Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.
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Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell linesFunctional interaction between c-Src and its mitotic target, Sam 68Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteinsMutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactionsA single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef proteinOverexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreadingAssociation of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loopContribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.The hunting of the SrcProtein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesionThe Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, HckThreonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activityThe Fyn tyrosine kinase binds Irs-1 and forms a distinct signaling complex during insulin stimulationp130cas but not paxillin is essential for Caco-2 intestinal epithelial cell spreading and migration on collagen IVThe N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src.Divergent modulation of Src-family kinase regulatory interactions with ATP-competitive inhibitors.C-terminal Src kinase-homologous kinase (CHK), a unique inhibitor inactivating multiple active conformations of Src family tyrosine kinases.HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction.Activation of the Src family kinase Hck without SH3-linker release.c-Src signaling induced by the adapters Sin and Cas is mediated by Rap1 GTPase.Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand.SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts.Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue.The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src.SH2- and SH3-mediated interactions between focal adhesion kinase and Src.Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling.The Src SH3 domain is required for DNA synthesis induced by platelet-derived growth factor and epidermal growth factor.Regulation of the Src protein tyrosine kinase.A novel mammalian myosin I from rat with an SH3 domain localizes to Con A-inducible, F-actin-rich structures at cell-cell contacts.Structure-function relationships in Src family and related protein tyrosine kinases.SH3 domains specifically regulate kinase activity of expressed Src family proteins.Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fynCsk suppression of Src involves movement of Csk to sites of Src activity.Aberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae.A functional screen in yeast for regulators and antagonizers of heterologous protein tyrosine kinases.
P2860
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P2860
Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.
description
1993 nî lūn-bûn
@nan
1993 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@ast
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@en
type
label
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@ast
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@en
prefLabel
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@ast
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@en
P2093
P2860
P356
P1476
Suppression of c-Src activity ...... with Saccharomyces cerevisiae.
@en
P2093
P2860
P304
P356
10.1128/MCB.13.9.5290
P407
P577
1993-09-01T00:00:00Z