FVIII stabilization: VWF D′D3 will do
Author:
Affiliation:
1. QUEEN’S UNIVERSITY
Publisher
American Society of Hematology
Subject
Cell Biology,Hematology,Immunology,Biochemistry
Link
http://ashpublications.org/blood/article-pdf/124/3/313/1464609/313.pdf
Reference9 articles.
1. A von Willebrand factor fragment containing the D’D3 domains is sufficient to stabilize coagulation factor VIII in mice.;Yee;Blood,2014
2. A major factor VIII binding domain resides within the amino-terminal 272 amino acid residues of von Willebrand factor.;Foster;J Biol Chem,1987
3. The acidic region of the factor VIII light chain and the C2 domain together form the high affinity binding site for von willebrand factor.;Saenko;J Biol Chem,1997
4. A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function.;Lü;Blood,2011
5. Type 2N von Willebrand disease: clinical manifestations, pathophysiology, laboratory diagnosis and molecular biology.;Mazurier;Best Pract Res Clin Haematol,2001
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4. Noncovalent stabilization of the factor VIII A2 domain enhances efficacy in hemophilia A mouse vascular injury models;Blood;2015-01-08
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