Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
about
Tyrosine kinase signalling in breast cancer: insulin-like growth factors and their receptors in breast cancer.SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeIdentification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to NckModulation of protein translation by Nck-1.Identification of Nck family genes, chromosomal localization, expression, and signaling specificityGrowth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1Interaction of Nck-associated protein 1 with activated GTP-binding protein RacNck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activationWiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domainsThe structure and function of p55PIK reveal a new regulatory subunit for phosphatidylinositol 3-kinaseNck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathwaysThe role of suppressors of cytokine signalling in human neoplasmsThe Nck-interacting kinase (NIK) phosphorylates the Na+-H+ exchanger NHE1 and regulates NHE1 activation by platelet-derived growth factorTyr624 and Tyr628 in insulin receptor substrate-2 mediate its association with the insulin receptorThe type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein NckInteraction of the Nck adapter protein with p21-activated kinase (PAK1)Insulin/IGF-1 and TNF-alpha stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathwaysInsulin stimulates the tyrosine dephosphorylation of docking protein p130cas (Crk-associated substrate), promoting the switch of the adaptor protein crk from p130cas to newly phosphorylated insulin receptor substrate-1The Fyn tyrosine kinase binds Irs-1 and forms a distinct signaling complex during insulin stimulationInsulin signal transduction in rat small intestine: role of MAP kinases in expression of mucosal hydrolasesInsulin-stimulated disassociation of the SOS-Grb2 complexIdentification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing moleculesThe role of the tyrosine kinase domain of the insulin-like growth factor-I receptor in intracellular signaling, cellular proliferation, and tumorigenesisRecombinant human insulin receptor substrate-1 protein. Tyrosine phosphorylation and in vitro binding of insulin receptor kinaseDock/Nck facilitates PTP61F/PTP1B regulation of insulin signalling.Nck adapter proteins: functional versatility in T cellsActivation of the Abl tyrosine kinase in vivo by Src homology 3 domains from the Src homology 2/Src homology 3 adaptor Nck.Angiotensin II stimulates serine phosphorylation of the adaptor protein Nck: physical association with the serine/threonine kinases Pak1 and casein kinase IExpression of mutated Nck SH2/SH3 adaptor respecifies mesodermal cell fate in Xenopus laevis developmentA casein kinase I activity is constitutively associated with Nck.Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.A complex of GRB2-dynamin binds to tyrosine-phosphorylated insulin receptor substrate-1 after insulin treatment.Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivoNitric oxide agents impair insulin-mediated signal transduction in rat skeletal muscleProtein-protein interaction in insulin signaling and the molecular mechanisms of insulin resistanceInsulin receptor substrates (IRSs) and breast tumorigenesis.Insulin receptor substrate-1 variants in non-insulin-dependent diabetesInsulin-dependent tyrosine phosphorylation of the vav protooncogene product in cells of hematopoietic origin.A rare co-segregation-mutation in the insulin receptor substrate 1 gene in one Chinese family with ankylosing spondylitis
P2860
Q21195187-1253C166-79C1-47DB-B64B-A55238F0D4FCQ21245515-83E29F8A-D26B-4A0B-9F5B-9FCEAA28C745Q22008787-D23BC7F5-F5A4-4AC1-8874-EE5D0F74B2C3Q24294686-B5831E28-5757-4E1C-877D-37EC7E1B35A1Q24313473-6826DDBE-B2EA-4D85-AA94-92C108460B0BQ24322608-C93A4068-0DA2-43B8-A828-D03FF1D6A4ECQ24530109-CD386D85-349D-446C-B121-AEF7966C74F0Q24554304-E7B29C6A-D0FF-4C63-B2E4-7BA114C0AD89Q24651136-5FA7E2D6-2D74-4506-A4CA-182FCB6BB7BDQ24651484-F73F6DDC-B624-4B41-90A3-B48FD2883455Q24655497-D0E52499-1B8B-4ACD-96AA-035009E4406DQ27026783-12DD78E4-5E58-4C76-98A9-DD36B5DDDE09Q28190227-513A5B64-A870-49E4-A7CC-1D50DC7BBCBBQ28241699-4CD18927-36E4-4CBC-951B-00AEA41E237AQ28272589-2CCC18B0-182A-430B-A10C-6C555F269478Q28278822-5EC7F00A-DB4E-4520-B280-BE656B453A3CQ28291014-F8061547-BE68-47FC-AF5D-7CA5521124ADQ28346530-5DBBAA2C-6143-4CEB-9CCF-29AFD5505D09Q28507779-65CC56C4-1E18-4921-B3A9-840318E0A9DAQ28510589-B3E10C8C-BA57-43E3-B085-67C89F62D67EQ28576668-B78F4204-3784-459A-B44C-E2AB2D2A344EQ28615780-40321313-FD91-4537-8390-A94461358EFAQ28646549-26F8A777-1865-4341-BE8B-3BEBF4983AD1Q28678337-AEF78956-4BF8-4F25-B001-8700A51D0354Q28678379-0CDA6708-73C5-4CB3-8B18-D93FD3686423Q30010287-F5C7383A-CDE6-4AD1-96DB-C9A026C68BD0Q30157371-3C846454-2796-41A6-88D9-128388940CE8Q30175353-803F3968-A6C5-4BB6-8FA0-E700909044B5Q30175420-92B82068-CCA3-4734-89E1-CE4F6209E598Q30176566-FEB927E2-E7C2-45DF-A5EF-B25CEBF220AEQ30176651-A69368B5-6C8C-49AF-9691-A6E7E9FE4B88Q30193588-6A3B54FB-7EE8-4339-8DC1-E4FF55C657DFQ30194218-DEA43083-98D4-4CF1-B063-FEF03E9F8322Q31033276-305B8B4B-CF5F-430B-BF07-034B33AEE2FFQ33244914-E4DEF550-2F7F-4CC6-8F35-C6B701490173Q33588931-C2E04EC0-F048-48AE-96A5-B72F461E4A7FQ33642166-DDB4FB5E-CCEE-4425-8FB6-EE697CF27FA4Q34184582-A9433317-AA48-428B-BD2F-81A8E48336FCQ34293585-C068D449-42FB-45D1-813B-90F41BFECD56Q35610750-3C799B5C-5418-4EDE-9C5A-AAC743D8D473
P2860
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
description
1993 nî lūn-bûn
@nan
1993 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@ast
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@en
type
label
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@ast
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@en
prefLabel
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@ast
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@en
P2093
P2860
P356
P1476
Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
@en
P2093
A G Batzer
E Y Skolnik
J Schlessinger
R Nishimura
P2860
P304
11713-11717
P356
10.1073/PNAS.90.24.11713
P407
P50
P577
1993-12-01T00:00:00Z