alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies of molecular determinants underlying integrin-rgd affinity and specificity
about
The evolution of extracellular fibrillins and their functional domainsEssential role for fibrillin-2 in zebrafish notochord and vascular morphogenesisBiogenesis and function of fibrillin assemblies.Induction of macrophage chemotaxis by aortic extracts from patients with Marfan syndrome is related to elastin binding protein.Mutations in fibrillin-1 cause congenital scleroderma: stiff skin syndrome.Fibrillin assemblies: extracellular determinants of tissue formation and fibrosisFibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactionsFibrillin-1 and alpha8 integrin are co-expressed in the glomerulus and interact to convey adhesion of mesangial cells.Fibrillin-containing microfibrils are key signal relay stations for cell function.Fibrillin-rich microfibrils - structural and instructive determinants of mammalian development and physiology.Choreographing metastasis to the tune of LTBP.Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils.TB domain proteins: evolutionary insights into the multifaceted roles of fibrillins and LTBPs.Fibronectin modified expression of Sonic hedgehog in ATRA-mediated neuronal differentiation.Cilengitide, a small molecule antagonist, targeted to integrin αν inhibits proliferation and induces apoptosis of laryngeal cancer cells in vitro.Selective integrin subunit reduction disrupts fibronectin extracellular matrix deposition and fibrillin 1 gene expression.The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.A microfibril assembly assay identifies different mechanisms of dominance underlying Marfan syndrome, stiff skin syndrome and acromelic dysplasiasFell-Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?Early fibrillin-1 assembly monitored through a modifiable recombinant cell approach.Colocalization in vivo and association in vitro of perlecan and elastin.Fibrillin-2 and Tenascin-C bridge the age gap in lung epithelial regeneration.p38 MAPK is an early determinant of promiscuous Smad2/3 signaling in the aortas of fibrillin-1 (Fbn1)-null mice.Recombinant Extracellular Matrix Protein fragments Support Human Embryonic Stem Cell Chondrogenesis.Multiscale Imaging Reveals the Hierarchical Organization of Fibrillin Microfibrils
P2860
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
P248
Q21134722-036604E5-675E-4B0A-9646-D5818F9D9EE8Q24608680-5B6395DF-BBDE-4810-AFCD-F8FBF74D2BFDQ33641386-52D008A5-DE8C-4414-B05B-A30C23ABA386Q33925296-6A561549-B89C-483E-A86D-BB9788EAE4E9Q34192783-C62BDE85-09E5-403F-9743-CD4DDDA402AEQ34447925-AE8C4F31-E82A-4A96-A439-E711907467B9Q34469801-D51DBBC9-0DEC-48D9-8CA5-7FFDAD004DA2Q36125086-5CE2DC0B-6229-4B1B-B3BB-FC35D3B524E8Q36470965-ADF981D7-0653-475D-A2E3-574FBE2EA952Q37091888-CC204D58-CB16-45F1-B274-EDE6948F64CBQ37106657-67167819-D9E5-4AB7-AB41-F1FB05919EAEQ37418467-7B8871F4-9EB3-4181-9515-16225B14727EQ37822821-7EA1DCCA-1992-4E58-B355-30FD42B844D7Q38866638-C330802A-126E-4632-9860-50E48AF8D803Q39025086-F5A269F6-82D4-4A2F-A5F1-3CED58A6E7B1Q39316797-7F89C481-9063-4EEC-8B25-0F42B6987250Q41312162-DD3E454B-1C54-4FE8-BF63-C09B0DE97BD8Q41373533-771E35B2-944D-4C2F-85F4-D60441572B5EQ42376279-8B603FB9-65ED-40B4-BAD0-DD79E8B8A687Q42402963-DB92CA07-2E8E-4DC0-A23B-3784E368BC50Q42493535-80059DF1-204D-4CD2-8F0B-5F8368E7E568Q42511759-27E4B57F-3540-477D-B86A-0E1DCA35E571Q43177529-53B273D7-D9C5-492A-BFD1-6CA2960A19A1Q47218182-ED981C5C-746A-4405-8180-4A897C9B3DD3Q58723125-A47A27C6-29D9-47AD-A71F-F38418ED781C
P2860
alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies of molecular determinants underlying integrin-rgd affinity and specificity
description
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2007
@ast
im März 2007 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2007/03/02)
@sk
vědecký článek publikovaný v roce 2007
@cs
wetenschappelijk artikel (gepubliceerd op 2007/03/02)
@nl
наукова стаття, опублікована в березні 2007
@uk
name
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@ast
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@en
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@nl
type
label
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@ast
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@en
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@nl
prefLabel
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@ast
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@en
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@nl
P2093
P2860
P921
P356
P1476
alphaVbeta6 is a novel recepto ...... n-rgd affinity and specificity
@en
P2093
Helen J Mardon
Jelena Jovanovic
Junichi Takagi
Laurence Choulier
P Anton van der Merwe
Penny A Handford
P2860
P304
P356
10.1074/JBC.M607008200
P407
P577
2006-12-11T00:00:00Z