The role of the ADAMTS13 cysteine-rich domain in VWF binding and proteolysis
Author:
Affiliation:
1. Centre for Haematology, Faculty of Medicine, Imperial College London, Hammersmith Hospital Campus, London, United Kingdom
Abstract
Publisher
American Society of Hematology
Subject
Cell Biology,Hematology,Immunology,Biochemistry
Link
http://ashpublications.org/blood/article-pdf/125/12/1968/1383674/1968.pdf
Reference34 articles.
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3. Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation.;Moake;J Clin Invest,1986
4. Shear-induced unfolding triggers adhesion of von Willebrand factor fibers.;Schneider;Proc Natl Acad Sci USA,2007
5. Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura.;Levy;Nature,2001
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