A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
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Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylationMitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylationThe rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residueCatalytically active membrane-distal phosphatase domain of receptor protein-tyrosine phosphatase alpha is required for Src activationActivation of Src and transformation by an RPTPα splice mutant found in human tumoursSynapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and FynDok-R mediates attenuation of epidermal growth factor-dependent mitogen-activated protein kinase and Akt activation through processive recruitment of c-Src and Csk.Dimerization of receptor protein-tyrosine phosphatase alpha in living cellsSRC-family tyrosine kinases in oogenesis, oocyte maturation and fertilization: an evolutionary perspectiveDiverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine PhosphatasesTyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factorsMeeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalphaRegulation of SRC family kinases in human cancersTwo mechanisms activate PTPalpha during mitosisSRC kinase regulation in progressively invasive cancerGain control of N-methyl-D-aspartate receptor activity by receptor-like protein tyrosine phosphatase alphaEmbryonal Fyn-associated substrate (EFS) and CASS4: The lesser-known CAS protein family membersThe Gβγ-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocationRole of protein tyrosine phosphatases in cancerThe regulation of N-methyl-D-aspartate receptors by Src kinase.Association of tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor.A TRIF-independent branch of TLR3 signaling.Calmodulin binds to and inhibits the activity of the membrane distal catalytic domain of receptor protein-tyrosine phosphatase alpha.Initiation factor eIF2-independent mode of c-Src mRNA translation occurs via an internal ribosome entry site.Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.Inhibition of Ser/Thr phosphatases induces capacitation-associated signaling in the presence of Src kinase inhibitors.Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growthImplications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle.Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface.Importance of protein-tyrosine phosphatase-alpha catalytic domains for interactions with SHP-2 and interleukin-1-induced matrix metalloproteinase-3 expressionSelected glimpses into the activation and function of Src kinase.c-SRC mediates neurite outgrowth through recruitment of Crk to the scaffolding protein Sin/Efs without altering the kinetics of ERK activation.An update on dual Src/Abl inhibitors.Regulation of endothelial permeability by Src kinase signaling: vascular leakage versus transcellular transport of drugs and macromolecules.Comprehensive binary interaction mapping of SH2 domains via fluorescence polarization reveals novel functional diversification of ErbB receptors.Striatal-enriched protein tyrosine phosphatase regulates the PTPα/Fyn signaling pathwayHistone deacetylase 3 localizes to the plasma membrane and is a substrate of Src.FRET analysis of protein tyrosine kinase c-Src activation mediated via aryl hydrocarbon receptorFibronectin rigidity response through Fyn and p130Cas recruitment to the leading edgeSrc SH2 arginine 175 is required for cell motility: specific focal adhesion kinase targeting and focal adhesion assembly function
P2860
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P2860
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
description
2000 nî lūn-bûn
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2000 թուականի Մարտին հրատարակուած գիտական յօդուած
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2000 թվականի մարտին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
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2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@ast
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en-gb
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@nl
type
label
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@ast
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en-gb
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@nl
prefLabel
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@ast
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en-gb
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@nl
P2093
P2860
P3181
P356
P1433
P1476
A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
@en
P2093
D Shalloway
R J Resnick
P2860
P304
P3181
P356
10.1093/EMBOJ/19.5.964
P407
P577
2000-03-01T00:00:00Z