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 changes
about
Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cellsMultiple forms of p55PIK, a regulatory subunit of phosphoinositide 3-kinase, are generated by alternative initiation of translationAutophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60srcCloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85Negative regulation of PI 3-kinase by Ruk, a novel adaptor proteinThe catalytic subunit of phosphatidylinositol 3-kinase is a substrate for the activated platelet-derived growth factor receptor, but not for middle-T antigen-pp60c-src complexesWortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reactionsrc-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo.Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-srcBMP2-induced chemotaxis requires PI3K p55γ/p110α-dependent phosphatidylinositol (3,4,5)-triphosphate production and LL5β recruitment at the cytocortexRhoB regulates PDGFR-beta trafficking and signaling in vascular smooth muscle cells.Stability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemiaConformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides.Platelet-derived growth factor-dependent activation of phosphatidylinositol 3-kinase is regulated by receptor binding of SH2-domain-containing proteins which influence Ras activitySpecific activation of p85-p110 phosphatidylinositol 3'-kinase stimulates DNA synthesis by ras- and p70 S6 kinase-dependent pathways.Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits.Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach5,8-Dimethoxy-2-Nonylamino-Naphthalene-1,4-Dione Inhibits Vascular Smooth Muscle Cell Proliferation by Blocking Autophosphorylation of PDGF-Receptor β.The phosphoinositide 3-kinase pathway in human cancer: genetic alterations and therapeutic implications.Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras.PI 3-kinase: structural and functional analysis of intersubunit interactions.PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity.Platelet-derived growth factor-induced phosphatidylinositol 3-kinase activation mediates actin rearrangements in fibroblasts.A novel recognition motif for phosphatidylinositol 3-kinase binding mediates its association with the hepatocyte growth factor/scatter factor receptor.Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses.Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation.Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.Computational models of tandem SRC homology 2 domain interactions and application to phosphoinositide 3-kinase.
P2860
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P2860
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 changes
description
1992 nî lūn-bûn
@nan
1992 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի դեկտեմբերին 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
Interaction of the p85 subunit ...... ysis of conformational changes
@ast
Interaction of the p85 subunit ...... ysis of conformational changes
@en
Interaction of the p85 subunit ...... ysis of conformational changes
@en-gb
Interaction of the p85 subunit ...... ysis of conformational changes
@nl
type
label
Interaction of the p85 subunit ...... ysis of conformational changes
@ast
Interaction of the p85 subunit ...... ysis of conformational changes
@en
Interaction of the p85 subunit ...... ysis of conformational changes
@en-gb
Interaction of the p85 subunit ...... ysis of conformational changes
@nl
prefLabel
Interaction of the p85 subunit ...... ysis of conformational changes
@ast
Interaction of the p85 subunit ...... ysis of conformational changes
@en
Interaction of the p85 subunit ...... ysis of conformational changes
@en-gb
Interaction of the p85 subunit ...... ysis of conformational changes
@nl
P2093
P2860
P1433
P1476
Interaction of the p85 subunit ...... ysis of conformational changes
@en
P2093
B Wroblowski
G Panayotou
M D Waterfield
M Federwisch
P2860
P304
P407
P50
P577
1992-12-01T00:00:00Z