Result: According to Figure 7B, it is observed that the van der Waals interactions of I47V, V32'I and V82'I in PR2 with APV are decreased by 1.42, 1.37 and 0.49 kcal mol-1 relative to PR1, respectively.
Result: As shown in Figure 7A, the van der Waals interactions of the mutated residues V32I, I47V, V32'I and I47'V in PR2 with DRV are decreased by 0.49, 0.86, 0.69 and 0.26 kcal mol-1 compared to PR1, respectively.
Result: Previous studies have proved that the above regions in PR2 have three key mutations V32I, I47V and V82I.
Result: The difference in motion modes induced by inhibitor bindings ma
A uniquely prevalent nonnucleoside reverse transcriptase inhibitor resistance mutation in Russian subtype A HIV-1 viruses.
Result: Of the 243 patients who received one or more protease inhibitors, 32 (13%) had a study-defined protease inhibitor-resistance mutation most commonly L10F, K20T, V32I, L33F, M46I/L, I47V/A, I50L, F53L, I54V/L, Q58E, L76V, V82A/C, I84V, L89V, and L90M.
2014 Update of the drug resistance mutations in HIV-1.
Discussion: However, there is emerging evidence that specific mutations, most notably I47A (and possibly I47V) and V32I, are associated with high-level resistance.
Discussion: The negative impact of the protease mutations I47V, I54M, T74P, and I84V and the positive impact of the protease mutation V82A on virologic response to darunavir/ritonavir were shown in 2 data sets independently.
Structures of darunavir-resistant HIV-1 protease mutant reveal atypical binding of darunavir to wide open flaps.
Result: Also for SQV, a second molecule was found in a location adjacent to the usual active site location in PR20/SQV and PRV32I/I47V/V82I/SQV structures.
Result: Mutants PRV32I and PRI47V have altered interactions with inhibitors DRV and SQV; however, V82I in the triple mutant PRV32I/I47V/V82I bearing the active site residues of HIV-2 PR does not significantly alter direct contacts with inhibitor.
Natural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.
Result: We modelled the proteins with unusual mutations (L5F, D29V, L63G, L63R, P79L and T91V), natural polymorphisms (L63H andL63S), and drug-resistant mutant PRs with single mutations or patterns of mutations (D30N, V32I, M36I, M46I, I47V, G48V, I50V, I50L, I54M, Q58E, T74P, L76V, V82A
Characteristics of HIV-1 natural drug resistance-associated mutations in former paid blood donors in Henan Province, China.
Discussion: Results from the HIV-1 drug resistance mutation research by the International AIDS Society-USA (updated in March 2013) have revealed that PI resistance mutation sites are L10I, K20M, V32I, M36I, M46I/L, I47V/A, I50V, Q58E, A71V, G73S, V82A/F/T, I84V, L89V,L90M; NRTIs resistance mutations are M41L, A62V, PMID: 23985909
2013
Journal of clinical microbiology
Abstract: All the wild-type and mutant alleles were unequivocally distinguished with plasmid templates, and the limits of detection were 1.56% for K219Q and K219E, 3.13% for L76V, 6.25% for K65R, K70R, L74V, L100I, K103N, K103R, Q151M, Y181C, and I47V, and 12.5% for M41L, K101P, K101E, V106A, V106M, Y115F, M184V, PMID: 23883841
2013
Japanese journal of infectious diseases
Abstract: The patients had primary antiretroviral resistance mutations to nucleos(t)ide reverse transcriptase (RT) inhibitors (NRTIs) (M41L, T215C, T215D, and K219Q), non-nucleoside RT inhibitors (NNRTIs; K103N), and protease inhibitors (PIs; I47V, G73S).
Persistence of HIV-1 transmitted drug resistance mutations.
PMID: 23904291
2013
The Journal of infectious diseases
Table: I47 V
Trends in Genotypic HIV-1 Antiretroviral Resistance between 2006 and 2012 in South African Patients Receiving First- and Second-Line Antiretroviral Treatment Regimens.
HIV mutation literature information.
PMID: 
2014
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