Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor.
about
GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunitA mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulatorsPhosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivoRaf-1 physically interacts with Rb and regulates its function: a link between mitogenic signaling and cell cycle regulationExpression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression systemMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsSerine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activationRb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signalsTyrosine phosphorylation of the proto-oncoprotein Raf-1 is regulated by Raf-1 itself and the phosphatase Cdc25AMonoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activityIdentification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrewEps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signalsInteractions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptorA DNA-activated protein kinase from HeLa cell nucleiAn Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinasesPICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid systemOverexpression of c-src enhances beta-adrenergic-induced cAMP accumulationThe 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 complexesThe membrane IgM-associated proteins MB-1 and Ig-beta are sufficient to promote surface expression of a partially functional B-cell antigen receptor in a nonlymphoid cell lineSequence requirements for binding of Src family tyrosine kinases to activated growth factor receptorsProtein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating proteinMultiple cDNAs encoding the esk kinase predict transmembrane and intracellular enzyme isoformsGrowth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domainRas recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylationTyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptorThe erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potencyDifferential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins.A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo.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.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.Raf-1 is a potential substrate for mitogen-activated protein kinase in vivo.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.Requirement for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytesInhibition of platelet-derived growth factor- and epidermal growth factor-mediated mitogenesis and signaling in 3T3 cells expressing delta Raf-1:ER, an estradiol-regulated form of Raf-1.Interleukin 2- and polyomavirus middle T antigen-induced modification of phosphatidylinositol 3-kinase activity in activated T lymphocytes.Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complexRas-induced activation of Raf-1 is dependent on tyrosine phosphorylationBoth p21ras and pp60v-src are required, but neither alone is sufficient, to activate the Raf-1 kinaseMolecular organization of the human Raf-1 promoter region.
P2860
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P2860
Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor.
description
1989 nî lūn-bûn
@nan
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
1989年论文
@zh
1989年论文
@zh-cn
name
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@en
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@nl
type
label
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@en
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@nl
prefLabel
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@en
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@nl
P2093
P1433
P1476
Direct activation of the serin ...... ion by the PDGF beta-receptor.
@en
P2093
Escobedo JA
Morrison DK
Roberts TM
Williams LT
P304
P356
10.1016/0092-8674(89)90100-1
P407
P577
1989-08-01T00:00:00Z