Domain unfolding plays a role in superfibronectin formation.
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Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeatForce-induced unfolding of fibronectin in the extracellular matrix of living cellsInterdomain association in fibronectin: insight into cryptic sites and fibrillogenesisStructure and unfolding of the third type III domain from human fibronectinFibronectins, their fibrillogenesis, and in vivo functions.Assembly of fibronectin extracellular matrix.Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectinStructural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectinConformational remodeling of the fibronectin matrix selectively regulates VEGF signaling.Coordinate regulation of fibronectin matrix assembly by the plasminogen activator system and vitronectin in human osteosarcoma cells.Dermatopontin interacts with fibronectin, promotes fibronectin fibril formation, and enhances cell adhesion.The TLR4 agonist fibronectin extra domain A is cryptic, exposed by elastase-2; use in a fibrin matrix cancer vaccineProbing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.Experimental and computational examination of anastellin (FnIII1c)-polymer interactions.Extracellular matrix: from atomic resolution to ultrastructure.SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.Regulation of p38 MAP kinase by anastellin is independent of anastellin's effect on matrix fibronectinFibronectin peptides that bind PDGF-BB enhance survival of cells and tissue under stress.The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Cryptic activity within the Type III1 domain of fibronectin regulates tissue inflammation and angiogenesis.Genetic analysis of beta1 integrin "activation motifs" in mice.The RGD motif in fibronectin is essential for development but dispensable for fibril assembly.Motogenic sites in human fibronectin are masked by long range interactions.Mapping the recognition domains of pneumococcal fibronectin-binding proteins PavA and PavB demonstrates a common pattern of molecular interactions with fibronectin type III repeats.Adrenocortical zonation factor 1 is a novel matricellular protein promoting integrin-mediated adhesion of adrenocortical and vascular smooth muscle cells.A novel fibronectin binding motif in MSCRAMMs targets F3 modules.Identification of fibronectin type I domains as amyloid-binding modules on tissue-type plasminogen activator and three homologs.Structure-critical distribution of aromatic residues in the fibronectin type III protein family.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.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
P2860
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P2860
Domain unfolding plays a role in superfibronectin formation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Domain unfolding plays a role in superfibronectin formation.
@en
Domain unfolding plays a role in superfibronectin formation.
@nl
type
label
Domain unfolding plays a role in superfibronectin formation.
@en
Domain unfolding plays a role in superfibronectin formation.
@nl
prefLabel
Domain unfolding plays a role in superfibronectin formation.
@en
Domain unfolding plays a role in superfibronectin formation.
@nl
P2860
P356
P1476
Domain unfolding plays a role in superfibronectin formation.
@en
P2093
Harold P Erickson
Tomoo Ohashi
P2860
P304
39143-39151
P356
10.1074/JBC.M509082200
P407
P577
2005-09-29T00:00:00Z