Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds (original) (raw)

Design and synthesis of HIV-1 protease inhibitors. Novel tetrahydrofuran P2/P2′-groups interacting with Asp29/30 of the HIV-1 protease. Determination of binding from X-ray crystal structure of inhibitor protease complex

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Potent New Antiviral Compound Shows Similar Inhibition and Structural Interactions with Drug Resistant Mutants and Wild Type HIV-1 Protease †

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1 Evaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed to be Robust against Drug Resistance

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Conformationally constrained HIV-1 protease inhibitors

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Inhibitor binding at the protein interface in crystals of a HIV1 protease complex

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Evaluating the substrate-envelope hypothesis: structural analysis of novel HIV-1 protease inhibitors designed to be robust against drug resistance

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The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations

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Structure Based Design of Inhibitors of Aspartic Protease of HIV-1

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