Increasing Hydrophobicity or Disulfide Bridging at the Factor VIII A1 and C2 Domain Interface Enhances Procofactor Stability
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Activation of factor VIII and mechanisms of cofactor action
2. Structure of the C2 domain of human factor VIII at 1.5 Å resolution
3. The tertiary structure and domain organization of coagulation factor VIII
4. Crystal Structure of Human Factor VIII: Implications for the Formation of the Factor IXa-Factor VIIIa Complex
5. Factor VIII Lacking the C2 Domain Retains Cofactor Activity in Vitro
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1. Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway;Journal of Thrombosis and Haemostasis;2016-03-21
2. Changes in the Factor VIII C2 domain upon membrane binding determined by hydrogen–deuterium exchange MS;Biochemical Journal;2014-07-10
3. Cofactor Activity in Factor VIIIa of the Blood Clotting Pathway Is Stabilized by an Interdomain Bond between His281 and Ser524 Formed in Factor VIII;Journal of Biological Chemistry;2014-05
4. Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa;Thrombosis and Haemostasis;2014-03-06
5. Genetics and classification of hemophilia;Contemporary Approaches to Hemophilia;2014-02
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