Tyr527 is phosphorylated in pp60c-src: implications for regulation.
about
ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic originIdentification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cellsMeasurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisalA tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1Characterization of cDNA clones for the human c-yes geneMouse disabled (mDab1): a Src binding protein implicated in neuronal developmentHuman proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligandThe role of Src in solid tumorsThe yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lckPrimary structure of the human fgr proto-oncogene product p55c-fgrRegulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contextsThe Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and diseaseThe hunting of the SrcRegulation of SRC family kinases in human cancerscDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain'Srcasm: a novel Src activating and signaling moleculeDual phosphorylations underlie modulation of unitary KCNQ K(+) channels by Src tyrosine kinaseGain control of N-methyl-D-aspartate receptor activity by receptor-like protein tyrosine phosphatase alphaMolecular and biochemical characterization of the human trk proto-oncogeneSH3 domain of c-Src governs its dynamics at focal adhesions and the cell membrane.Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytesHerpes simplex virus requires VP11/12 to induce phosphorylation of the activation loop tyrosine (Y394) of the Src family kinase Lck in T lymphocytes.Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.An electrostatic network and long-range regulation of Src kinasesConformational basis for SH2-Tyr(P)527 binding in Src inactivation.C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases.The distinct capacity of Fyn and Lck to phosphorylate Sam68 in T cells is essentially governed by SH3/SH2-catalytic domain linker interactions.The kinase-deficient Src acts as a suppressor of the Abl kinase for Cbl phosphorylationPolyomavirus middle-T antigen associates with the kinase domain of Src-related tyrosine kinases.Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.Activation of c-Src in cells bearing v-Crk and its suppression by CskSelective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-srcSite-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Src homology domain 2-containing protein-tyrosine phosphatase-1 (SHP-1) binds and dephosphorylates G(alpha)-interacting, vesicle-associated protein (GIV)/Girdin and attenuates the GIV-phosphatidylinositol 3-kinase (PI3K)-Akt signaling pathway.Src family tyrosine kinase regulates intracellular pH in cardiomyocytesActivation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus.
P2860
Q22008016-536F6121-A34E-4628-A4FB-4567CC454C39Q24298621-51E6623A-1E84-4BE8-A328-97665B16F14FQ24299170-87F7FE13-75B5-44F8-8578-4483C9B28800Q24306895-C0041119-B845-4F6B-BF7D-6EED08719DEAQ24310428-FF10E5B3-4BE1-4EF4-A7F9-8F8DD0683257Q24315067-3216B143-E89C-498F-BB1C-82B56AE4DDDCQ24532070-C4EABBB9-1832-474A-B663-63F4EFC13EFAQ24555963-D78EF4E9-4A22-4A24-815C-7A1D91FF4E6BQ24616659-AF6CE4D8-6CE2-4761-BF9E-0A68F9BA35E6Q24629004-6A43E783-982F-4C1D-8C69-82E9B70D8BADQ24632830-8CCFA936-106A-4737-89BE-7CFB2C774BC7Q24652254-1DC562F0-52AD-4082-8603-C599E084896FQ24677033-4536EDC5-839A-4427-8C94-574E843F33AFQ28199081-10EB892D-A955-42E6-A432-447D711B849BQ28243770-962F1499-536F-4BAA-B3DA-6E5DB35FD7C9Q28261183-DF43DDA4-FF65-4994-BF58-0B35701DBD66Q28280523-79700805-248E-489E-A731-01ACBF00C8B8Q28505622-3691EB74-40F4-4FE4-A5E6-025FDBC9076CQ28575228-FFFB68B1-388E-40E7-AECE-4BD84FAA5A62Q28575902-41FE3459-F41B-4831-B01A-A88A2893EE62Q28854584-9E92E455-8C93-4F83-BC76-862DC7FD7BA5Q30009127-F71B7FA6-1F72-417C-BADB-823CFA83FE9DQ30010240-8EC5A34A-9FE2-42FB-8461-99F0CB3B19DAQ30157107-597AE634-79BE-4454-A259-E20AF417B322Q30157342-88798D15-B538-40AE-B1AC-E58A646A277AQ30157622-38A99C88-D0BF-454B-A28E-0EC1FB1C97DCQ30159758-0DA31F36-A14B-4DE8-8667-6F9670A8789BQ30160101-DD9A32F3-9A6D-4435-9F8D-742CED34042AQ30165155-943CDB16-88D3-4120-B50B-63E6F09AD034Q30169010-8814903D-8FB8-41B8-8091-66CB0CA8FB2DQ30177032-D37D4283-CE3E-4F40-AE58-7B8590252225Q30194623-89E34515-00BB-4018-BB22-0923E7812D43Q30194700-FDB82DB5-6C7E-4EF3-8B3B-5E2C5350BA6BQ30194837-671D05F8-C8C3-499B-BAC4-F1EB13519B28Q30195267-EC18F49B-B146-41B0-845B-BABAD1B02EBFQ30195559-1F8D328D-27D8-4045-B814-65E6C535732FQ30195875-E44237FD-8D9F-47DD-8EA9-44343A33F345Q30424937-3FAB542D-EB39-4CB7-A77D-10AC094F1EB0Q30442099-8305AC85-CA27-4F36-AD4F-74DBCE0D1E16Q30448511-DFCDD1F7-B7E5-4EE0-9987-09D169283CA0
P2860
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
description
1986 nî lūn-bûn
@nan
1986 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի մարտին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@ast
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@en
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@nl
type
label
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@ast
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@en
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@nl
prefLabel
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@ast
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@en
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@nl
P2093
P356
P1433
P1476
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
@en
P2093
P304
P356
10.1126/SCIENCE.2420005
P407
P577
1986-03-01T00:00:00Z