Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells
about
Identification of a mammalian gene structurally and functionally related to the CDC25 gene of Saccharomyces cerevisiaeAsh/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGFBcr-Abl oncoproteins bind directly to activators of the Ras signalling pathwayThe SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signallingAstrocyte elevated gene-1 activates cell survival pathways through PI3K-Akt signalingActivation of extracellular signal-regulated kinase, ERK2, by p21ras oncoproteinp21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating proteinMolecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein.Tyr-716 in the platelet-derived growth factor beta-receptor kinase insert is involved in GRB2 binding and Ras activationTyrosine 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 activationAssociation of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1Assembly of cyclin D-dependent kinase and titration of p27Kip1 regulated by mitogen-activated protein kinase kinase (MEK1)Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120(GAP) C2 domainRas uses the novel tumor suppressor RASSF1 as an effector to mediate apoptosisPERK mediates cell-cycle exit during the mammalian unfolded protein responseExpression of RALT, a feedback inhibitor of ErbB receptors, is subjected to an integrated transcriptional and post-translational controlSmgGDS displays differential binding and exchange activity towards different Ras isoformsThe Ca2+-dependent lipid binding domain of P120GAP mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins. Evidence for a direct interaction between annexin VI and P120GAPGlycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localizationThe Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, HckGTPase-activating protein interactions with the viral and cellular Src kinases.Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating proteinAssociation of MEK1 with p21ras.GMPPNP is dependent on B-Raf.Characterization of murine A-raf, a new oncogene related to the v-raf oncogeneGenetic analysis of Ras signalling pathways in cell proliferation, migration and survival.Cellular response to oncogenic ras involves induction of the Cdk4 and Cdk6 inhibitor p15(INK4b)Platelet-derived growth factor receptor mediates activation of ras through different signaling pathways in different cell typesRapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblastsThe erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potencycAMP antagonizes p21ras-directed activation of extracellular signal-regulated kinase 2 and phosphorylation of mSos nucleotide exchange factorAn essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1Ras oncogenes: split personalitiesRas-GAP controls Rho-mediated cytoskeletal reorganization through its SH3 domain.GTPase-activating protein SH2-SH3 domains induce gene expression in a Ras-dependent fashion.Molecular interactions of human immunodeficiency virus type 1 with primary human oral keratinocytes.Ras history: The saga continues.Mutational activation of c-raf-1 and definition of the minimal transforming sequence.Regulation of tetradecanoyl phorbol acetate-induced responses in NIH 3T3 cells by GAP, the GTPase-activating protein associated with p21c-ras.Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein.Interferons block protein kinase C-dependent but not-independent activation of Raf-1 and mitogen-activated protein kinases and mitogenesis in NIH 3T3 cells.
P2860
Q24293058-EC7AB2EB-F8B8-4F4A-AD04-EF01939D8AEEQ24321704-8BE89731-31F1-4427-BA34-DF192E89AECAQ24324144-123D3C14-29BF-4D24-A257-30DF8EE46167Q24336226-E552DB41-C78D-4B4A-859C-1D35BE92C1AFQ24337742-D77D0B99-F207-4813-8FD6-8D18C5FDAF0DQ24555703-3A55CD68-58B5-4040-8B6C-B88D952D635BQ24563005-A3A24CE6-3C70-439B-A2CE-E2FECCD3E86FQ24596400-CDD44D36-FFF2-4172-B065-A09BDFE146CFQ24609334-2FF78434-ACDD-4A19-BDF0-3C9873110964Q24646756-08FCF77C-3BD9-4799-9BEC-87AD9BF47C01Q24646917-5A3BDB7F-D16E-4663-9954-4F013270CA6DQ24685138-3FCBF740-94CE-462E-9C18-4E5306A43266Q28138067-6A8785E4-665D-4A36-BE30-35DDA761BED8Q28139203-4AAF6686-74EB-4FEA-AAE4-9699905EED0CQ28141519-B0665C9D-0DEA-421A-BBD5-C45DDC41D238Q28201580-443B2882-6A39-4AEE-AA30-7A3F26523931Q28214447-102021CE-676F-4F86-AB73-FE802EE3373DQ28289383-E021FC56-1349-441B-AA72-6C1E2975226EQ28290083-266EF712-EDC1-45B8-A12C-733137C12AF2Q28303352-00CA5996-D11C-4ADB-ACA0-01F308EFB0AEQ28569005-D9A05B38-FD18-4974-A817-F1BB31FAB318Q28578484-CB66DDB9-29AD-4805-8226-3D0BC587047CQ28583306-D55AEFB4-818C-4899-A6AA-D8F050736BDCQ28592226-E9AEE3F3-FD2B-43B0-8C3C-F4D8BBBEC1E1Q28595029-398A3DDC-1CE4-48E2-80AA-69628C744927Q28609756-535F3C51-959D-48CA-9906-D3A94B6F8148Q28645713-8E9FA6BF-2FF7-4871-82ED-E2E0BC3423F5Q28646356-4192DE54-82C6-4F5C-A60B-689E75DCA7C6Q28678671-5B0BE201-D357-49AA-BCB1-FEC725DA8973Q28775865-BA33E87F-3E58-4904-BD1B-687F18411569Q29614256-4A7BBB09-BF26-4D3E-8D58-5E8B03072F52Q29615405-EE45BA7D-EC49-459D-A68E-BD67138922CDQ30176086-11A264AB-6024-44C1-9070-3EE7E4AC9FC5Q30195307-2C7EFA50-86CF-48B3-9EC4-951CB1026ADBQ30350882-C0157802-648F-4FC8-9927-BEC821996CE9Q30404024-038AC23B-57FB-4DE0-927D-783F700DB704Q30406579-129E9CA5-8152-4AA9-85FD-B7D028C3827BQ30434662-D3399710-F9EE-480A-B135-6FF7EBB6C1BBQ30441879-E3958A8A-AFB3-43B4-83EC-8B96117D47C4Q30450194-A5101E1F-95D1-4CE2-984F-CEB9DE6B0827
P2860
Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells
description
1985 nî lūn-bûn
@nan
1985 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@ast
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@en
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@nl
type
label
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@ast
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@en
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@nl
prefLabel
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@ast
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@en
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@nl
P2093
P356
P1433
P1476
Requirement for ras proto-onco ...... ulated growth of NIH 3T3 cells
@en
P2093
D W Stacey
L S Mulcahy
P2888
P356
10.1038/313241A0
P407
P577
1985-01-01T00:00:00Z
P6179
1052282285