Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, “fibrinogen Osaka II”. Evidence for a unique solitary cystine structure at the mutation site.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference49 articles.
1. Evidence for Localization of Polymerization Sites in Fibrinogen
2. Fibrinogen Detroit - an abnormal fibrinogen with non-functional NH2-terminal polymerization domain
3. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the .gamma. chain
4. γ-γ Cross-linking sites in human and bovine fibrin
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1. A novel fibrinogen variant – Liberec: dysfibrinogenaemia associated with γ Tyr262Cys substitution;European Journal of Haematology;2008-08
2. A new electrophoretic variant of fibrinogen associated with venous thromboembolism, fibrinogen Bordeaux A Arg439Cys;Journal of Thrombosis and Haemostasis;2008-08
3. A classification of the fibrin network structures formed from the hereditary dysfibrinogens;Journal of Thrombosis and Haemostasis;2006-08
4. Recombinant fibrinogen, gamma275ArgCys, exhibits formation of disulfide bond with cysteine and severely impaired D:D interactions;Journal of Thrombosis and Haemostasis;2004-03
5. Identification of a dysfibrinogenemia of γR275C (Fibrinogen Fukushima);Clinica Chimica Acta;2002-11
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