Design of novel HIV-1 protease inhibitors incorporating isophthalamide-derived P2-P3 ligands: Synthesis, biological evaluation and X-ray structural studies of inhibitor-HIV-1 protease complex.
Ghosh, Arun K; Brindisi, Margherita; Nyalapatla, Prasanth R; Takayama, Jun; Ella-Menye, Jean-Rene; Yashchuk, Sofiya; Agniswamy, Johnson; Wang, Yuan-Fang; Aoki, Manabu; Amano, Masayuki; Weber, Irene T; Mitsuya, Hiroaki.
Bioorg Med Chem
; 25(19): 5114-5127, 2017 10 01.
Artigo em Inglês | MEDLINE | ID: mdl-28434781
Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D↑G↑S mutant in the South African HIV-1 subtype C protease.
NMR and MD studies combined to elucidate inhibitor and water interactions of HIV-1 protease and their modulations with resistance mutations.
Fast and accurate determination of the relative binding affinities of small compounds to HIV-1 protease using non-equilibrium work.
Pressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach.
Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease.
Structure-based design, synthesis, X-ray studies, and biological evaluation of novel HIV-1 protease inhibitors containing isophthalamide-derived P2-ligands.
SMD-Based Interaction-Energy Fingerprints Can Predict Accurately the Dissociation Rate Constants of HIV-1 Protease Inhibitors.
Characterization of Nine Compounds Isolated from the Acid Hydrolysate of <i>Lonicera fulvotomentosa</i> Hsu et S. C. Cheng and Evaluation of Their In Vitro Activity towards HIV Protease.
Sub-picomolar Inhibition of HIV-1 Protease with a Boronic Acid.
Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.