Heparin Binding Domain of Human Antithrombin III Inferred from the Sequential Reduction of Its Three Disulfide Linkages
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. ANTITHROMBIN III AND HEPARIN
2. Mechanism of the anticoagulant action of heparin
3. Evidence by Chemical Modification for the Involvement of One or More Tryptophanyl Residues of Bovine Antithrombin in the Binding of High-Affinity Heparin
4. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin.
5. The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence.
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1. Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin;Journal of Biological Chemistry;2007-11
2. Characterization of molecular defect of 13387-9delG mutated antithrombin in inherited type I antithrombin deficiency;Blood Coagulation & Fibrinolysis;2005-03
3. Antithrombin gene mutation 5356?5364*delCTT with type I deficiency and early-onset thrombophilia and a brief review of the antithrombin ?-helix D molecular pathology;Annals of Hematology;2004-08-10
4. Five Novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis;International Journal of Hematology;2003-02
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