Autoregulation of von Willebrand factor function by a disulfide bond switch
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Title
Autoregulation of von Willebrand factor function by a disulfide bond switch
Authors
Keywords
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Journal
Science Advances
Volume 4, Issue 2, Pages eaaq1477
Publisher
American Association for the Advancement of Science (AAAS)
Online
2018-03-01
DOI
10.1126/sciadv.aaq1477
References
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Related references
Note: Only part of the references are listed.- Mutual A domain interactions in the force sensing protein von Willebrand factor
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- A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor
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- Flow-induced elongation of von Willebrand factor precedes tension-dependent activation
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- N-linked glycan stabilization of the VWF A2 domain
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- A substrate-driven allosteric switch that enhances PDI catalytic activity
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- Cooperative unfolding of distinctive mechanoreceptor domains transduces force into signals
- (2016) Lining Ju et al. eLife
- Force-Sensitive Autoinhibition of the von Willebrand Factor Is Mediated by Interdomain Interactions
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- Force-Induced Unfolding of Leucine-Rich Repeats of Glycoprotein Ibα Strengthens Ligand Interaction
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- Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics
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- (2015) Yunfeng Chen et al. Jove-Journal of Visualized Experiments
- Redox Regulation of Methionine Aminopeptidase 2 Activity
- (2014) Joyce Chiu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The N-terminal Flanking Region of the A1 Domain Regulates the Force-dependent Binding of von Willebrand Factor to Platelet Glycoprotein Ibα
- (2013) Lining Ju et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Allosteric Control of βII-Tryptase by a Redox Active Disulfide Bond
- (2013) Kristina M. Cook et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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- Pathologic shear triggers shedding of vascular receptors: a novel mechanism for down-regulation of platelet glycoprotein VI in stenosed coronary vessels
- (2012) M. Al-Tamimi et al. BLOOD
- N-terminal Flanking Region of A1 Domain in von Willebrand Factor Stabilizes Structure of A1A2A3 Complex and Modulates Platelet Activation under Shear Stress
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- Calcium stabilizes the von Willebrand factor A2 domain by promoting refolding
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- Lateral self-association of VWF involves the Cys2431-Cys2453 disulfide/dithiol in the C2 domain
- (2011) T. Ganderton et al. BLOOD
- N-acetylcysteine reduces the size and activity of von Willebrand factor in human plasma and mice
- (2011) Junmei Chen et al. JOURNAL OF CLINICAL INVESTIGATION
- A shear-based assay for assessing plasma ADAMTS13 activity and inhibitors in patients with thrombotic thrombocytopenic purpura
- (2011) Yue Han et al. TRANSFUSION
- The importance of vicinal cysteines, C1669 and C1670, for von Willebrand factor A2 domain function
- (2010) B. M. Luken et al. BLOOD
- Disulfide bond reduction of von Willebrand factor by ADAMTS-13
- (2010) H.-C. YEH et al. JOURNAL OF THROMBOSIS AND HAEMOSTASIS
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- N-linked glycosylation of VWF modulates its interaction with ADAMTS13
- (2007) T. A. J. McKinnon et al. BLOOD
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