Transition-State Affinity as a Basis for the Design of Enzyme Inhibitors-Reference-Cited by-同舟云学术

Transition-State Affinity as a Basis for the Design of Enzyme Inhibitors

Author:

Wolfenden Richard

Publisher

Springer US

Link

Reference55 articles.

1. V. Henri, Lois Generales De L’Action Des Diastases, Hermann, Paris (1903).

2. H. L. Segal, in: The Enzymes (P. D. Boyer, H. Lardy, and K. Myrbäck, eds.), Vol. 1, pp. 1–48, Academic Press, New York (1959).

4. W. P. Jencks, in: Current Aspects of Biochemical Energetics ( N. O. Kaplan and E. P. Kennedy, eds.), pp. 273–298, Academic Press, New York (1966).

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