosine kinase - recombinant fusion protein - recombinant interferon-gamma - recombinant protein - ...

https://en.wikipedia.org/wiki/Index_of_biochemistry_articles

Sekar, Y; Moon, TC; Slupsky, CM; Befus, AD (1 July 2010). "Protein tyrosine nitration of aldolase in mast cells: a plausible ... alkaline phosphatase and aldolase isozymes in tissue sections". Histochemistry. 48 (2): 101-9. doi:10.1007/BF00494548. PMID ... In human mast cells (MCs), ALDOA has been observed to undergo post-translational regulation by protein tyrosine nitration, ... the key catalytic amino acid residues involved in the reaction are lysine and tyrosine. The tyrosine acts as an efficient ...

https://en.wikipedia.org/wiki/Aldolase_A

Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex". The Journal of Biological Chemistry. 282 (33): 23878-91. doi: ... By directly binding membrane PtdIns(3)P, the FYVE finger domain of PIKfyve is essential in localizing the protein to the ... January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94-101. ... December 2008). "VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and ...

https://en.wikipedia.org/wiki/PIKFYVE

PTPRF encodes protein phosphatase which can localize at adherent junction. This phosphatase may also regulate epithelial cell ... The protein tyrosine receptor type F gene (PTPRF) is particularly important in nipple-areola region development. ... Amastia may also be caused by the inability of producing parathyroid hormone related protein. The absence of this protein will ...

https://en.wikipedia.org/wiki/Amastia

"The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase ... Also known as the ubiquitin-binding protein p62, it is an autophagosome cargo protein that targets other proteins that bind to ... Geetha T, Wooten MW (February 2003). "Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve ... "The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor". J. Biol. ...

https://en.wikipedia.org/wiki/Sequestosome_1

PTP-PEST, a soluble protein tyrosine phosphatase that is ubiquitously expressed in mice both during embryonic development and ... allowing the CAS protein to function as a scaffold for other proteins including CRK proteins and C3G, a guanine nucleotide ... In humans, the 561 amino acid EFS protein acts as a scaffolding protein for cell signaling based on interactions with SRC, FAK ... these tyrosine motifs are bound by the SH2 domains of signaling proteins. Important binding partners for this region include ...

https://en.wikipedia.org/wiki/Embryonal_fyn-associated_substrate

"Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of ... "Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45". The Journal ... is a protein that in humans is encoded by the CD79A gene. The CD79a protein together with the related CD79b protein, forms a ... Flaswinkel H, Reth M (Jan 1994). "Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction ...

https://en.wikipedia.org/wiki/CD79A

Receptor-type tyrosine-protein phosphatase N2 (R-PTP-N2) also known as islet cell autoantigen-related protein (ICAAR) and ... Pietropaolo M, Hutton JC, Eisenbarth GS (February 1997). "Protein tyrosine phosphatase-like proteins: link with IDDM". Diabetes ... the protein encoded by this gene has traditionally been considered a member of the protein tyrosine phosphatase (PTP) family. ... "Entrez Gene: PTPRN2 protein tyrosine phosphatase, receptor type, N polypeptide 2". Caromile LA, Oganesian A, Coats SA, Seifert ...

https://en.wikipedia.org/wiki/PTPRN2

"The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase". EMBO J. 22 (14): 3524-3535. doi: ... Cdc14 is dual-specificity, which means it has serine/threonine and tyrosine-directed activity. A preference for serines next to ... Cdc55, a regulatory subunit of Protein phosphatase 2 (PP2A), sequesters Cdc14 in the nucleolus during early stage of meiosis. ... April 1999). "Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from nucleolar RENT ...

https://en.wikipedia.org/wiki/Cdc14

The signaling cascade is down-regulated by dephosphorylation by protein tyrosine phosphatases. Additional characteristics of ... while receptor protein tyrosine phosphatases (RPTP) (e.g. CD45, CD148) mediate the dephosphorylation of the same residues. SFK ... bind to cytoplasmic tyrosine phosphatases. Immunoreceptor Tyrosine-based Switch Motifs (ITSMs) with the signature TxYxx(I/V) ... lack a cytoplasmic tail and therefore associate with adaptor proteins containing the same tyrosine residues. Adaptor proteins ...

https://en.wikipedia.org/wiki/Non-catalytic_tyrosine-phosphorylated_receptor

... an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases". Mol. Cell. Biol. 10 (12): 6316- ... "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation". J. Biol. Chem. 277 (42 ... This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have ... Pandey A, Lazar DF, Saltiel AR, Dixit VM (December 1994). "Activation of the Eck receptor protein tyrosine kinase stimulates ...

https://en.wikipedia.org/wiki/EPH_receptor_A2

Guan has made seminal contributions in the fields of protein tyrosine phosphatase, Mitogen-Activated Protein (MAP) kinase, and ... TSC1 and TSC2 proteins form a physical and functional complex. Recent studies from Guan's laboratory demonstrate that TSC1/TSC2 ...

https://en.wikipedia.org/wiki/Kun-Liang_Guan

... tyrosine kinase Lck phosphorylates ITAMs in CD3 complex) and factors that inhibit signalling (tyrosine phosphatases CD45 and ... On plasma membrane of a T cell there is the T-cell receptor (consists of α,β chains and multiple CD3 adaptor proteins), as well ... When T-cell and APC membranes separate, the close-contact zone vanishes and large-ectodomain tyrosine phosphatases are allowed ... Lin, J; Weiss, A (18 August 2003). "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates ...

https://en.wikipedia.org/wiki/Kinetic-segregation_model_of_T_cell_activation

"Lysine-independent turnover of cyclin G1 can be stabilized by B'alpha subunits of protein phosphatase 2A". Molecular and ... Cbl is an E3 ubiquitin ligase with a RING finger domain that interacts with its tyrosine kinase binding (TKB) domain, ... coordinating the cellular localization of proteins, activating and inactivating proteins, and modulating protein-protein ... The protein modifications can be either a single ubiquitin protein (monoubiquitylation) or a chain of ubiquitin ( ...

https://en.wikipedia.org/wiki/Ubiquitin

Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 is a protein that in humans is encoded by the ARAP3 ... 2007). "The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner". Cell. ... 2005). "ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP- ... It is a specific PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6-GAP protein. An alternatively spliced transcript has been found ...

https://en.wikipedia.org/wiki/CENTD3

Angers-Loustau A, Côté JF, Charest A, Dowbenko D, Spencer S, Lasky LA, Tremblay ML (March 1999). "Protein tyrosine phosphatase- ... PTK2 protein tyrosine kinase 2 (PTK2), also known as focal adhesion kinase (FAK), is a protein that, in humans, is encoded by ... The encoded protein is a member of the FAK subfamily of protein tyrosine kinases that included PYK2, but lacks significant ... Lineage for Protein: Focal adhesion kinase 1 Q00944 "Entrez Gene: PTK2 PTK2 protein tyrosine kinase 2". Guan JL, Shalloway D ( ...

https://en.wikipedia.org/wiki/PTK2

Together, cells of the immune system express at least half of the 107 protein tyrosine phosphatase (PTP) genes in the hu … ... Reversible tyrosine phosphorylation of proteins is a key regulatory mechanism for numerous important aspects of eukaryotic ... physiology and is catalysed by kinases and phosphatases. ... Protein tyrosine phosphatases and the immune response Tomas ... Protein tyrosine phosphatases and the immune response Tomas Mustelin et al. Nat Rev Immunol. 2005 Jan. ...

https://pubmed.ncbi.nlm.nih.gov/15630428

Protein target information for Protein-tyrosine-phosphatase (zebrafish). Find diseases associated with this biological target ...

https://pubchem.ncbi.nlm.nih.gov/protein/B8A5N7

p,During this funding period, we have successfully developed a lead candidate therapeutic that inhibits a protein that is ... nbsp;By inhibiting this protein on blood stem cells, this therapeutic causes human blood stem cells to regenerate following ...

https://www.cirm.ca.gov/our-progress/awards/protein-tyrosine-phosphatase-sigma-inhibitors-hematopoietic-regeneration

... protein tyrosine phosphatase receptor type C (human). Find diseases associated with this biological target and compounds tested ... PTP_N; Protein tyrosine phosphatase N terminal. * NM_002838.5 → NP_002829.3 receptor-type tyrosine-protein phosphatase C ... PTPc; Protein tyrosine phosphatase, catalytic domain. cd00047. Location:632 → 863. PTPc; Protein tyrosine phosphatases (PTP) ... PTPc; Protein tyrosine phosphatase, catalytic domain. cd00047. Location:614 → 845. PTPc; Protein tyrosine phosphatases (PTP) ...

https://www.ncbi.nlm.nih.gov/gene?term=(PTPRC%5BGene%20Name%5D)%20AND%209606%5BTaxonomy%20ID%5D

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22. Journal of Clinical Investigation, 126(5): ... We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic ... We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic ... Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. ...

https://www.zora.uzh.ch/id/eprint/125052/

Overexpression of protein tyrosine phosphatase 1B impairs glucose-stimulated insulin secretion in INS-1 cells - Minerva ... Lu B, Gu P, Xu Y, Ye X, Wang Y, Du H, et al. Overexpression of protein tyrosine phosphatase 1B impairs glucose-stimulated ... Overexpression of protein tyrosine phosphatase 1B impairs glucose-stimulated insulin secretion in INS-1 cells. Bin LU, Ping GU ... BACKGROUND: Protein tyrosine phosphatase 1B (PTP1B) has been implicated as a negative regulator of insulin signaling. We ...

https://www.minervamedica.it/en/journals/minerva-endocrinology/article.php?cod=R07Y2016N01A0001

... in protein-tyrosine phosphatases",. abstract = "The catalytic activity of protein-tyrosine phosphatases (PTPs) is mediated by a ... Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. / Peters, Günther H.j.; ... Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. Biochemistry. 1998;37(16): ... N2 - The catalytic activity of protein-tyrosine phosphatases (PTPs) is mediated by a cysteine side chain which carries out a ...

https://orbit.dtu.dk/en/publications/electrostatic-evaluation-of-the-signature-motif-hvcx5rst-in-prote

Secrist, JP, Burns, LA, Karnitz, L, Koretzky, GA & Abraham, RT 1993, Stimulatory effects of the protein tyrosine phosphatase ... In this study, we have examined the effects of pervanadate, a powerful inhibitor of protein tyrosine phosphatases (PTP), on the ... Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. In: Journal of ... In this study, we have examined the effects of pervanadate, a powerful inhibitor of protein tyrosine phosphatases (PTP), on the ...

https://mayoclinic.pure.elsevier.com/en/publications/stimulatory-effects-of-the-protein-tyrosine-phosphatase-inhibitor

Protein tyrosine phosphatases (PTPs) are a class of enzymes that play important roles in the regulation of many mammalian ... Exo-affinity labeling agents as inactivators of protein tyrosine phosphatases: Exploiting/exploring/creating covalent chemistry ...

https://www.morressier.com/o/event/5fc631d303137aa525498a83/article/5fc6329a9e0a135cbec99f0f

Moreover, there are important evolutional mutations that can change the conformation of the proteins, for instance, hydrophilic ... which are critical regulators of tyrosine phosphorylation-dependent signaling events. It is a highly plausible candidate for ... PTP1B is a prototypic enzyme of the superfamily protein tyrosine phosphatases (PTPs) ... PTP1B is a prototypic enzyme of the superfamily protein tyrosine phosphatases (PTPs) which are critical regulators of tyrosine ...

https://springerplus.springeropen.com/articles/10.1186/2193-1801-3-380

Tyrosine-protein phosphatase Lar-like [Source:Uni... [more]. ptp-3. 3.542e-39. 34.39. Tyrosine-protein phosphatase Lar-like [ ... Tyrosine-protein phosphatase Lar-like [Source:Uni... [more]. ptp-3. 3.980e-39. 34.39. Tyrosine-protein phosphatase Lar-like [ ... protein tyrosine phosphatase receptor type J [Sour... [more]. PTPRJ. 7.206e-46. 37.25. protein tyrosine phosphatase receptor ... protein tyrosine phosphatase receptor type J [Sour... [more]. PTPRS. 6.038e-43. 38.52. protein tyrosine phosphatase receptor ...

https://planosphere.stowers.org/feature/Schmitea/mediterranea-sexual/transcript/SMED30031329

The SH2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2 have been implicated in regulating signaling from a ... Megakaryocyte-specific deletion of the protein-tyrosine phosphatases Shp1 and Shp2 causes abnormal megakaryocyte development, ... Deletion of the immunoreceptor tyrosine-based inhibition motif-containing receptor G6b-B in the MP lineage phenocopied multiple ...

https://pesquisa.bvsalud.org/perinatal/resource/es/mdl-23509158

Androgen-regulation of the protein tyrosine phosphatase PTPRR activates ERK1/2 signalling in prostate cancer. Lookup NU author( ... Further characterisation of PTPRR protein in LNCaP cells revealed it is an early and direct target of the androgen receptor ...

https://eprints.ncl.ac.uk/209106

Protein tyrosine phosphatase 1B (PTP1B) is known to regulate the ER stress signaling pathway, but its role in neuronal systems ... Neuroprotective Effects of Protein Tyrosine Phosphatase 1B Inhibition against ER Stress-Induced Toxicity Yu-Mi Jeon, Shinrye ... Protein tyrosine phosphatase 1B (PTP1B) is a ubiquitously expressed enzyme anchored in the ER membrane (Popov, 2012). PTP1B ... Ozek, C., Kanoski, S.E., Zhang, Z.Y., Grill, H.J., and Bence, K.K. (2014). Protein-tyrosine phosphatase 1B (PTP1B) is a novel ...

https://www.molcells.org/journal/PubReader.html?volume=40&number=4&spage=280

Role of Protein Tyrosine Phosphatase () Gene [C1858T] Functional Variant in Genetic Susceptibility of Psoriatic Arthritis in ... in the protein tyrosine phosphatase (PTPN22) gene, which encoded Arg620Trp in the lymphoid protein tyrosine phosphatase (LYP) ... The protein tyrosine phosphatase non-receptor 22 (PTPN22) gene, located on chromosome 1p13, codes for a protein, LYP, which is ... Association of protein tyrosine phosphatase non-receptor type 22 gene functional variant C1858T, HLA-DQ/DR genotypes and ...

https://openrheumatologyjournal.com/VOLUME/14/PAGE/15/FULLTEXT/

Low molecular weight protein tyrosine phosphatase (LWM-PTP), also known as acid phosphatase, is a highly conserved tyrosine ... Here, we revealed a homolog of acid phosphatase, APH, in Arabidopsis plants, is a functional protein tyrosine phosphatase. The ... Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis. Yanyan Du, ... Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis. Stress ...

https://accounts.public.ce.basespace.illumina.com/b/search/article.nb?id=35935594

Cyclic-AMP-dependent protein kinase and a transmembrane tyrosine phosphatase in Caenorhabditis elegans: Structure, function and ... Protein kinases and protein phosphatases are central components of signal transduction pathways. This thesis characterized two ... of cAMP-dependent protein kinase (cAMP-PK) and a tyrosine phosphatase (PTPase).;C. elegans has a single gene and mRNA encoding ... The remaining residues connecting the FN III and the catalytic domain are not related to other proteins in various data bases. ...

https://repository.yu.edu/handle/20.500.12202/3339

Inhibition of protein tyrosine phosphatase 1B by ursane-type triterpenes isolated from Symplocos paniculata. ... Dive into the research topics of Inhibition of protein tyrosine phosphatase 1B by ursane-type triterpenes isolated from ...

https://pure.korea.ac.kr/en/publications/inhibition-of-protein-tyrosine-phosphatase-1b-by-ursane-type-trit/fingerprints/?sortBy=alphabetically

Oxidation state of protein tyrosine phosphatase 1B Coordinates. PDB Format Method. X-RAY DIFFRACTION 2.20 Å. Oligo State. ... van Montfort, R.L. et al., Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature (2003) ... Oxidation state of protein tyrosine phosphatase 1B ... PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1: A. SMTL:PDB ...

https://swissmodel.expasy.org/templates/1oev

Cocaine reward is reduced by decreased expression of receptor-type protein tyrosine phosphatase D (PTPRD) and by a novel PTPRD ... Receptor-type protein tyrosine phosphatase D (PTPRD) is a neuronal cell-adhesion molecule that has been associated with ... Receptor-type protein tyrosine phosphatase D (PTPRD) is a neuronal cell-adhesion molecule/synaptic specifier that has been ... abstract = {Receptor-type protein tyrosine phosphatase D (PTPRD) is a neuronal cell-adhesion molecule/synaptic specifier that ...

https://irp.nida.nih.gov/hot-off-the-press-october-25-2018/

T2 - Deletion of protein tyrosine phosphatase 1B (PTP1B) enhances endothelial cyclooxygenase 2 expression and protects mice ... Correction: Deletion of protein tyrosine phosphatase 1B (PTP1B) enhances endothelial cyclooxygenase 2 expression and protects ... Correction: Deletion of protein tyrosine phosphatase 1B (PTP1B) enhances endothelial cyclooxygenase 2 expression and protects ... Correction : Deletion of protein tyrosine phosphatase 1B (PTP1B) enhances endothelial cyclooxygenase 2 expression and protects ...

https://augusta.elsevierpure.com/en/publications/correction-deletion-of-protein-tyrosine-phosphatase-1b-ptp1b-enha

... protein kinase cAMP-dependent (PKA)/adenosine monophosphate activated protein kinase (AMPK) pathway, against high-fat-diet- ... and mitogen-activated protein kinases (MAPKs)/c-jun N-terminal kinase (JNK) signaling pathways involved in pro-inflammatory ... In skeletal muscles of EHP-treated animals, mRNA and protein levels of protein tyrosine phosphatase 1B (PTP1B), a factor known ... protein tyrosine phosphatase 1B. References. *Karczewski, J.; Śledzińska, E.; Baturo, A.; Jończyk, I.; Maleszko, A.; Samborski ...

https://www.mdpi.com/1422-0067/21/21/8108

SHP1 Protein Tyrosine Phosphatase. Protein Tyrosine Phosphatase, Non-Receptor Type 6. Thioredoxin Reductase (NADPH). ... Phosphoprotein Phosphatases. Protein-Tyrosine-Phosphatase. Protein Tyrosine Phosphatases. Rhodopsin Kinase. G-Protein-Coupled ... Protein Isoprenylation. Protein Prenylation. G09 - Circulatory and Respiratory Physiology. Hemodynamic Processes. Hemodynamics ... Ca(2+)-Calmodulin Dependent Protein Kinase. Calcium-Calmodulin-Dependent Protein Kinases. Cholesterol Esterase. Sterol Esterase ...

https://decs.bvs.br/I/rep_i2008.htm

Protein Tyrosine Phosphatases- Potential Roles in Disease. Andersen, H.S., et al., J. Med. Chem., 45, 4443-4459 (2002). 90. ... Protein Purification and Detection Tools. st ed 0. 00 1 un it 0. 00 15 u ni t 0. 00 2 un it 0. 00 25 u ni t 0. 00 3 un it 0. 00 ...

https://www.sigmaaldrich.com/US/en/search/598-55-0?focus=documents&page=1&perpage=30&sort=relevance&term=598-55-0&type=site_content

PDCD1 protein, human * Programmed Cell Death 1 Receptor * PTPN11 protein, human * Protein Tyrosine Phosphatase, Non-Receptor ... and the src homology 2 domain-containing tyrosine phosphatase 2 gene (PTPN11) and susceptibility to IBD. ...

https://pubmed.ncbi.nlm.nih.gov/19160029/?dopt=Abstract

The tyrosine phosphatase PTPN14 (Pez) inhibits metastasis by altering protein trafficking. Science signaling 8, https://doi.org ... Eto, M., Kirkbride, J. A. & Brautigan, D. L. Assembly of MYPT1 with protein phosphatase-1 in fibroblasts redirects localization ... Fibroblast activation protein expression by stromal cells and tumor-associated macrophages in human breast cancer. Hum Pathol ... The Inositol Polyphosphate 5-Phosphatase PIPP Regulates AKT1-Dependent Breast Cancer Growth and Metastasis. Cancer Cell 28, 155 ...

https://www.nature.com/articles/s41598-017-17177-5?error=cookies_not_supported

Target-specific control of protein tyrosine phosphatase activity. Protein tyrosine phosphatases (PTPs) are enzymes that help to ... In a project that focuses on a different PTP, we seek to discover allosteric inhibitors of T-cell protein phosphatase (TCPTP). ... send cellular messages by enzymatically removing phosphate groups from other proteins. When cellular phosphate removal goes ...

https://www.amherst.edu/people/facstaff/acbishop/research_interests

Role of protein phosphatases in the loss of KCC2 tyrosine phosphorylation. A loss of tyrosine phosphorylation of KCC2 may ... and the tyrosine phosphatase inhibitor Na3VO4 (100 μm), resulting in an increased proportion of tyrosine-phosphorylated KCC2 ( ... and other possible tyrosine phosphatase blockers (e.g., phenylarsine oxide and Na2MoO4), but not a serine-threonine phosphatase ... a specific inhibitor of tyrosine phosphatases (Swarup et al., 1982), on the oxidative stress-induced change in KCC2 tyrosine ...

https://www.jneurosci.org/content/27/7/1642

PTK, protein-tyrosine kinase; PTP, protein-tyrosine phosphatase; RPTK, receptor PTK; RPTP, receptor- like PTP; RSV, Rous ... Ornithine decarboxylase-induced cellular transformation: the involvement of protein tyrosine kinase(s) and pp130 ... View article titled, Ornithine decarboxylase-induced cellular transformation: the involvement of protein tyrosine kinase(s) and ... the involvement of protein tyrosine kinase(s) and pp130 ... the involvement of protein tyrosine kinase(s) and pp I 30 Erkki ...

https://portlandpress.com/biochemsoctrans/search-results?qb=%7B%22Keywords1%22:%22RSV%2C+Rous+sarcoma+virus%22%7D

Anatomy24

Organisms11

Diseases3

Chemicals and Drugs150

Analytical, Diagnostic and Therapeutic Techniques and Equipment19

Phenomena and Processes45

Disciplines and Occupations1

Information Science3

Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. (1/4408)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (2/4408)

Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway. (3/4408)

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor. (4/4408)

gp49B1 inhibits IgE-initiated mast cell activation through both immunoreceptor tyrosine-based inhibitory motifs, recruitment of src homology 2 domain-containing phosphatase-1, and suppression of early and late calcium mobilization. (5/4408)

Involvement of tyrosine phosphorylation in HMG-CoA reductase inhibitor-induced cell death in L6 myoblasts. (6/4408)

Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (7/4408)

Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. (8/4408)

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Protein Tyrosine Phosphatases

Protein Tyrosine Phosphatase, Non-Receptor Type 1

Receptor-Like Protein Tyrosine Phosphatases, Class 2

Protein Tyrosine Phosphatase, Non-Receptor Type 11

Protein Tyrosine Phosphatase, Non-Receptor Type 2

Protein Tyrosine Phosphatase, Non-Receptor Type 6

Tyrosine

Receptor-Like Protein Tyrosine Phosphatases, Class 3

Receptor-Like Protein Tyrosine Phosphatases, Class 4

Protein Tyrosine Phosphatases, Non-Receptor

Receptor-Like Protein Tyrosine Phosphatases, Class 5

Receptor-Like Protein Tyrosine Phosphatases

Protein Tyrosine Phosphatase, Non-Receptor Type 12

SH2 Domain-Containing Protein Tyrosine Phosphatases

Phosphorylation

Protein Tyrosine Phosphatase, Non-Receptor Type 13

Vanadates

Receptor-Like Protein Tyrosine Phosphatases, Class 7

Phosphoprotein Phosphatases

Protein Tyrosine Phosphatase, Non-Receptor Type 22

Receptor-Like Protein Tyrosine Phosphatases, Class 8

Signal Transduction

Protein Tyrosine Phosphatase, Non-Receptor Type 3

Phosphotyrosine

Protein-Tyrosine Kinases

Protein Phosphatase 2

Intracellular Signaling Peptides and Proteins

Protein Phosphatase 1

Molecular Sequence Data

Amino Acid Sequence

Antigens, CD45

Acid Phosphatase

src Homology Domains

Enzyme Inhibitors

Enzyme Activation

Cell Line

src-Family Kinases

Protein Tyrosine Phosphatase, Non-Receptor Type 4

Lymphocyte Specific Protein Tyrosine Kinase p56(lck)

Phosphoric Monoester Hydrolases

Phosphoproteins

Genistein

Cells, Cultured

Substrate Specificity

Protein Binding

Proto-Oncogene Proteins pp60(c-src)

Kinetics

Dual-Specificity Phosphatases

Base Sequence

Recombinant Fusion Proteins

Proto-Oncogene Proteins c-fyn

Transfection

Catalytic Domain

Mutation

Protein Structure, Tertiary

Tumor Cells, Cultured

Proto-Oncogene Proteins

Sequence Homology, Amino Acid

Recombinant Proteins

Binding Sites

Glucose-6-Phosphatase

Isoenzymes

Cloning, Molecular

Tyrosine 3-Monooxygenase

Precipitin Tests

Receptor Protein-Tyrosine Kinases

Blotting, Western

cdc25 Phosphatases

Receptors, Cell Surface

Mitogen-Activated Protein Kinases

COS Cells

Gene Expression Regulation, Enzymologic

Okadaic Acid

Adaptor Proteins, Signal Transducing

3T3 Cells

Membrane Proteins

Tyrphostins

Receptor, Insulin

RNA, Messenger

Mice, Knockout