Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability
about
Multiple SH2-mediated interactions in v-src-transformed cells.Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinaseDisease specificity of kinase domains: the src-encoded catalytic domain converts erbB into a sarcoma oncogeneBinding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase.Activated lck tyrosine protein kinase stimulates antigen-independent interleukin-2 production in T cells.Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.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.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins.Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein.Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527).Differential modulation of plasminogen activator gene expression by oncogene-encoded protein tyrosine kinasesThe sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-srcStable association of activated pp60src with two tyrosine-phosphorylated cellular proteinspp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-srcSrc homology region 2 domains direct protein-protein interactions in signal transduction.Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function.Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinasesSecondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.Transformation of chicken embryo fibroblast cells by avian retroviruses containing the human Fyn gene and its mutated genes.
P2860
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P2860
Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability
description
1989 nî lūn-bûn
@nan
1989 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Deletions and insertions withi ...... nd modulate membrane stability
@ast
Deletions and insertions withi ...... nd modulate membrane stability
@en
type
label
Deletions and insertions withi ...... nd modulate membrane stability
@ast
Deletions and insertions withi ...... nd modulate membrane stability
@en
prefLabel
Deletions and insertions withi ...... nd modulate membrane stability
@ast
Deletions and insertions withi ...... nd modulate membrane stability
@en
P2860
P1433
P1476
Deletions and insertions withi ...... nd modulate membrane stability
@en
P2093
P2860
P304
P577
1989-01-01T00:00:00Z