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Biochemistry|November 19, 1985
Structural evidence for leucine at the reactive site of heparin cofactor IIM J Griffith, C M Noyes, J A Tyndall, et al.The Journal of Biological Chemistry|September 10, 1979
The covalent differences between bovine alpha- and beta-thrombin. A structural explanation for the changes in catalytic activityR L Lundblad, C M Noyes, K G Mann, et al.The Journal of Biological Chemistry|April 15, 1986
Mechanism of the calcium-dependent self-association of bovine prothrombin. Use of a covalent cross-linking reagent to study the reactionR C Tarvers, C M Noyes, J K Tarvers, 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|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 Biological Chemistry|March 15, 1988
The reaction of bovine alpha-thrombin with tetranitromethane. Characterization of the modified proteinR L Lundblad, C M Noyes, G L Featherstone, et al.Analytical Biochemistry|December 1, 1986
Comparison of five techniques for the determination of protein content in mixed human salivaJ W Jenzano, S L Hogan, C M Noyes, et al.The Journal of Biological Chemistry|June 15, 1987
Identification of a lysyl residue in antithrombin which is essential for heparin bindingC B Peterson, C M Noyes, J M Pecon, et al.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.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.Pageof 3