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 HIV mutation literature information.


  In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor.
 PMID: 9696850       1998       Journal of virology
Abstract: Selection of viral variants with increasing concentrations of ABT-378 revealed a sequential appearance of mutations in the protease gene: I84V-L10F-M46I-T91S-V32I-I47V.


  Drug-resistant HIV-1 proteases identify enzyme residues important for substrate selection and catalytic rate.
 PMID: 9753473       1998       Biochemistry
Abstract: Mutants containing R8K, V32I, V82T, I84V, G48V/L90M, or V82T/I84V substitutions were analyzed for differences in substrate preference and catalytic efficiency using a set of single amino acid substituted HIV-1 CA-NCa cleavage site peptides.
Abstract: Only the R8K and V32I mutants showed significant differences in subsite selection compared to wild-type enzyme.


  Predicting structural effects in HIV-1 protease mutant complexes with flexible ligand docking and protein side-chain optimization.
 PMID: 9779795       1998       Proteins
Abstract: Flexible ligand docking and optimization of mobile protein side-chains have been performed to predict structural effects in the V32I/I47V/V82I HIV-1 protease mutant bound with the SB203386 ligand and in the V82A HIV-1 protease mutant bound with the A77003 ligand.


  Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors.
 PMID: 8995629       1997       Journal of virology
Abstract: Active-site mutations V32I and I84V/A were consistently observed in the protease of highly resistant viruses, along with up to six other mutations.
Abstract: Despite these observations, however, most mutations had little effect on viral replication except when the active-site mutations V32I and I84V/A were coexpressed in the protease.


  Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity.
 PMID: 8756683       1996       Biochemistry
Abstract: SB203386 is a potent inhibitor of HIV-1 protease (Ki = 18 nM) but shows decreased inhibition of the HIV-1 protease (Val32Ile, Ile47Val, Val82Ile) triple mutant (Ki = 112 nM) and SIV protease (Ki = 960 nM).
Abstract: To gain greater understanding of the structural basis of human immunodeficiency virus (HIV) protease ligand specificity, we have crystallized and determined the structures of the HIV-1 protease (Val32Ile, Ile47Val, Val82Ile) triple mutant and simian immunodeficiency virus (SIV) protease in complex with SB203386, a tripeptide analogue inhibitor containing a


  Antiviral and resistance studies of AG1343, an orally bioavailable inhibitor of human immunodeficiency virus protease.
 PMID: 8834868       1996       Antimicrobial agents and chemotherapy
Abstract: Resistance, however, was not detected for recombinant viruses containing other key mutations in HIV-1 protease, including a Val to Ile change at residue 32 or a Val to Ala or Phe at residue 82.


  Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure.
 PMID: 7626598       1995       Biochemistry
Abstract: Eleven different recombinant, drug-resistant HIV-1 protease (HIV PR) mutants--R8Q, V32I, M46I, V82A, V82F, V82I, I84V, V32I/I84V, M46I/V82F, M46I/I84V, and V32I/K45I/F53L/A71V/I84V/L89M--were generated on the basis of results of in vitro selection experiments using the inh



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