Structural analysis of factor IX protein variants to predict functional aberration causing haemophilia B
Author:
Publisher
Wiley
Subject
Genetics(clinical),Hematology,General Medicine
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2516.2008.01788.x/fullpdf
Reference16 articles.
1. A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S;Di Scipio;Biochemistry,1977
2. Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX;Freedman;Biochemistry,1995
3. Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy;Freedman;J Biol Chem,1995
4. Crystal structure of Mg2+ and Ca2+ bound Gla domain of factor IX complexed with binding protein;Shikatamoto;J Biol Chem,2003
5. Crystal structure of Ca2+ stabilized human factor IX Gla domain bound to a conformation specific anti-factor IX antibody;Huang;J Biol Chem,2004
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1. Impact of formaldehyde, acetaldehyde, and N-(3-(Dimethylamino)propyl)methacrylamide on the efficacy of the human derived coagulation factor IX;International Journal of Pharmaceutics;2023-03
2. F8/F9 variants in the population-based PedNet Registry cohort compared with locus-specific genetic databases of the European Association for Haemophilia and Allied Disorders and the Centers for Disease Control and Prevention Hemophilia A or Hemophilia B Mutation Project;Research and Practice in Thrombosis and Haemostasis;2023-01
3. In silico analysis of missense mutations in exons 1–5 of the F9 gene that cause hemophilia B;BMC Bioinformatics;2019-06-28
4. Hemophilia B: molecular pathogenesis and mutation analysis;Journal of Thrombosis and Haemostasis;2015-05-18
5. In silicoanalyses of missense mutations in coagulation factor VIII: identification of severity determinants of haemophilia A;Haemophilia;2015-04-09
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