Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
about
The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contactsActivation of the c-Jun N-terminal kinase pathway by a novel protein kinase related to human germinal center kinase14-3-3zeta interacts with the alpha-chain of human interleukin 9 receptorInsulin regulates the dynamic balance between Ras and Rap1 signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes.Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activationTyrosine phosphorylation of the proto-oncoprotein Raf-1 is regulated by Raf-1 itself and the phosphatase Cdc25Ap50(cdc37) acting in concert with Hsp90 is required for Raf-1 functionActivation of phosphoinositide 3-kinase by interaction with Ras and by point mutationHuman immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2APhosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signalingRaf activation is regulated by tyrosine 510 phosphorylation in DrosophilaRaf-interactome in tuning the complexity and diversity of Raf function.Regulation of Raf through phosphorylation and N terminus-C terminus interactionProtein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions14-3-3 proteins interact with specific MEK kinasesIdentification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alphaMEK kinase activity is not necessary for Raf-1 function.The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domainIdentification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK bindingThe 14-3-3ζ protein binds to the cell adhesion molecule L1, promotes L1 phosphorylation by CKII and influences L1-dependent neurite outgrowthA different function for a critical tryptophan in c-Raf and Hck.Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylationInactivation of raf-1 by a protein-tyrosine phosphatase stimulated by GTP and reconstituted by Galphai/o subunits.Activation of a protein tyrosine phosphatase and inactivation of Raf-1 by somatostatinThe cytoplasmic domain of the platelet glycoprotein Ibalpha is phosphorylated at serine 609.14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor.Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.Platelet-derived growth factor activates mitogen-activated protein kinase in isolated caveolae.Multiple signaling pathways of the insulin-like growth factor 1 receptor in protection from apoptosis.Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells.Overexpression of transforming growth factor β1 in malignant prostate cells is partly caused by a runaway of TGF-β1 auto-induction mediated through a defective recruitment of protein phosphatase 2A by TGF-β type I receptor.Serum- and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf.Ras-MAP kinase signaling pathways and control of cell proliferation: relevance to cancer therapy.A PP2A regulatory subunit positively regulates Ras-mediated signaling during Caenorhabditis elegans vulval induction14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide.14-3-3 proteins: a number of functions for a numbered protein.Raf kinases: function, regulation and role in human cancer.Regulation of Raf-1-dependent signaling during early Xenopus development.Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells.
P2860
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P2860
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@ast
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@en
type
label
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@ast
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@en
prefLabel
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@ast
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@en
P2093
P356
P1433
P1476
Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
@en
P2093
P304
P356
10.1126/SCIENCE.7604263
P407
P577
1995-06-01T00:00:00Z