A new member of the LIM protein family binds to filamin B and localizes at stress fibers
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Structural basis of the migfilin-filamin interaction and competition with integrin beta tailsMigfilin, a molecular switch in regulation of integrin activationIdentification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and cross-talkThe LIM domain: from the cytoskeleton to the nucleusFilamin B mutations cause chondrocyte defects in skeletal developmentExpression of migfilin is increased in esophageal cancer and represses the Akt-β-catenin activation.Migfilin and filamin as regulators of integrin activation in endothelial cells and neutrophils.Documentation and localization of force-mediated filamin A domain perturbations in moving cells.Biochemical characterization of the cell-biomaterial interface by quantitative proteomics.Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration.A molecular and clinical study of Larsen syndrome caused by mutations in FLNBThe filamins: organizers of cell structure and functionFilamin interacts with epithelial sodium channel and inhibits its channel function.Cell Adhesion and Transcriptional Activity - Defining the Role of the Novel Protooncogene LPPInteractome disassembly during apoptosis occurs independent of caspase cleavage.Kindlins in FERM adhesion.Migfilin sensitizes cisplatin-induced apoptosis in human glioma cells in vitro.TMEM158 and FBLP1 as novel marker genes of cisplatin sensitivity in non-small cell lung cancer cells.Supervillin binds the Rac/Rho-GEF Trio and increases Trio-mediated Rac1 activation.Possible involvement of a cell adhesion molecule, Migfilin, in brain development and pathogenesis of autism spectrum disorders.Structural Analysis of G1691S Variant in the Human Filamin B Gene Responsible for Larsen Syndrome: A Comparative Computational Approach.Comparative analysis of the two extremes of FLNB-mutated autosomal dominant disease spectrum: from clinical phenotypes to cellular and molecular findings.
P2860
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P2860
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@ast
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@en
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@nl
type
label
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@ast
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@en
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@nl
prefLabel
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@ast
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@en
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@nl
P2093
P2860
P356
P1476
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
@en
P2093
Kingo Fujimura
Mari Saeki
Sandor S Shapiro
Tetsuro-Takahiro Fujimoto
Toshiro Takafuta
P2860
P304
P356
10.1074/JBC.M209339200
P407
P577
2003-04-04T00:00:00Z