The effect of bovine thrombomodulin on the specificity of bovine thrombin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Complex formation between thrombin and thrombomodulin inhibits both thrombin-catalyzed fibrin formation and factor V activation.
2. Thrombomodulin blocks the ability of thrombin to activate platelets.
3. Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C.
4. Anticoagulant properties of bovine plasma protein C following activation by thrombin
5. The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V
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1. Exosite 2-Directed Ligands Attenuate Protein C Activation by the Thrombin–Thrombomodulin Complex;Biochemistry;2017-06-07
2. Investigating the Role of T7 and T12 Residues on the Biological Properties of Thrombin-Binding Aptamer: Enhancement of Anticoagulant Activity by a Single Nucleobase Modification;Journal of Medicinal Chemistry;2012-11-19
3. Meizothrombin Is an Unexpectedly Zymogen-like Variant of Thrombin;Journal of Biological Chemistry;2012-08
4. The effects of exosite occupancy on the substrate specificity of thrombin;Archives of Biochemistry and Biophysics;2009-09
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