Mutation of Protease Domain Residues Lys37-39 in Human Protein C Inhibits Activation by the Thrombomodulin-Thrombin Complex without Affecting Activation by Free Thrombin
Open Access
- 1 September 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (37) , 22285-22288
- https://doi.org/10.1074/jbc.271.37.22285
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- New Molecular Insights into the Genetics of Thrombophilia. Resistance to Activated Protein C Caused by Arg506 to Gin Mutation in Factor V as a Pathogenic Risk Factor for Venous ThrombosisThrombosis and Haemostasis, 1995
- Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogenProtein Science, 1994
- Charge reversal at the P3′ position in protein C optimally enhances thrombin affinity and activation rateProtein Science, 1994
- Enhancing protein C interaction with thrombin results in a clot-activated anticoagulantNature, 1992
- Isolation and Characterization of a Mouse Protein C cDNAThe Journal of Biochemistry, 1992
- Mapping active sites of blood coagulation serine proteases—activated protein C and thrombin—on simple graphics modelsJournal of Molecular Graphics, 1989
- The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAsNucleic Acids Research, 1985
- Cloning and sequencing of liver cDNA coding for bovine protein C.Proceedings of the National Academy of Sciences, 1984
- Preparation and properties of bovine factor VIII (antihemophilic factor)Biochemistry, 1980
- Anticoagulant properties of bovine plasma protein C following activation by thrombinBiochemistry, 1977