Replacing the Factor VIII C1 Domain with a Second C2 Domain Reduces Factor VIII Stability and Affinity for Factor IXa
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Activation of factor VIII and mechanisms of cofactor action;Fay;Blood Rev,2004
2. Activation of the factor VIIIa-factor IXa enzyme complex of blood coagulation by membranes containing phosphatidyl-l-serine;Gilbert;J. Biol. Chem,1996
3. Specific membrane binding of factor VIII is mediated by O-phospho-l-serine, a moiety of phosphatidylserine;Gilbert;Biochemistry,1993
4. Four hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs;Gilbert;J. Biol. Chem,2002
5. Contributions of Asn2198, Met2199, and Phe2200 in the factor VIII C2 domain to cofactor activity, phospholipid-binding, and von Willebrand factor-binding;Lewis;Thromb. Haemost,2003
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1. Structural basis for inhibition of coagulation factor VIII reveals a shared antigenic hotspot on the C1 domain;Journal of Thrombosis and Haemostasis;2024-09
2. The emicizumab-bridged ternary complex with activated factor IX and factor X evaluated by fluorescence resonance energy transfer;Thrombosis Research;2024-05
3. SAXS analysis of the intrinsic tenase complex bound to a lipid nanodisc highlights intermolecular contacts between factors VIIIa/IXa;Blood Advances;2022-05-31
4. SAXS analysis of intrinsic tenase complex bound to lipid nanodisc highlights intermolecular contacts between factors VIIIa/IXa;2021-07-10
5. Unique surface‐exposed hydrophobic residues in the C1 domain of factor VIII contribute to cofactor function and von Willebrand factor binding;Journal of Thrombosis and Haemostasis;2019-11-28
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