Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
about
sameAs
The diversification of the LIM superclass at the base of the metazoa increased subcellular complexity and promoted multicellular specializationThe roles of two distinct regions of PINCH-1 in the regulation of cell attachment and spreadingThe structural basis of integrin-linked kinase-PINCH interactionsThe integrin-actin connection, an eternal love affairElevated expression of the integrin-associated protein PINCH suppresses the defects of Drosophila melanogaster muscle hypercontraction mutantsStructural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinasePINCH: More than just an adaptor protein in cellular response.Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survivalPurification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complexIntegrin-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 cardiomyocytesRole of PINCH and its partner tumor suppressor Rsu-1 in regulating liver size and tumorigenesisGnRH-(1-5) transactivates EGFR in Ishikawa human endometrial cells via an orphan G protein-coupled receptorThe mouse blood-brain barrier transcriptome: a new resource for understanding the development and function of brain endothelial cellsPINCH1 regulates Akt1 activation and enhances radioresistance by inhibiting PP1alphaSox10 controls migration of B16F10 melanoma cells through multiple regulatory target genes.Talin1 has unique expression versus talin 2 in the heart and modifies the hypertrophic response to pressure overload.Role of the RNA-binding protein IMP-2 in muscle cell motility.BMP promotes motility and represses growth of smooth muscle cells by activation of tandem Wnt pathwaysPINCH in the cellular stress response to tau-hyperphosphorylation.The integrin-linked kinase-PINCH-parvin complex supports integrin αIIbβ3 activation.GPR17 gene disruption does not alter food intake or glucose homeostasis in mice.Clinicopathological significance of stromal variables: angiogenesis, lymphangiogenesis, inflammatory infiltration, MMP and PINCH in colorectal carcinomas.Mechanical stimuli and IL-13 interact at integrin adhesion complexes to regulate expression of smooth muscle myosin heavy chain in airway smooth muscle tissue.PINCH-2 expression in cancers involving serosal effusions using quantitative PCR.Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes.Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signalingParvin-beta inhibits breast cancer tumorigenicity and promotes CDK9-mediated peroxisome proliferator-activated receptor gamma 1 phosphorylation.Roles of PINCH-2 in regulation of glomerular cell shape change and fibronectin matrix deposition.Particularly interesting cysteine- and histidine-rich protein in cardiac development and remodeling.Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis.Transcriptome of Cultured Lung Fibroblasts in Idiopathic Pulmonary Fibrosis: Meta-Analysis of Publically Available Microarray Datasets Reveals Repression of Inflammation and Immunity Pathways.Particularly interesting Cys-His-rich protein is highly expressed in human intracranial aneurysms and resists aneurysmal rupture.How integrins control mammary epithelial differentiation: a possible role for the ILK-PINCH-Parvin complex.PINCH-2 presents functional copy number variation and suppresses migration of colon cancer cells by paracrine activity.Signaling via PINCH: Functions, binding partners and implications in human diseases.MiRNA let-7g regulates skeletal myoblast motility via Pinch-2.Integrin-linked kinase regulates chondrocyte shape and proliferationA dual role for integrin-linked kinase in platelets: regulating integrin function and alpha-granule secretion.gamma-Parvin is dispensable for hematopoiesis, leukocyte trafficking, and T-cell-dependent antibody response.
P2860
Q21560967-BDF8E3F2-DB22-46F4-B370-98A2E3CA4E2BQ24302005-FF65609A-BD4F-4F8F-B63A-A3325390406BQ24324678-5D0B2EBA-C489-4BD1-906F-6766D91D19DCQ24676735-4A6DDA9D-533F-450A-ABE7-5F73544AA089Q27323931-165A05E3-BE2F-4ABA-8657-33CB9CA69F3BQ27658441-AA6E10DF-929F-42DA-8006-83B3C88EF0E3Q27691415-4896AF1C-F02A-488A-BD31-BEFC40FD93A9Q28255061-19818516-17D5-4025-AACC-F7236BE0171EQ28485871-A1593AEA-859C-464A-9235-16F94A3A2A3DQ28585627-7EDA0573-7465-407B-B921-F4E9A682F9DBQ28586847-5F9B6B6E-B83A-4EBA-B120-E1577B8432AFQ28594335-F6F5483E-EED0-4BF4-93BB-7079A88E6857Q33663674-7924985C-03BA-41D3-9580-1A610DDAFF81Q33741896-F559F72B-0C62-4982-B577-9F084222A42EQ33968025-0CDA5A93-EBDA-4419-8E8F-89EE1CEE17F3Q34170999-E82CD9F0-19B6-4E03-AEFF-59434C33E10AQ34319557-6DF5952E-6F17-4B1B-B1E7-900956C8F1A7Q34416295-33A53609-B6E8-4AF5-899D-178B79266B4DQ34483074-7A0D7CBE-48BA-4366-8FFC-0CA029253CAAQ34647958-A5A5027E-B7DC-486B-BA41-8FE82BC7543BQ35078592-0E631D2B-01A0-4AE8-A252-CDCC058529CCQ35089970-1328714B-6C9B-434C-BC1F-873445432B2CQ35104008-6303D19D-0038-448E-88BF-3E2EC462DDFFQ35217372-7C191703-CCB1-49B7-A5E9-DEA4EBFA254AQ35576881-6F4D85A4-84EF-47F9-A80E-59088911F55BQ35941444-3CB7D58F-86D1-47C3-BC5B-1510431D2FC0Q36124192-33324AC5-0CE5-46DC-A6EF-F7B0101C01A1Q36421428-CE1D1143-4533-4EBB-B5AC-9BA3B43F6B14Q36807076-FDBC8246-97F9-4914-A267-6EA10057B10AQ37012318-9F3A740C-4B80-40DF-AA4C-D35A5E3A18F0Q37118092-1C2CF734-094D-4E45-B212-3FE43F362B50Q37534819-35015FAF-4CC7-441C-8FBD-B8FB92D85E3CQ37581757-1019897B-0926-4427-931F-A7E1343FC74BQ37875475-9EEEA28D-C09A-4AF3-9C88-9B64DC0DACC2Q38945020-FE21149E-7A2F-4D38-BB93-2FDD4DFFDE42Q38945219-AA383BD3-F15D-47A8-9295-1D130A2C62B2Q39016873-6E19E8FE-6B48-4095-9DE6-9B11FA23FD89Q40771629-25A8235F-098A-470E-845B-2D722198C581Q41144341-48C52733-CFA8-4AFF-9050-8552B67396C7Q42124473-2872868D-9519-45E3-9218-22C8C9A7ECA2
P2860
Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Characterization of PINCH-2, a ...... cell spreading, and migration
@ast
Characterization of PINCH-2, a ...... cell spreading, and migration
@en
Characterization of PINCH-2, a ...... cell spreading, and migration
@nl
type
label
Characterization of PINCH-2, a ...... cell spreading, and migration
@ast
Characterization of PINCH-2, a ...... cell spreading, and migration
@en
Characterization of PINCH-2, a ...... cell spreading, and migration
@nl
prefLabel
Characterization of PINCH-2, a ...... cell spreading, and migration
@ast
Characterization of PINCH-2, a ...... cell spreading, and migration
@en
Characterization of PINCH-2, a ...... cell spreading, and migration
@nl
P2093
P2860
P356
P1476
Characterization of PINCH-2, a ...... cell spreading, and migration
@en
P2093
Chuanyue Wu
Yongjun Zhang
P2860
P304
P356
10.1074/JBC.M205576200
P407
P577
2002-10-11T00:00:00Z