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 the SDR mutations, M46L and I84V, identified by Sanger sequencing, were found be tightly clustered and almost exclusively associated with the mutant Sanger sequence
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.
A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
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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