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Biochemistry|May 16, 1995
Factor Xa-factor Va complex assembles in two dimensions with unexpectedly high affinity: an experimental and theoretical approachJ Ye, C T EsmonThe Journal of Biological Chemistry|July 8, 1994
Glycosaminoglycan contributions to both protein C activation and thrombin inhibition involve a common arginine-rich site in thrombin that includes residues arginine 93, 97, and 101J Ye, A R Rezaie, C T EsmonThe Journal of Biological Chemistry|February 5, 1993
The chondroitin sulfate moiety of thrombomodulin binds a second molecule of thrombinJ Ye, C T Esmon, A E JohnsonBiochemistry|July 22, 1997
Influence of Arginines 93, 97, and 101 of thrombin to its functional specificityX He, J Ye, C T Esmon, et al.The Journal of Biological Chemistry|December 5, 1991
The active site of thrombin is altered upon binding to thrombomodulin. Two distinct structural changes are detected by fluorescence, but only one correlates with protein C activationJ Ye, N L Esmon, C T Esmon, et al.The Journal of Biological Chemistry|December 15, 1991
Proteolytic formation of either of the two prothrombin activation intermediates results in formation of a hirugen-binding siteL W Liu, J Ye, A E Johnson, et al.The Journal of Biological Chemistry|June 5, 1992
The fifth and sixth growth factor-like domains of thrombomodulin bind to the anion-binding exosite of thrombin and alter its specificityJ Ye, L W Liu, C T Esmon, et al.Journal of Autoimmunity|September 2, 2000
The anticoagulant and anti-inflammatory roles of the protein C anticoagulant pathwayC T EsmonCritical Care (London, England)|May 31, 2001
The normal role of Activated Protein C in maintaining homeostasis and its relevance to critical illnessC T EsmonCritical Care Medicine|July 11, 2001
Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammationC T EsmonPageof 138