Design of Potent Aspartic Protease Inhibitors to Treat Various Diseases
Author:
Publisher
Wiley
Subject
Drug Discovery,Pharmaceutical Science
Reference96 articles.
1. Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine
2. A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease
3. Rigid backbone moiety of KNI-272, a highly selective HIV protease inhibitor: methanol, acetone and dimethylsulfoxide solvated forms of 3-[3-benzyl-2-hydroxy-9-(isoquinolin-5-yloxy)-6-methylsulfanylmethyl-5,8-dioxo-4,7-diazanonanoyl]-N-tert-butyl-1,3-thiazolidine-4-carboxamide
4. Structure of the aspartic protease plasmepsin 4 from the malarial parasitePlasmodium malariaebound to an allophenylnorstatine-based inhibitor
5. Compensating Enthalpic and Entropic Changes Hinder Binding Affinity Optimization
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