Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
about
GFP's mechanical intermediate statesUsing molecular mechanics to predict bulk material properties of fibronectin fibersStructure and unfolding of the third type III domain from human fibronectinContribution of unfolding and intermolecular architecture to fibronectin fiber extensibility.Dynamic structure of plasma fibronectin.SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.Protein conformation as a regulator of cell-matrix adhesion.Forced protein unfolding leads to highly elastic and tough protein hydrogels.Chemical Protein Modification through Cysteine.Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis.Studying early stages of fibronectin fibrillogenesis in living cells by atomic force microscopy.Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis.Fibronectin fibrils regulate TGF-β1-induced Epithelial-Mesenchymal Transition.Mechanotransduction Dynamics at the Cell-Matrix Interface.Multiple Cryptic Binding Sites are Necessary for Robust Fibronectin Assembly: An In Silico Study.Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.Studying early stages of fibronectin fibrillogenesis in living cells by atomic force microscopy.Rationally designed synthetic protein hydrogels with predictable mechanical properties.Heparin-induced conformational changes of fibronectin within the extracellular matrix promote hMSC osteogenic differentiation.Conformational distribution of surface-adsorbed fibronectin molecules explored by single molecule localization microscopy
P2860
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P2860
Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Probing the folded state of fi ...... buried cysteine accessibility.
@ast
Probing the folded state of fi ...... buried cysteine accessibility.
@en
type
label
Probing the folded state of fi ...... buried cysteine accessibility.
@ast
Probing the folded state of fi ...... buried cysteine accessibility.
@en
prefLabel
Probing the folded state of fi ...... buried cysteine accessibility.
@ast
Probing the folded state of fi ...... buried cysteine accessibility.
@en
P2860
P356
P1476
Probing the folded state of fi ...... buried cysteine accessibility
@en
P2093
Harold P Erickson
Tomoo Ohashi
P2860
P304
26375-26382
P356
10.1074/JBC.M111.240028
P407
P577
2011-06-07T00:00:00Z