Associated Papers
Multiple Molecular Dynamics Simulations of the Inhibitor GRL-02031 Complex with Wild Type and Mutant HIV-1 Protease Reveal the Binding and Drug-Resistance Mechanism.
Wang R et al.
Langmuir : the Acs Journal of Surfaces and Colloids, 2020
Halogen Bond Interactions of Novel HIV-1 Protease Inhibitors (PI) (GRL-001-15 and GRL-003-15) with the Flap of Protease Are Critical for Their Potent Activity against Wild-Type HIV-1 and Multi-PI-Resistant Variants.
Hattori SI et al.
Antimicrobial Agents and Chemotherapy, 2019
Computational Studies of a Mechanism for Binding and Drug Resistance in the Wild Type and Four Mutations of HIV-1 Protease with a GRL-0519 Inhibitor.
Hu G et al.
International Journal of Molecular Sciences, 2016
Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.
Yu Y et al.
Scientific Reports, 2015
Disubstituted Bis-THF Moieties as New P2 Ligands in Nonpeptidal HIV-1 Protease Inhibitors (II).
Hohlfeld K et al.
Journal of Medicinal Chemistry, 2015
Loss of protease dimerization inhibition activity of darunavir is associated with the acquisition of resistance to darunavir by HIV-1.
Koh Y et al.
Journal of Virology, 2011
Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.
Hu GD et al.
European Journal of Medicinal Chemistry, 2010
HIV-1 Protease: Structural Perspectives on Drug Resistance.
Weber IT et al.
Viruses, 2009
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