Toward the Design of Mutation-Resistant Enzyme Inhibitors: Further Evaluation of the Substrate Envelope Hypothesis

Chemical Biology and Drug Design- United Kingdom

doi 10.1111/j.1747-0285.2009.00851.x

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September 1, 2009

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Wiley

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Toward the Design of Mutation-Resistant Enzyme Inhibitors: Further Evaluation of the Substrate Envelope Hypothesis

Chemical Biology and Drug Design- United Kingdom

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

HIV-1 Protease Inhibitors From Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant Variants

Further Evaluation of the Tetrodotoxin-Resistant Circadian Pacemaker in the Suprachiasmatic Nuclei

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Structure-Based Design, Synthesis, and Biological Evaluation of Non-Acyl Sulfamate Inhibitors of the Adenylate-Forming Enzyme MenE

An Application of Photoactivatable Substrate for the Evaluation of Epithelial-Mesenchymal Transition Inhibitors

HIV1 Protease Inhibitors Incorporating Stereochemically Defined P2 Ligands to Optimize Hydrogen Bonding in the Substrate Envelope

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