The Role of Cleavage of the Light Chain at Positions Arg1689 or Arg1721 in Subunit Interaction and Activation of Human Blood Coagulation Factor VIII
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference49 articles.
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4. Isolation and characterization of human factor VIII: molecular forms in commercial factor VIII concentrate, cryoprecipitate, and plasma.
5. Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
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1. The C-terminal acidic region in the A1 domain of factor VIII facilitates thrombin-catalyzed activation and cleavage at Arg<sup>372</sup>;Japanese Journal of Thrombosis and Hemostasis;2023
2. Acidic Region Residues 1680–1684 in the A3 Domain of Factor VIII Contain a Thrombin-Interactive Site Responsible for Proteolytic Cleavage at Arg1689;Thrombosis and Haemostasis;2021-02-16
3. The C‐terminal acidic region in the A1 domain of factor VIII facilitates thrombin‐catalyzed activation and cleavage at Arg 372;Journal of Thrombosis and Haemostasis;2020-12-26
4. Discordance between platelet‐supported and vesicle‐supported factor VIII activity in the presence of anti‐C2 domain inhibitory antibodies;Journal of Thrombosis and Haemostasis;2020-10-21
5. A mathematical model of coagulation under flow identifies factor V as a modifier of thrombin generation in hemophilia A;Journal of Thrombosis and Haemostasis;2019-11
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