A molten globule intermediate of the Von Willebrand factor A1 domain firmly tethers platelets under shear flow
Author:
Affiliation:
1. Departments of Internal Medicine Division of Hematology; Mayo Clinic; Rochester Minnesota
2. Biochemistry and Molecular Biology; Mayo Clinic; Rochester Minnesota
Funder
National Heart Lung and Blood Institute of the National Institutes of Health
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.24464/fullpdf
Reference49 articles.
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2. C1272S: a new candidate mutation in type 2A von Willebrand disease that disrupts the disulfide loop responsible for the interaction of VWF with platelet GP Ib-IX;Penas;Am J Hematol,2004
3. Gene defects in 150 unrelated French cases with type 2 von Willebrand disease: from the patient to the gene. INSERM Network on Molecular Abnormalities in von Willebrand Disease;Meyer;Thromb. Haemost,1997
4. Defects in type IIA von Willebrand disease: a cysteine 509 to arginine substitution in the mature von Willebrand factor disrupts a disulphide loop involved in the interaction with platelet glycoprotein Ib-IX;Lavergne;Br J Haematol,1992
5. Disulfide bond requirements for assembly of the platelet glycoprotein Ib-binding domain of von Willebrand factor;Azuma;J Biol Chem,1993
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