The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen.
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Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kineticsMutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain.An HMM-based algorithm for evaluating rates of receptor-ligand binding kinetics from thermal fluctuation data.A recombinant fragment of von Willebrand factor reduces fibrin-rich microthrombi formation in mice with endotoxemiaInteraction of Shiga toxin with the A-domains and multimers of von Willebrand Factor.Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stressThe mechanism of VWF-mediated platelet GPIbalpha binding.Analysis of the role of von Willebrand factor, platelet glycoprotein VI-, and α2β1-mediated collagen binding in thrombus formation.GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease.N-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress.Differential surface activation of the A1 domain of von Willebrand factor.Cooperative unfolding of distinctive mechanoreceptor domains transduces force into signals.Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalpha.The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Ibα.On the versatility of von Willebrand factorPurified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibalpha.M1761K mutation in the von Willebrand factor A3 domain associated with impaired collagen binding and without platelet dysfunction.The Von Willebrand Factor A1-Collagen III Interaction Is Independent of Conformation and Type 2 Von Willebrand Disease Phenotype.von Willebrand Factor, Free Hemoglobin and Thrombosis in ECMO
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P2860
The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen.
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2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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name
The interaction of von Willebr ...... A1 domain induced by collagen.
@en
The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S
@nl
type
label
The interaction of von Willebr ...... A1 domain induced by collagen.
@en
The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S
@nl
prefLabel
The interaction of von Willebr ...... A1 domain induced by collagen.
@en
The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S
@nl
P2093
P2860
P1476
The interaction of von Willebr ...... A1 domain induced by collagen.
@en
P2093
P2860
P304
P356
10.1111/J.1538-7836.2006.01742.X
P577
2006-02-01T00:00:00Z