A biophysical view on von Willebrand factor activation
Author:
Affiliation:
1. Department of Physics and Center for NanoScienceLMU MunichMunichGermany
2. Department of Pediatric Hematology and OncologyUniversity Medical Center Hamburg‐EppendorfHamburgGermany
Publisher
Wiley
Subject
Cell Biology,Clinical Biochemistry,Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcp.25887
Reference76 articles.
1. Shear-Flow-Induced Unfolding of Polymeric Globules
2. Force-Sensitive Autoinhibition of the von Willebrand Factor Is Mediated by Interdomain Interactions
3. Conformational Stability and Domain Unfolding of the Von Willebrand Factor A Domains
4. Changes in Thermodynamic Stability of von Willebrand Factor Differentially Affect the Force-Dependent Binding to Platelet GPIbα
5. 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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