Abstract: The human immunodeficiency virus type 1 protease mutation N88S, which is occasionally selected by treatment with nelfinavir or indinavir, confers hypersusceptibility to amprenavir in vitro.
Abstract: We report a case of N88S developing after virologic failure of both indinavir- and nelfinavir-containing regimens that was managed successfully with a regimen that contained amprenavir.
In vitro resistance profile of the human immunodeficiency virus type 1 protease inhibitor BMS-232632.
PMID: 10952574
2000
Antimicrobial agents and chemotherapy
Abstract: Genotypic and phenotypic analysis of three different HIV strains resistant to BMS-232632 indicated that an N88S substitution in the viral protease appeared first during the selection process in two of the three strains.
A mutation in human immunodeficiency virus type 1 protease, N88S, that causes in vitro hypersensitivity to amprenavir.
Abstract: All viruses that carried the N88S mutation were hypersensitive to amprenavir.
Abstract: Site-directed mutagenesis studies confirmed the causal role of N88S in determining amprenavir hypersensitivity.
Abstract: The most pronounced increases in susceptibility were strongly associated with an N88S mutation in protease.
Abstract: The presence of the N88S mutation and associated amprenavir hypersensitivity may be useful in predicting an improved clinical response to amprenavir salvage therapy.
Estimate of the frequency of human immunodeficiency virus type 1 protease inhibitor resistance within unselected virus populations in vitro.
PMID: 9527815
1998
Antimicrobial agents and chemotherapy
Abstract: Two variants with single mutations responsible for drug resistance (V82A and N88S) were quantifiably isolated after only one round of replication, yielding a crude frequency estimate of at least 1 SC-55389A-resistant variant per 3.5 x 10(5) wild-type infectious units.
A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A.
PMID: 9055985
1997
Antimicrobial agents and chemotherapy
Abstract: Resistant isolates from both strains consistently had a mutation to serine for asparagine at amino acid 88 (N88S) in the protease gene either alone or in combination with a change to phenylalanine at position 10.
Abstract: The N88S mutation, recreated by oligonucleotide-mediated site-directed mutagenesis in HXB2, was sufficient to confer resistance to SC-55389A.
Abstract: The potencies of L735,524 and Ro31-8959 were not reduced when these compounds were assayed against variants with either the N88S or N88D substitution.
HIV mutation literature information.
PMID: 
2002
AIDS (London, England)
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