Nck-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 pathways
about
Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to NckA new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreadingPINCH1 is transcriptional regulator in podocytes that interacts with WT1 and represses podocalyxin expressionStructural insight into the binding diversity between the Tyr-phosphorylated human ephrinBs and Nck2 SH2 domainNckbeta adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bbThe LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cellsThe murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin networkActin remodeling by Nck regulates endothelial lumen formationSolution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domainPINCH: More than just an adaptor protein in cellular response.Identification of PINCH in Schwann cells and DRG neurons: shuttling and signaling after nerve injuryIdentification and kinetic analysis of the interaction between Nck-2 and DOCK180Grb4/Nckbeta acts as a nuclear repressor of v-Abl-induced transcription from c-jun/c-fos promoter elementsMolecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survivalInhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cellsSrc homology 3 domain-dependent interaction of Nck-2 with insulin receptor substrate-1Purification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complexMutations in the paxillin-binding site of integrin-linked kinase (ILK) destabilize the pseudokinase domain and cause embryonic lethality in miceRole of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophyIntegrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulationPINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytesIntegrin-linked kinase is required for radial sorting of axons and Schwann cell remyelination in the peripheral nervous systemIntegrin-linked kinase mediates bone morphogenetic protein 7-dependent renal epithelial cell morphogenesisDirect regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.[A uNick protein].Nck adapter proteins: functional versatility in T cellsNck/Dock: an adapter between cell surface receptors and the actin cytoskeleton.Integrin-linked kinase controls neurite outgrowth in N1E-115 neuroblastoma cells.Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivoAlzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein.The role of the focal adhesion protein PINCH1 for the radiosensitivity of adhesion and suspension cell culturesParticularly interesting new cysteine-histidine rich protein expression in colorectal adenocarcinomas.Impact of PINCH expression on survival in colorectal cancer patients.PINCH1 regulates Akt1 activation and enhances radioresistance by inhibiting PP1alphaPINCH is an independent prognostic factor in rectal cancer patients without preoperative radiotherapy--a study in a Swedish rectal cancer trial of preoperative radiotherapyIntegrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexesSystematic prediction of human membrane receptor interactions.The integrin-linked kinase-PINCH-parvin complex supports integrin αIIbβ3 activation.Clinicopathological significance of stromal variables: angiogenesis, lymphangiogenesis, inflammatory infiltration, MMP and PINCH in colorectal carcinomas.The focal adhesion protein PINCH-1 associates with EPLIN at integrin adhesion sites.
P2860
Q22008787-8B77953C-A15A-4CC6-AA81-C232A1E16301Q24291182-B61FF827-E46A-46D1-88B9-815F6721C6B6Q24296236-D5E28B13-EAD7-4E06-A4DE-3951D2E17C6FQ24297924-1496DD63-49DB-41D5-92AB-0FB65D815913Q24551163-E042F813-D556-44B1-9EB4-37F09F8B290EQ24554520-7E2DBC2C-6F51-4F8A-9D48-EF968E13F439Q24682994-2B554BDF-625A-4A2C-A74C-107B31434F5EQ27305490-A2E09423-C794-4A93-A584-49E1E1CC7BFFQ27628157-7E536A31-1B80-4FE6-A3C4-16CE53868DD2Q27691415-3AB27171-655F-439B-A018-050EC04DD63DQ28203144-1CEDB7E8-E5D7-421F-849D-01B73BFCACC8Q28203896-748EAADE-DA5D-4FB5-8E91-A8DC5AF69560Q28213938-5734CC32-E842-402E-9293-1ED47F99B74FQ28255061-C2EBB938-C463-46A6-A45F-7FB7D39165EFQ28344025-07772BF7-C8D7-4299-ADB2-4348A97A272CQ28348345-05AF8F25-5539-4BD5-912C-5CF3E9E9EDEEQ28485871-1FE59A0D-706D-469D-8236-A8E028D4A0C1Q28508913-CEAFB306-F240-42B2-907D-4935A49EB8E9Q28567124-87D3045B-BD5D-4B99-96C6-0C7038B6DF49Q28585627-6D703DBB-7EA2-42E9-BF09-F7076F298802Q28586847-3AC30BBA-0064-4E82-BE67-130E340DE436Q28587844-794B217F-E339-4E01-89BE-430CE1820A02Q28589224-BF9EB89E-C30B-4F44-9A10-55B3D9404744Q30009968-7A723FA4-8560-43A6-8962-63E665860FD1Q30010244-5751F1E7-596D-430E-AA1C-2555F7B0322BQ30157371-CB0DCC03-9995-461F-BA5E-F864341AD4AAQ30167854-5014546D-0250-482D-94DD-B9993484B51BQ31010256-37A0A904-5A2B-46D0-8673-375792C123CBQ31033276-D2DC3826-6F07-4183-A073-65A4F89D15A4Q33292161-89408B6F-702A-4CED-9405-AB116F343342Q33712107-76BE6DBA-3362-4B89-B783-FD3DF742CB4EQ33788152-B5CFDB74-DD42-44FD-968C-B711C4011E43Q33852653-50AF02FD-78BA-4AE0-95D2-1A4631A49BCCQ33968025-E224DD59-88A9-4F90-9693-8FD1523EEF0CQ34156316-FCB722AF-0ED5-46DC-9B55-717060941EA9Q34429805-96ADD2F5-C8E8-4DBD-8D59-CA757507E67AQ34789186-A1533C07-8AB9-48FE-946F-93EE592A0574Q35078592-A62CF1D1-F620-46DC-AC4E-717B079CDF56Q35104008-E0557C89-1018-4E68-83BE-2B69CF069305Q35126974-3FF273BC-145A-4B08-8E80-C2CF461A9EF5
P2860
Nck-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 pathways
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@ast
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@en
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@nl
type
label
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@ast
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@en
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@nl
prefLabel
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@ast
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@en
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@nl
P2093
P2860
P356
P1476
Nck-2, a novel Src homology2/3 ...... ptor kinase-signaling pathways
@en
P2093
P2860
P304
P356
10.1091/MBC.9.12.3367
P407
P577
1998-12-01T00:00:00Z