Coagulation factor VIII: its molecular structure and functional mechanism
نویسندگان
چکیده
منابع مشابه
Coagulation Therapy in Hemophilia A and its Relation to Factor VIII Inhibitor in Northeast of Iran
متن کامل
Molecular defects in coagulation Factor VIII and their impact on Factor VIII function.
Molecular defects in Factor VIII (FVIII), such as haemophilia A-related mutations or denaturative conformational changes, may affect the stability of FVIII as well as its interactions with physiological activators, von Willebrand Factor, phospholipid, or conformationally sensitive antibodies. We summarize the contemporary assays which allow identification of impaired functional interactions of ...
متن کاملThe tertiary structure and domain organization of coagulation factor VIII.
Factor VIII (fVIII) is a serum protein in the coagulation cascade that nucleates the assembly of a membrane-bound protease complex on the surface of activated platelets at the site of a vascular injury. Hemophilia A is caused by a variety of mutations in the factor VIII gene and typically requires replacement therapy with purified protein. We have determined the structure of a fully active, rec...
متن کاملcoagulation therapy in hemophilia a and its relation to factor viii inhibitor in northeast of iran
0
متن کاملRevisiting the mechanism of coagulation factor XIII activation and regulation from a structure/functional perspective
The activation and regulation of coagulation Factor XIII (FXIII) protein has been the subject of active research for the past three decades. Although discrete evidence exists on various aspects of FXIII activation and regulation a combinatorial structure/functional view in this regard is lacking. In this study, we present results of a structure/function study of the functional chain of events f...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Japanese Journal of Thrombosis and Hemostasis
سال: 2014
ISSN: 0915-7441,1880-8808
DOI: 10.2491/jjsth.25.99