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注意:仅列出部分参考文献,下载原文获取全部文献信息。P3-P3′ Residues Flanking Scissile Bonds in Factor VIII Modulate Rates of Substrate Cleavage and Procofactor Activation by Thrombin
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Acidic residues C-terminal to the A2 domain facilitate thrombin-catalyzed activation of factor VIII
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Identification of a thrombin-interactive site within the FVIII A2 domain that is responsible for the cleavage at Arg372
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Tyr346 -> Cys mutation results in factor VIII : C assay discrepancy and a normal bleeding phenotype - is this mild haemophilia A?
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Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 site
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Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain
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Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain
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JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Mechanisms of factor Xa-catalyzed cleavage of the factor VIIIa A1 subunit resulting in cofactor inactivation
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JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Structural requirements for the activation of human factor VIII by thrombin
T Myles et al.
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A Tyr346→Cys substitution in the interdomain acidic region a1 of factor VIII in an individual with factor VIII:C assay discrepancy
AD Mumford et al.
BRITISH JOURNAL OF HAEMATOLOGY (2002)
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PJ Fay et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Circulating factor VIII immune complexes in patients with type 2 acquired hemophilia A and protection from activated protein C-mediated proteolysis
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BLOOD (2001)
Factor VIIIC2 domain contains the thrombin-binding site responsible for thrombin-catalyzed cleavage at Arg1689
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