Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.
about
Soluble Jagged 1 represses the function of its transmembrane form to induce the formation of the Src-dependent chord-like phenotypeModulation of protein translation by Nck-1.Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profilingCsk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcAlpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testesMutational analysis of the STAT6 SH2 domainProtein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulinSpecific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activationDifferential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signalsProtein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptorPhospho-tyrosine dependent protein-protein interaction networkThe SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signallingPhosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal regionThe human GRB2 and Drosophila Drk genes can functionally replace the Caenorhabditis elegans cell signaling gene sem-5.Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changesDirect interaction of Jak1 and v-Abl is required for v-Abl-induced activation of STATs and proliferationSocs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferationA limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interactionThe PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activityGenetic analysis of a phosphatidylinositol 3-kinase SH2 domain reveals determinants of specificityMutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinaseDirect association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1Differential effects of B cell receptor and B cell receptor-FcgammaRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domainSuperbinder SH2 domains act as antagonists of cell signalingAssociation of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partnerCIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signalingConservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domainsA spectrum of mutations in SH2D1A that causes X-linked lymphoproliferative disease and other Epstein-Barr virus-associated illnessesNon-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinaseProline-rich sequences that bind to Src homology 3 domains with individual specificitiesp150TSP, a conserved nuclear phosphoprotein that contains multiple tetratricopeptide repeats and binds specifically to SH2 domainsThe cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene productsIdentification of the rat adapter Grb14 as an inhibitor of insulin actionsMutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction.Interaction of p72syk with the gamma and beta subunits of the high-affinity receptor for immunoglobulin E, Fc epsilon RIDifferential activation of acute phase response factor/Stat3 and Stat1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130. II. Src homology SH2 domains define the specificity of stat factor activationThe role of individual SH2 domains in mediating association of phospholipase C-gamma1 with the activated EGF receptor
P2860
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P2860
Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Point mutations in the abl SH2 ...... transforming activity in vivo.
@ast
Point mutations in the abl SH2 ...... transforming activity in vivo.
@en
type
label
Point mutations in the abl SH2 ...... transforming activity in vivo.
@ast
Point mutations in the abl SH2 ...... transforming activity in vivo.
@en
prefLabel
Point mutations in the abl SH2 ...... transforming activity in vivo.
@ast
Point mutations in the abl SH2 ...... transforming activity in vivo.
@en
P2093
P2860
P356
P1476
Point mutations in the abl SH2 ...... transforming activity in vivo.
@en
P2093
D Baltimore
P K Jackson
R A Van Etten
P2860
P304
P356
10.1128/MCB.12.2.609
P407
P577
1992-02-01T00:00:00Z