The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.
about
A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.CMS: an adapter molecule involved in cytoskeletal rearrangementsPKC phosphorylation increases the ability of AFAP-110 to cross-link action filamentsSrc kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domainCsk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcIntroduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinasesTransformation suppression by protein tyrosine phosphatase 1B requires a functional SH3 ligandA novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent mannerMultiple SH2-mediated interactions in v-src-transformed cells.Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domainsAssociation of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.Hyaluronan and the hyaluronan receptor RHAMM promote focal adhesion turnover and transient tyrosine kinase activityCortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortexT cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T)The molecular effect of metastasis suppressors on Src signaling and tumorigenesis: new therapeutic targetsNSP-CAS Protein Complexes: Emerging Signaling Modules in CancerSrc kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.Crystallization of the SH2-binding site of p130Cas in complex with Lck, a Src-family kinase.Regulation of c-SRC activity and function by the adapter protein CASCas mediates transcriptional activation of the serum response element by Src.The role of the Src homology domains in morphological transformation by v-srcGi-mediated activation of the Ras/MAP kinase pathway involves a 100 kDa tyrosine-phosphorylated Grb2 SH3 binding protein, but not Src nor ShcPhysical 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.Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylationThe Src-family kinase, Fyn, regulates the activation of phosphatidylinositol 3-kinase in an interleukin 2-responsive T cell line.Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK.Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate.Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblastsThe SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels.Host range mutants of v-src: alterations in kinase activity and substrate interactionsEffects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor.Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology.Identification and characterization of a novel cytoskeleton-associated pp60src substrate.Regulation of tetradecanoyl phorbol acetate-induced responses in NIH 3T3 cells by GAP, the GTPase-activating protein associated with p21c-ras.Src phosphorylates Cas on tyrosine 253 to promote migration of transformed cellsCaspase-mediated cleavage of p130cas in etoposide-induced apoptotic Rat-1 cells.Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
P2860
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P2860
The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.
description
1991 nî lūn-bûn
@nan
1991 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@ast
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@en
type
label
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@ast
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@en
prefLabel
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@ast
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@en
P2093
P2860
P1433
P1476
The SH2 and SH3 domains of pp6 ...... ylated proteins p130 and p110.
@en
P2093
A B Reynolds
J T Parsons
S B Kanner
P2860
P304
P407
P577
1991-07-01T00:00:00Z