Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
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The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytesCsk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcSH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchangeMolecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein.Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1Phosphorylation of c-Crk II on the negative regulatory Tyr222 mediates nerve growth factor-induced cell spreading and morphogenesisThe kinase-deficient Src acts as a suppressor of the Abl kinase for Cbl phosphorylationRegulation of the Src protein tyrosine kinase.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.Binding 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.Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias.Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins.Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrixTransformation 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).Src regulated by C-terminal phosphorylation is monomericKinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance.Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.Requirement of phosphatidylinositol-3 kinase modification for its association with p60src.Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity.pp60v-src transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain.Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity.Focal adhesion as a signal transduction organelle.New insights into protein-tyrosine kinase receptor signaling complexes.A Bcl-2-related gene is activated in avian cells transformed by the Rous sarcoma virus.CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.Constitutive activation of STAT5 by a point mutation in the SH2 domain.A new monoclonal antibody which selectively recognizes the active form of Src tyrosine kinase.Rapid and efficient purification of Src homology 2 domain-containing proteins: Fyn, Csk and phosphatidylinositol 3-kinase p85.
P2860
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P2860
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@ast
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@en
type
label
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@ast
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@en
prefLabel
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@ast
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@en
P2093
P2860
P356
P1476
Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.
@en
P2093
P2860
P304
P356
10.1128/MCB.10.6.2855
P407
P577
1990-06-01T00:00:00Z