Abstract: Primary-resistance mutations associated with protease inhibitors (V82A, L90M) were detected in three (4%) of 70 individuals; two of these had also RTI-resistance mutations.
Genetic variation and susceptibilities to protease inhibitors among subtype B and F isolates in Brazil.
PMID: 9925514
1999
Antimicrobial agents and chemotherapy
Abstract: The frequency of critical PI resistance substitutions (amino acid changes D30N, V82A/F/T, I84V, N88D, and L90M) among Brazilian isolates is very low (mean, 2.5%), and the associated secondary substitutions (amino acid positions 10L, 20K, 36M, 46M, 48G, 54I, 63P, 71A, and 77A) are infrequent.
Estimate of the frequency of human immunodeficiency virus type 1 protease inhibitor resistance within unselected virus populations in vitro.
PMID: 9527815
1998
Antimicrobial agents and chemotherapy
Abstract: Two variants with single mutations responsible for drug resistance (V82A and N88S) were quantifiably isolated after only one round of replication, yielding a crude frequency estimate of at least 1 SC-55389A-resistant variant per 3.5 x 10(5) wild-type infectious units.
Genotypic changes in human immunodeficiency virus type 1 associated with loss of suppression of plasma viral RNA levels in subjects treated with ritonavir (Norvir) monotherapy.
Abstract: A virologic response beyond 60 days was not observed unless plasma HIV RNA levels were suppressed below 2,000 copies/ml, consistent with estimates from V82A doubling times for selection of a single resistance mutation to dominate the replicating population.
Abstract: Doubling times of the V82A mutant virus were estimated to be 2.4 to 4.8 days.
Abstract: The concomitant acquisition of an L63P/A mutation with the V82A/F mutation at the time when plasma RNA levels rebounded suggests a role for the L63P/A mutation in improving the fitness of the V82A/F mutation.
Abstract: The relative fitness of the protease V82A ritonavir resistance mutation and PMID: 9573309
1998
Journal of virology
Abstract: In addition, all six patients who developed the G48V mutation during saquinavir therapy developed the V82A mutation either on continued saquinavir or after a switch to nelfinavir or indinavir.
Resistance to HIV protease inhibitors: a comparison of enzyme inhibition and antiviral potency.
Abstract: Four of the five mutations studied (V82F, V82A, I84V, and V82F/I84V) had been identified as conferring resistance during in vitro selection using a protease inhibitor.
Predicting structural effects in HIV-1 protease mutant complexes with flexible ligand docking and protein side-chain optimization.
Abstract: Flexible ligand docking and optimization of mobile protein side-chains have been performed to predict structural effects in the V32I/I47V/V82I HIV-1 protease mutant bound with the SB203386 ligand and in the V82A HIV-1 protease mutant bound with the A77003 ligand.
Resistance mutations in protease and reverse transcriptase genes of human immunodeficiency virus type 1 isolates from patients with combination antiretroviral therapy failure.
PMID: 9780274
1998
The Journal of infectious diseases
Abstract: The most commonly observed PR mutations were L10I, V82A/T/F, and L90M.
An Escherichia coli expression assay and screen for human immunodeficiency virus protease variants with decreased susceptibility to indinavir.
PMID: 9835523
1998
Antimicrobial agents and chemotherapy
Abstract: The discovered HIV protease variants contain amino acid substitutions commonly associated with indinavir resistance in clinical isolates, including the substitutions L90M, L63P, I64V, V82A, L24I, and I54T.
Structure-based thermodynamic analysis of HIV-1 protease inhibitors.
Abstract: Furthermore, the formalism correctly predicts the observed change in inhibition constant for the complex of A77003 and the resistant protease mutant V82A, for which the high-resolution structure is also available.
HIV mutation literature information.
PMID: 
1999
Lancet (London, England)
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