Mutations in the catalytic domain of factor IX that are related to the subclass hemophilia Bm
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00076a004
Reference19 articles.
1. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
2. Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX.
3. Intramolecular Reorientational Motion in Trypsinogen Studied by Perturbed Angular Correlation ofHg199mLabels
4. Hydrogen bonding and biological specificity analysed by protein engineering
5. Mapping of monoclonal antibodies to human factor IX
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1. Crippling down factor IX for therapeutic gain;Journal of Thrombosis and Haemostasis;2023-12
2. Role of glycine 221 in catalytic activity of hyaluronan-binding protein 2;Journal of Biological Chemistry;2017-04
3. Next generation FIX muteins with FVIII-independent activity for alternative treatment of hemophilia A;Journal of Thrombosis and Haemostasis;2014-10-15
4. Factor IX Deficiency or Hemophilia B: Clinical Manifestations and Management;Hemostasis and Thrombosis;2014-02-14
5. Potent Anticoagulant Aptamer Directed against Factor IXa Blocks Macromolecular Substrate Interaction;Journal of Biological Chemistry;2012-04
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