A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
about
Structural basis for paxillin binding and focal adhesion targeting of β-parvinThe roles of two distinct regions of PINCH-1 in the regulation of cell attachment and spreadingPhosphorylation and interaction of myopodin by integrin-link kinase lead to suppression of cell growth and motility in prostate cancer cellsInteraction of integrin-linked kinase with the kidney chloride/bicarbonate exchanger, kAE1Affixin activates Rac1 via betaPIX in C2C12 myoblastAffixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interactionThe integrin-actin connection, an eternal love affairPhosphorylation of actopaxin regulates cell spreading and migrationILK: a pseudokinase in the center stage of cell-matrix adhesion and signalingThe Pseudoactive Site of ILK Is Essential for Its Binding to α-Parvin and Localization to Focal AdhesionsThe paxillin LD motifsCharacterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migrationPurification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complexRole of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophyActopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinaseIntegrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulationAlpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signallingAn integrin-linked machinery of cytoskeletal regulation that enables experimental tumor initiation and metastatic colonizationIntegrin-linked kinase is a functional Mn2+-dependent protein kinase that regulates glycogen synthase kinase-3β (GSK-3beta) phosphorylationPathway analysis using genome-wide association study data for coronary restenosis--a potential role for the PARVB gene.Correlating global gene regulation to angiogenesis in the developing chick extra-embryonic vascular system.SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity.Integrin-linked kinase functions as a downstream signal of platelet-derived growth factor to regulate actin polymerization and vascular smooth muscle cell migration.The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!Integration of cell attachment, cytoskeletal localization, and signaling by integrin-linked kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN.Molecular dissection of actopaxin-integrin-linked kinase-Paxillin interactions and their role in subcellular localization.Functional plasticity of CH domains.Expression of parvin-beta is a prognostic factor for patients with urothelial cell carcinoma of the upper urinary tract.Beta-parvin inhibits integrin-linked kinase signaling and is downregulated in breast cancer.Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexesILK mediates the effects of strain on intestinal epithelial wound closureBiochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase.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.Integrin-linked kinase regulates the rate of platelet activation and is essential for the formation of stable thrombi.mda-9/Syntenin protein positively regulates the activation of Akt protein by facilitating integrin-linked kinase adaptor function during adhesion to type I collagen.PARVB overexpression increases cell migration capability and defines high risk for endophytic growth and metastasis in tongue squamous cell carcinoma.CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt.The parvins.Parvin-beta inhibits breast cancer tumorigenicity and promotes CDK9-mediated peroxisome proliferator-activated receptor gamma 1 phosphorylation.
P2860
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P2860
A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
A novel integrin-linked kinase ...... of cell-substrate interaction
@ast
A novel integrin-linked kinase ...... of cell-substrate interaction
@en
A novel integrin-linked kinase ...... of cell-substrate interaction
@nl
type
label
A novel integrin-linked kinase ...... of cell-substrate interaction
@ast
A novel integrin-linked kinase ...... of cell-substrate interaction
@en
A novel integrin-linked kinase ...... of cell-substrate interaction
@nl
prefLabel
A novel integrin-linked kinase ...... of cell-substrate interaction
@ast
A novel integrin-linked kinase ...... of cell-substrate interaction
@en
A novel integrin-linked kinase ...... of cell-substrate interaction
@nl
P2093
P2860
P3181
P356
P1476
A novel integrin-linked kinase ...... of cell-substrate interaction
@en
P2093
H Kanamori
Y Ishigatsubo
Y Sugiyama
P2860
P304
P3181
P356
10.1083/JCB.153.6.1251
P407
P577
2001-06-11T00:00:00Z