Site-directed mutagenesis of alanine-382 of human antithrombin III
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(91)80305-M/fullpdf
Reference20 articles.
1. Anticoagulant Action of Heparin
2. T.E. Petersen G. Dudek-Wojciechowska L. Sottrup-Jensen S. Magnusson D. Collen The Physiological Inhibitor of Coagulation and Fibrinolysis 1979 Elsevier Amsterdam 42 54
3. The Molecular Pathology of Inherited Human Antithrombin III Deficiency
4. Molecular Heterogeneity of Inherited Antithrombin III Deficiency
5. Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity
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1. Antithrombin;Advances in Experimental Medicine and Biology;1997
2. Structural basis for serpin inhibitor activity;Proteins: Structure, Function, and Genetics;1995-07
3. Regulation of Thrombin Activity by Antithrombin and Heparin;Seminars in Thrombosis and Hemostasis;1994-10
4. Antithrombin: The Principal Inhibitor of Thrombin;Seminars in Thrombosis and Hemostasis;1994-10
5. Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins;FEBS Letters;1994-07-04
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