The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.
about
Structural and functional analysis of the fibronectin-binding protein FNE from Streptococcus equi spp. equiStructural Analysis of Collagen Type I Interactions with Human Fibronectin Reveals a Cooperative Binding ModeBorrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational ExtensionThe tandem β-zipper: modular binding of tandem domains and linear motifs.Molecular architecture of native fibronectin fibrils.Bivalent ligation of the collagen-binding modules of fibronectin by SFS, a non-anchored bacterial protein of Streptococcus equi.Reactivity of the N-terminal region of fibronectin protein to transglutaminase 2 and factor XIIIAOn-Off Kinetics of Engagement of FNI Modules of Soluble Fibronectin by β-Strand Addition.Fibronectin binding to the Treponema pallidum adhesin protein fragment rTp0483 on functionalized self-assembled monolayersLigation of the fibrin-binding domain by β-strand addition is sufficient for expansion of soluble fibronectin.Dynamic structure of plasma fibronectin.Cooperative binding and activation of fibronectin by a bacterial surface protein.
P2860
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P2860
The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
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2010年论文
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name
The streptococcal binding site ...... linear arrangement of modules.
@en
type
label
The streptococcal binding site ...... linear arrangement of modules.
@en
prefLabel
The streptococcal binding site ...... linear arrangement of modules.
@en
P2093
P2860
P50
P356
P1476
The streptococcal binding site ...... linear arrangement of modules.
@en
P2093
Andrew S Brentnall
David Staunton
Iain D Campbell
Ioannis Vakonakis
Jennifer R Potts
Kate E Atkin
Michele C Erat
P2860
P304
36977-36983
P356
10.1074/JBC.M110.156935
P407
P577
2010-09-15T00:00:00Z