Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1
about
Nuclear import of LASP-1 is regulated by phosphorylation and dynamic protein-protein interactionsLasp-1 regulates podosome functionIdentification of Xin-repeat proteins as novel ligands of the SH3 domains of nebulin and nebulette and analysis of their interaction during myofibril formation and remodelingThe Nebulin family: an actin support groupLIM and SH3 protein 1 promotes tumor proliferation and metastasis in lung carcinoma.Regulation of matrix metalloproteinases (MMPs) expression and secretion in MDA-MB-231 breast cancer cells by LIM and SH3 protein 1 (LASP1)Upregulated LASP-1 correlates with a malignant phenotype and its potential therapeutic role in human cholangiocarcinoma.LASP1, a Newly Identified Melanocytic Protein with a Possible Role in Melanin Release, but Not in Melanoma ProgressionAn update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker proteinLIM and SH3 domain protein 1 (LASP-1) overexpression was associated with aggressive phenotype and poor prognosis in clear cell renal cell cancer.Tumor-suppressive microRNA-218 inhibits cancer cell migration and invasion via targeting of LASP1 in prostate cancer.The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse.Nuclear localisation of LASP-1 correlates with poor long-term survival in female breast cancer.LIM and SH3 protein-1 modulates CXCR2-mediated cell migration.Contribution of the LIM domain and nebulin-repeats to the interaction of Lasp-2 with actin filaments and focal adhesions.Global gene expression analysis identifies PDEF transcriptional networks regulating cell migration during cancer progressionTargeted disruption of the Lasp-1 gene is linked to increases in histamine-stimulated gastric HCl secretionThe LIM and SH3 domain protein family: structural proteins or signal transducers or both?Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisationShort-term retention of actin filament binding proteins on lamellipodial actin bundles.AP-1 differentially expressed proteins Krp1 and fibronectin cooperatively enhance Rho-ROCK-independent mesenchymal invasion by altering the function, localization, and activity of nondifferentially expressed proteins.Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators.Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.Nebulette is a powerful cytolinker organizing desmin and actin in mouse heartsNuclear localization and cytosolic overexpression of LASP-1 correlates with tumor size and nodal-positivity of human breast carcinomaLASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition.Nonmuscle myosin IIB, a sarcomeric component in the extraocular muscles.Linkage analysis of three families with arrythmogenic right ventricular cardiomyopathy in India.Nebulette knockout mice have normal cardiac function, but show Z-line widening and up-regulation of cardiac stress markers.Ectopic expression of LIM-nebulette (LASP2) reveals roles in cell migration and spreading.Exploratory Visual Analysis of statistical results from microarray experiments comparing high and low grade gliomaLasp1 gene disruption is linked to enhanced cell migration and tumor formationZyxin emerges as a key player in the mechanotransduction at cell adhesive structures.The interactome of LIM domain proteins: the contributions of LIM domain proteins to heart failure and heart development.Proteomic analysis of human substantia nigra identifies novel candidates involved in Parkinson's disease pathogenesis.Animal Models of Congenital Cardiomyopathies Associated With Mutations in Z-Line Proteins.Overview of the Muscle Cytoskeleton.alpha-Actinin links LPP, but not zyxin, to cadherin-based junctions.Lasp2 enhances tumor invasion via facilitating phosphorylation of FAK and predicts poor overall survival of non-small cell lung cancer patients.New Frontiers for the Cytoskeletal Protein LASP1
P2860
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P2860
Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1
description
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im Mai 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 7 May 2004)
@en
vedecký článok (publikovaný 2004/05/07)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/05/07)
@nl
наукова стаття, опублікована в травні 2004
@uk
name
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@ast
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@en
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@nl
type
label
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@ast
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@en
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@nl
prefLabel
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@ast
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@en
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@nl
P2860
P356
P1476
Zyxin interacts with the SH3 d ...... teins LIM-nebulette and Lasp-1
@en
P2093
P2860
P304
P356
10.1074/JBC.M310304200
P407
P50
P577
2004-05-07T00:00:00Z