SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
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A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cellsIdentification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gammaHierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptorAkt binds to and phosphorylates phospholipase C-gamma1 in response to epidermal growth factorThe phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptorActivation of Src family kinases by colony stimulating factor-1, and their association with its receptorSubstrate specificity of the protein tyrosine phosphatasesIdentification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinasesTwo signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptorPhospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for SykPLC-gamma1 and Rac1 coregulate EGF-induced cytoskeleton remodeling and cell migrationPhospholipase Cgamma/diacylglycerol-dependent activation of beta2-chimaerin restricts EGF-induced Rac signalingThe SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signallingSH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchangeIdentification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophagesNucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicitySH2 domain-mediated interaction of inhibitory protein tyrosine kinase Csk with protein tyrosine phosphatase-HSCFThe SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatmentThe SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptorsMutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinaseTyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activationA comprehensive pathway map of epidermal growth factor receptor signalingPhosphotyrosine interactome of the ErbB-receptor kinase familyAssociation and colocalization of Eps15 with adaptor protein-2 and clathrinHost nucleotide polymorphism in hepatitis B virus-associated hepatocellular carcinomaEGFR ligands exhibit functional differences in models of paracrine and autocrine signalingInhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR SignalingBLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteinsThe phospholipase C isozymes and their regulationA kinase cascade leading to Rab11-FIP5 controls transcytosis of the polymeric immunoglobulin receptorCaveolin-1 Dependent Endocytosis Enhances the Chemosensitivity of HER-2 Positive Breast Cancer Cells to Trastuzumab Emtansine (T-DM1)Phosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase C gamma 1Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and VavThe ErbB signaling network: receptor heterodimerization in development and cancerFunctional independence and interdependence of the Src homology domains of phospholipase C-gamma1 in B-cell receptor signal transduction.Requirement for phospholipase C-gamma1 enzymatic activity in growth factor-induced mitogenesisRegulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.A 31-amino-acid N-terminal extension regulates c-Crk binding to tyrosine-phosphorylated proteins.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.
P2860
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P2860
SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
description
1992 nî lūn-bûn
@nan
1992 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@ast
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@en
type
label
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@ast
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@en
prefLabel
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@ast
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@en
P2093
P2860
P1433
P1476
SH2 domains prevent tyrosine d ...... ains of phospholipase C gamma.
@en
P2093
B Margolis
E H Fischer
J Schlessinger
W H Burgess
P2860
P304
P407
P577
1992-02-01T00:00:00Z