Cleavage of Factor VIII Heavy Chain Is Required for the Functional Interaction of A2 Subunit with Factor IXa
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Expression of active human factor VIII from recombinant DNA clones
2. Molecular cloning of a cDNA encoding human antihaemophilic factor
3. Structure of human factor VIII
4. Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein
5. The size of human factor VIII heterodimers and the effects produced by thrombin
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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. The factor VIII heavy chain improves emicizumab-tenase assembly to enhance the factor VIII-mimicking cofactor activity;Thrombosis Research;2018-06
5. An in silico and in vitro approach to elucidate the impact of residues flanking the cleavage scissile bonds of FVIII;PLOS ONE;2017-07-06
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