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Archives of Biochemistry and Biophysics|May 1, 1985
Activation of normal and abnormal human factor IX with trypsinD M Monroe, C M Noyes, D L Straight, et al.
Thrombosis Research|September 1, 1982
Cleavage and activation of human prothrombin by Echis carinatus venomE Briet, C M Noyes, H R Roberts, et al.
The Journal of Biological Chemistry|March 10, 1985
Structural and functional characteristics of activated human factor IX after chemical modification of gamma-carboxyglutamic acid residuesD L Straight, G B Sherrill, C M Noyes, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1983
Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145C M Noyes, M J Griffith, H R Roberts, et al.
Biochemical and Biophysical Research Communications|October 15, 1984
Inactivation of human blood coagulation factor X by chemical modification of gamma-carboxyglutamic acid residuesG B Sherrill, D L Straight, R G Hiskey, et al.
Biochemistry|September 25, 1984
Interaction of substrates with glutamine synthetase after limited proteolysisD M Monroe, C M Noyes, R L Lundblad, et al.
The Journal of Clinical Investigation|December 1, 1981
Characterization of the defect in activation of factor IX Chapel Hill by human factor XIaK M Braunstein, C M Noyes, M J Griffith, et al.
Biochemistry|December 31, 1985
Comparison of lipid binding and kinetic properties of normal, variant, and gamma-carboxyglutamic acid modified human factor IX and factor IXaM E Jones, M J Griffith, D M Monroe, et al.
The Journal of Clinical Investigation|January 1, 1985
Characterization of the clotting activities of structurally different forms of activated factor IX. Enzymatic properties of normal human factor IXa alpha, factor IXa beta, and activated factor IX Chapel HillM J Griffith, L Breitkreutz, H Trapp, et al.
The Journal of Biological Chemistry|February 25, 1985
Reactive site peptide structural similarity between heparin cofactor II and antithrombin IIIM J Griffith, C M Noyes, F C Church
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