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Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptorMolecular basis of the recognition of nephronectin by integrin alpha8beta1RGD-containing peptides inhibit fibrinogen binding to platelet alpha(IIb)beta3 by inducing an allosteric change in the amino-terminal portion of alpha(IIb)Epitopes in α8β1 and other RGD-binding integrins delineate classes of integrin-blocking antibodies and major binding loops in α subunitsFocal adhesions are sites of integrin extension.Ligand-induced Epitope Masking: DISSOCIATION OF INTEGRIN α5β1-FIBRONECTIN COMPLEXES ONLY BY MONOCLONAL ANTIBODIES WITH AN ALLOSTERIC MODE OF ACTION.The thioesterase domain from a nonribosomal peptide synthetase as a cyclization catalyst for integrin binding peptides.In vitro selection of fibronectin gain-of-function mutationsInsights into integrin-ligand binding and activation from the first crystal structure.Metal ion and ligand binding of integrin α5β1Bio-adhesive surfaces to promote osteoblast differentiation and bone formation.Three-dimensional MR mapping of angiogenesis with alpha5beta1(alpha nu beta3)-targeted theranostic nanoparticles in the MDA-MB-435 xenograft mouse model.Priming integrin alpha5 promotes human mesenchymal stromal cell osteoblast differentiation and osteogenesis.Osteogenic differentiation of human mesenchymal stem cells on α5 integrin binding peptide hydrogels is dependent on substrate elasticitySurface modification and endothelialization of biomaterials as potential scaffolds for vascular tissue engineering applications.Structure of integrin alpha5beta1 in complex with fibronectin.Mapping the ligand-binding pocket of integrin alpha5beta1 using a gain-of-function approach.Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in an integrin-dependent manner.Dual functionality of the anti-beta1 integrin antibody, 12G10, exemplifies agonistic signalling from the ligand binding pocket of integrin adhesion receptors.A biomimetic peptide fluorosurfactant polymer for endothelialization of ePTFE with limited platelet adhesion.Interaction of the α2A domain of integrin with small collagen fragments.Platelet and endothelial adhesion on fluorosurfactant polymers designed for vascular graft modificationGeneration of a minimal alpha5beta1 integrin-Fc fragment.Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain.Rac2 specificity in macrophage integrin signaling: potential role for Syk kinase.Conformational Changes in the Integrin βA Domain Provide a Mechanism for Signal Transduction via Hybrid Domain MovementMolecular Basis of Ligand Recognition by Integrin α5β1
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P2860
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Juli 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2000
@uk
name
Molecular Basis of Ligand Recognition by Integrin α5β1
@en
Molecular Basis of Ligand Recognition by Integrin α5β1
@nl
type
label
Molecular Basis of Ligand Recognition by Integrin α5β1
@en
Molecular Basis of Ligand Recognition by Integrin α5β1
@nl
prefLabel
Molecular Basis of Ligand Recognition by Integrin α5β1
@en
Molecular Basis of Ligand Recognition by Integrin α5β1
@nl
P2093
P2860
P356
P1476
Molecular basis of ligand reco ...... by Trp157 OF THE alpha subunit
@en
P2093
J A Askari
J D Humphries
M J Humphries
P2860
P304
20337-20345
P356
10.1074/JBC.M000568200
P407
P577
2000-07-01T00:00:00Z