HIV mutation literature information.


  Trends in Genotypic HIV-1 Antiretroviral Resistance between 2006 and 2012 in South African Patients Receiving First- and Second-Line Antiretroviral Treatment Regimens.
 PMID: 23840622       2013       PloS one
Method: The following protease mutations were considered LPV/r-resistance mutations: L10F, L24I, V32I, L33F, M46IL, I47A, I50V, I54MLV, L76V, V82ATSFMC, I84V, L89V, L90M.
Table: V82A


  Crystallographic study of multi-drug resistant HIV-1 protease lopinavir complex: mechanism of drug recognition and resistance.
 PMID: 23792096       2013       Biochemical and biophysical research communications
Abstract: Mutations at residues 32I, L33F, 46I, 47A, I54V, V82A, I84V, and L90M render the protease drug resistant against LPV.
Introduction: Although drug resistance is relatively less likely to develop against LPV compared to other HIV-1 protease inhibitors, resistance mutations, including 32I, 47A, 46I, L33F, I54V, V82A, I84V, and L90M, or combinations among L76V, M46I, and V82A in the protease, and A431V


  A Comparative Molecular Dynamics, MM-PBSA and Thermodynamic Integration Study of Saquinavir Complexes with Wild-Type HIV-1 PR and L10I, G48V, L63P, A71V, G73S, V82A and I84V Single Mutants.
 PMID: 26587633       2013       Journal of chemical theory and computation
Abstract: In this work, we examine L10I, G48V, L63P, A71V, G73S, V82A, and I84V single mutant HIV-1 PR strains in complexes with saquinavir to elucidate drug-protease interactions and dynamics.
Abstract: Mutants lacking this interaction (G48V, V82A, I84V) demonstrated reduced binding affinities.
Abstract: The preservation of hydrogen bonds of saquinavir with both the active site and flap residues in the wild-type and certain single mutants (A71V, V82A) is also crucial for effective inhibition.


  Increasing trends in primary NNRTI resistance among newly HIV-1-diagnosed individuals in Buenos Aires, Argentina.
 PMID: 24093951       2013       Journal of the International AIDS Society
Table: V82A


  Prevalence and mutation patterns of HIV drug resistance from 2010 to 2011 among ART-failure individuals in the Yunnan Province, China.
 PMID: 24009694       2013       PloS one
Table: V82A


  Potential elucidation of a novel CTL epitope in HIV-1 protease by the protease inhibitor resistance mutation L90M.
 PMID: 24015196       2013       PloS one
Method: Equations 1, 2, 3, 4 and 5 represent L90M frequency estimators trained from the V82A, I54V, A71V, M46I and I84V sets respectively.
Result: Five sequence sets were constructed, each devoid of M46I, I54V, V71A, V82A and I84V respectively, which were
Table: V82A


  Persistence of HIV-1 transmitted drug resistance mutations.
 PMID: 23904291       2013       The Journal of infectious diseases
Table: V82A


  Frequency and patterns of protease gene resistance mutations in HIV-infected patients treated with lopinavir/ritonavir as their first protease inhibitor.
 PMID: 22258921       2012       The Journal of antimicrobial chemotherapy
Abstract: One or more protease mutations were detected in 32 (11%) patients; the most frequent were I54V (n = 12), M46I (n = 11), V82A (n = 7) and L76V (n = 3).


  HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.
 PMID: 22404139       2012       Biochemistry
Result: Similarly, mutations in the active site cavity of PR20 (D30N, V32I, I47V and I84V) alter the charge and increase the distance between the flaps and the base of the cavity relative to the values in MDR769 (V82A and I84V).


  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
Abstract: Crystal structures at resolutions of 1.25-1.55 A were analyzed for complexes of 1 with the PR containing major drug resistant mutations, PR(I47V), PR(L76V), PR(V82A), and PR(N88D).
Abstract: Mutations of I47V and V82A alter residues in the inhibitor-binding site, while L76V and N88D are distal mutations having no direct contact with the inhibitor.
Abstract: Substitution of a smaller amino acid in PR(I47V) and PR(



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