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 HIV mutation literature information.


  Persistence of HIV-1 transmitted drug resistance mutations.
 PMID: 23904291       2013       The Journal of infectious diseases
Table: V82 T


  Potent antiviral HIV-1 protease inhibitor GRL-02031 adapts to the structures of drug resistant mutants with its P1'-pyrrolidinone ring.
 PMID: 22401672       2012       Journal of medicinal chemistry
Introduction: Mutations of V82A/T/F/S/L are very common in PI resistance and show reduced susceptibility to all the clinical PIs except DRV.


  Loss of the protease dimerization inhibition activity of tipranavir (TPV) and its association with the acquisition of resistance to TPV by HIV-1.
 PMID: 23015723       2012       Journal of virology
Abstract: HIV(11MIX)(P10) contained various amino acid substitutions, including I54V and V82T.
Abstract: However, the introduction of I54V/V82T into cHIV(B) (cHIV(B)(I54V/V82T)) compromised TPV's dimerization inhibition and cHIV(B)(I54V/V82T) proved to be significantly TPV resistant.
Abstract: The introduction of I54V/V82T into wild-type cHIV(NL4-3) (cHIV(NL4-3(I54V/V82T))) did not block TPV's dimerization inhibition or confer TPV resistance.


  Does GSS still maintain relevance on HAART outcome after the introduction of newest active antiretroviral drugs? 48 weeks results.
 PMID: 22211659       2011       Current HIV research
Abstract: About 60% of tests reported L10FIRVC, M36ILV, M46IL, I54VLAMTS, V82AFTSLI, and L90M mutations in the protease region.


  Can linear regression modeling help clinicians in the interpretation of genotypic resistance data? An application to derive a lopinavir-score.
 PMID: 22110581       2011       PloS one
Table: V82T


  HIV type-1 genotypic resistance profiles in vertically infected patients from Argentina reveal an association between K103N+L100I and L74V mutations.
 PMID: 20587857       2010       Antiviral therapy
Abstract: Mutations V82A/F/T/S/M/I were primarily selected by the administration of ritonavir (RTV) in an historical ARV regimen.
Abstract: RESULTS: In protease (PR), resistance-associated mutations M46I/L, I54M/L/V/A/S and V82A/F/T/S/M/I were associated with each other and with minor mutations at codons 10, 24 and 71.


  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.


  Decomposing the energetic impact of drug resistant mutations in HIV-1 protease on binding DRV.
 PMID: 20543885       2010       Journal of chemical theory and computation
Abstract: Two drug-resistant protease variants FLAP+ (L10I, G48V, I54V, V82A) and ACT (V82T, I84V) decrease the binding affinity with DRV by 1.0 kcal/mol and 1.6 kcal/mol respectively.
Introduction: In this study, the binding of DRV was investigated with wild-type HIV-1 protease and two drug-resistant variants: FLAP+ (Figure 1B) with L10I, G48V, I54V, V82A which are a combination of flap and active site mutations, and ACT (Figure 1C) with V82T, I84V which are active site mutations.
Method: For the ACT mu


  HIV-1 protease mutations and protease inhibitor cross-resistance.
 PMID: 20660676       2010       Antimicrobial agents and chemotherapy
Abstract: Of the mutations with the greatest effect on PI susceptibility, I84AV was associated with decreased susceptibility to eight PIs; V32I, G48V, I54ALMSTV, V82F, and L90M were associated with decreased susceptibility to six to seven PIs; I47A, G48M, I50V, L76V, V82ST, and N88S were associated with decreased susceptibility to four to five PIs; and D30N,  PMID: 19149765       2009       The Biochemical journal
Result: PRMDR contains multiple drug-resistant mutations (L10I, K45R, I54V, L63P, A71V, V82T, L90M and I93L) and is highly resistant to a number of active-site inhibitors, although it remains sensitive to the experimental active-site inhibitor JE-2147.



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