Susceptibility to PNU-140690 (Tipranavir) of human immunodeficiency virus type 1 isolates derived from patients with multidrug resistance to other protease inhibitors.
PMID: 10770770
2000
Antimicrobial agents and chemotherapy
Abstract: The substitutions among the amino acid residues of the protease included L10I, K20R, L24I, M36I, N37D, G48V, I54V, L63P, I64V, A71V, V77I, V82A, I84V, and L90M.
In vitro resistance profile of the human immunodeficiency virus type 1 protease inhibitor BMS-232632.
PMID: 10952574
2000
Antimicrobial agents and chemotherapy
Abstract: An I84V change appeared to be an important substitution in the third strain used.
Polymorphism of HIV type 1 gag p7/p1 and p1/p6 cleavage sites: clinical significance and implications for resistance to protease inhibitors.
PMID: 10957718
2000
AIDS research and human retroviruses
Abstract: Natural polymorphism P453L might direct the PR resistance pathway through I84V instead of V82 mutation.
Abstract: Natural polymorphism P453L was strongly associated with the selection of PR I84V (OR 49.5; 95% CI 12-212) and selected against V82 mutation (OR 0.15; 95% CI 0.02-1.
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.
Abstract: Another contribution of the V82F/I84V to binding affinity originates from an increase in the energy penalty associated with the conformational change of the protease upon binding.
Abstract: The V82F
Abstract: The active site mutant V82F/I84V has been shown to lower the binding affinity of protease inhibitors in clinical use.
Abstract: The predominantly enthalpic effect of the V82F/I84V mutation is consistent with the idea that the introduction of the bulkier Phe side chain at position 82 and the Val side chain at position 84 distort the binding site and weaken van der Waals and other favorable interactions with inhibitors preshaped to the wild-type binding site.
Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1.
Abstract: In order to study drug resistance, the wild-type HIV-1 protease and the mutants R8Q, V32I, M46I, V82A, V82I, V82F, I84V, V32I/I84V and M46I/I84V were modeled with the inhibitors saquinavir and indinavir using the program AMMP.
Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.
Abstract: Sedimentation equilibrium studies were also carried out on several drug-resistant HIV-1 protease mutants: V82F, V82F/I84V, V82T/I84V, and L90M.
Real-time measurements of dark substrate catalysis.
Abstract: The method was applied to HIV-1 protease and to the V82F/I84V drug resistant mutant enzyme.
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.
Molecular mechanisms of resistance: free energy calculations of mutation effects on inhibitor binding to HIV-1 protease.
Abstract: The changes in the inhibitor binding constants due to the mutation of isoleucine to valine at position 84 of HIV-1 protease are calculated using molecular dynamics simulations.
HIV mutation literature information.
PMID: 
2000
Antimicrobial agents and chemotherapy
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