Abstract: Using Sanger sequencing, two TDR mutations, M46L and I84V, were each detected as mixtures at a frequency of 1.04% (1/96).
Table: I84V
Figure: All positive pyrosequencing reads containing M46L (a) and I84V (b) were analyzed with Sanger sequences from the 96 specimens using Neighbour-Joining (K-2-P) with 100 bootstraps.
Figure: Two TDR mutations, M46L and I84V, were detected by conventional Sanger sequencing, each in one of the 96 examined specimens.
Discussion: Pyrosequencing reads of both th
Discussion: The dendograms for the M46L and I84V mutations detected by pyrosequencing were unique among those SDRM found at frequencies of less than 1%.
HIV-1 protease inhibitors with a transition-state mimic comprising a tertiary alcohol: improved antiviral activity in cells.
PMID: 19961222
2010
Journal of medicinal chemistry
Abstract: The synthesis of 25 new and optically pure HIV-1 protease inhibitors is reported, along with methods for elongation of the inhibitor P1' side chain using microwave-accelerated, palladium-catalyzed cross-coupling reactions, the biological evaluation, and X-ray data obtained from one of the most potent analogues cocrystallized with both the wild type and the L63P, V82T, I84 V mutant of the HIV-1 protease.
Design and synthesis of novel P2 substituents in diol-based HIV protease inhibitors.
PMID: 19926360
2010
European journal of medicinal chemistry
Abstract: These inhibitors were also tested against an HIV protease inhibitor resistant strain carrying the M46I, V82F, and I84V mutations.
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.
PMID: 19910081
2010
European journal of medicinal chemistry
Abstract: Our results show I50V and V82A have larger structural changes than I84V compared with WT.
Abstract: The reduced van der Waals energy explains the drug resistance of I84V to GRL-98065.
Abstract: The single mutations I50V, V82A and I84V are considered as the key residue mutations of the HIV-1 protease drug resistance.
Accurate ensemble molecular dynamics binding free energy ranking of multidrug-resistant HIV-1 proteases.
PMID: 20384328
2010
Journal of chemical information and modeling
Abstract: Multidrug resistance to lopinavir is enthalpically driven and increases through a decrease in the protein-ligand van der Waals interaction, principally due to the V82A/I84V mutation, and an increase in net electrostatic repulsion due to water-mediated disruption of protein-ligand interactions in the catalytic region.
Prevalence and clinical significance of HIV drug resistance mutations by ultra-deep sequencing in antiretroviral-naive subjects in the CASTLE study.
Abstract: The PR(I84V)-APV complex had lost hydrophobic contacts with APV, the PR(V32I)-APV complex showed increased hydrophobic contacts within the hydrophobic cluster and the PR(I50V) complex had weaker polar and hydrophobic interactions with APV.
Abstract: The observed structural changes in PR(I84V)-APV, PR(V32I)-APV and PR(I50V)-APV were related to their reduced inhibition by APV of six-, 10- and 30-fold, respectively, relative to wild-type PR.
Abstract: The structural and kinetic effects of amprenavir (APV), a clinical HIV
Decomposing the energetic impact of drug resistant mutations in HIV-1 protease on binding DRV.
PMID: 20543885
2010
Journal of chemical theory and computation
Figure: B) The perturbation of Ile84 to Val84.
Figure: Perturbation of Val82 to Thr and Ile84 to Val.
Discussion: Comparing the trajectories from MD simulations on the wild-type protease and the V82F/I84V protease variant, Perryman et al.
Discussion: In the case of the ACT (V82T, I84V) mutant here, the TI method not only gave the more accurate predicted energy than the MM-PB/GBSA method, but also had better
Discussion: found that the mutation I84V has decreased the vdW interaction between APV and the drug-resistant variant, which might account for the loss of binding affinity between APV and the drug-resistant variant.
Novel protease inhibitors (PIs) containing macrocyclic components and 3(R),3a(S),6a(R)-bis-tetrahydrofuranylurethane that are potent against multi-PI-resistant HIV-1 variants in vitro.
PMID: 20439612
2010
Antimicrobial agents and chemotherapy
Abstract: At passage 50 with GRL-216 (the HIV isolate selected with GRL-216 at up to 0.16 microM [HIV216-0.16 microM]), HIV-1NL4-3 containing the L10I, L24I, M46L, V82I, and I84V mutations remained relatively sensitive to PIs, including darunavir, with the EC50s being 3- to 8-fold-greater than the EC50 of each drug for HIV-1NL4-3.
HIV mutation literature information.
PMID: 
2010
PloS one
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