Molecular dynamics and free energy studies on the wild-type and mutated HIV-1 protease complexed with four approved drugs: mechanism of binding and drug resistance.
PMID: 19537723
2009
Journal of chemical information and modeling
Abstract: In agreement with virological and clinical data, the structural analysis showed that the single mutations V82A, I84V, and M46I are associated with higher energetic values for all analyzed complexes with respect to wild-type, indicating their decreased stability.
Mutation N155H in HIV-2 integrase confers high phenotypic resistance to raltegravir and impairs replication capacity.
Abstract: Genotypic analysis at month 8 with raltegravir, revealed the development of N155H resistant mutation along with other changes in the HIV-2 integrase: V72I, I84V, A153G, N160K and S163S/G.
Transmitted antiretroviral drug resistance among acute and recent HIV infections in North Carolina from 1998 to 2007.
Abstract: Several patterns were frequently observed, including mutations in the NC-p1 cleavage site in combination with I50L, V82A, and I84V within the protease and mutations within the p1-p6 cleavage site in combination with D30N, I50V, and I84V within the protease.
Minority variants associated with transmitted and acquired HIV-1 nonnucleoside reverse transcriptase inhibitor resistance: implications for the use of second-generation nonnucleoside reverse transcriptase inhibitors.
PMID: 19734799
2009
Journal of acquired immune deficiency syndromes (1999)
Result: The sample from PID 30062 - which contained four NRTI-resistance mutations - also had the following minority protease inhibitor (PI) resistance mutations: M46I (0.8%), I84V (0.9%), and L90M (0.9%) (data not shown).
Factors associated with the selection of mutations conferring resistance to protease inhibitors (PIs) in PI-experienced patients displaying treatment failure on darunavir.
PMID: 18039922
2008
Antimicrobial agents and chemotherapy
Abstract: The most common mutations that emerged at rebound included V32I (44%), I54M/L (24%), L33F (25%), I84V (21%), and L89V (12%).
Conformational analysis of TMC114, a novel HIV-1 protease inhibitor.
PMID: 18173253
2008
Journal of chemical information and modeling
Abstract: All 43 conformers were subject to both rigid and flexible ligand docking in the wild-type and a triple mutant (L63P/V82T/I84V) of HIV-1 protease.
Characterization of a novel human immunodeficiency virus type 1 protease inhibitor, A-790742.
PMID: 18212102
2008
Antimicrobial agents and chemotherapy
Abstract: During in vitro selection, A-790742 selected two primary mutations (V82L and I84V) along with L23I, L33F, K45I, A71V/A, and V77I in the pNL4-3 background and two other mutations (A71V and V82G) accompanied by M46I and L63P in the HIV-1 RF background.
Abstract: HIV-1 pNL4-3 clones with a single V82L or I84V mutation were phenotypically resistant to A-790742 and ritonavir.
Genotypic resistance profile and clinical progression of treatment-experienced HIV type 1-infected patients with virological failure.
PMID: 18240962
2008
AIDS research and human retroviruses
Abstract: In multivariable models adjusting for prior AIDS, baseline CD4 counts, HIV-1 RNA, and calendar year, viral resistance variables associated with increased hazards of clinical progression were the presence of reverse transcriptase substitution T215F (p = 0.002) and the presence of three or more protease substitutions among L33F/I/V, V82A/F/L/T, I84V, and L90M (p = 0.003).
Possible allosteric interactions of monoindazole-substituted P2 cyclic urea analogues with wild-type and mutant HIV-1 protease.
PMID: 18368496
2008
Journal of computer-aided molecular design
Abstract: Similar QSAR models were also observed for the biological activity of these molecules tested against a panel of mutant viruses including mutant strains with single amino acid substitution (I84V), double amino acid substitutions (I84V/V82F), and multiple amino acid changes corresponding to mutations observed in clinical isolates of patients treated with Ritonavir((R)).
HIV mutation literature information.
PMID: 
2009
Journal of chemical information and modeling
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