Bioorganic and Medicinal Chemistry Letters p. 67 - 72 (1997)
Update date:2022-08-03
Topics:
Lyle, Terry A.
Chen, Zhongguo
Appleby, Sandra D.
Freidinger, Roger M.
Gardell, Stephen J.
Lewis, S. Dale
Li, Ying
Lyle, Elizabeth A.
Lynch Jr., Joseph J.
Mulichak, Anne M.
Ng, Assunta S.
Naylor-Olsen, Adel M.
Sanders, William M.
Removal of the β-ketoamide functionality from L-370,518 (K(i) = 0.09 nM) provided a 5 nM K(i) inhibitor of thrombin: L-371,912. Comparison of the enzyme-inhibitor crystal structures suggests a possible explanation for the relatively small change in affini
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