Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precur - Wikidata - awgldk - TriplyDB

Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precur

Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precur

http://www.wikidata.org/entity/Q34344036

about

The choreography of HIV-1 proteolytic processing and virion assembly Purifying selection masks the mutational flexibility of HIV-1 reverse transcriptase.Association of efavirenz hypersusceptibility with virologic response in ACTG 368, a randomized trial of abacavir (ABC) in combination with efavirenz (EFV) and indinavir (IDV) in HIV-infected subjects with prior nucleoside analog experience.Phenotypic hypersusceptibility to multiple protease inhibitors and low replicative capacity in patients who are chronically infected with human immunodeficiency virus type 1.Low human immunodeficiency virus envelope diversity correlates with low in vitro replication capacity and predicts spontaneous control of plasma viremia after treatment interruptions.Efficient identification of human immunodeficiency virus type 1 mutants resistant to a protease inhibitor by using a random mutant library.HIV-1 diversity after a class switch failure.Impact of human immunodeficiency virus type 1 subtype C on drug resistance mutations in patients from Botswana failing a nelfinavir-containing regimen Role of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivity Infectivity and replication capacity of drug-resistant human immunodeficiency virus type 1 variants isolated during primary infection Characterization of a thymus-tropic HIV-1 isolate from a rapid progressor: role of the envelope.Interplay between single resistance-associated mutations in the HIV-1 protease and viral infectivity, protease activity, and inhibitor sensitivity A sensitive real-time PCR based assay to estimate the impact of amino acid substitutions on the competitive replication fitness of human immunodeficiency virus type 1 in cell culture Clinical significance of human immunodeficiency virus type 1 replication fitness.Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors Role of the K101E substitution in HIV-1 reverse transcriptase in resistance to rilpivirine and other nonnucleoside reverse transcriptase inhibitors Diversity of human immunodeficiency virus type 1 subtype A and CRF03_AB protease in Eastern Europe: selection of the V77I variant and its rapid spread in injecting drug user populations.Relationships between infectious titer, capsid protein levels, and reverse transcriptase activities of diverse human immunodeficiency virus type 1 isolates.Novel single-cell-level phenotypic assay for residual drug susceptibility and reduced replication capacity of drug-resistant human immunodeficiency virus type 1.HIV-1 protease inhibitor mutations affect the development of HIV-1 resistance to the maturation inhibitor bevirimat.Amino acid substitutions at position 190 of human immunodeficiency virus type 1 reverse transcriptase increase susceptibility to delavirdine and impair virus replication.Parameters driving the selection of nelfinavir-resistant human immunodeficiency virus type 1 variants.The hepatitis B virus polymerase mutation rtV173L is selected during lamivudine therapy and enhances viral replication in vitro.RNA motif discovery by SHAPE and mutational profiling (SHAPE-MaP).Evolution of human immunodeficiency virus type 1 protease genotypes and phenotypes in vivo under selective pressure of the protease inhibitor ritonavir.

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P2860

Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precur

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2002 nî lūn-bûn

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2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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Nelfinavir-resistant, amprenav ...... ess the Gag polyprotein precur

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Nelfinavir-resistant, amprenav ...... ess the Gag polyprotein precur

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JVI.76.17.8659-8666.2002

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Journal of Virology

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Nelfinavir-resistant, amprenav ...... ess the Gag polyprotein precur

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P2093

Andrea Gamarnik

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Neil Parkin

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Rainer Ziermann

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Wolfgang Resch

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P2860

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

A mutation in human immunodeficiency virus type 1 protease, N88S, that causes in vitro hypersensitivity to amprenavir

In vitro resistance profile of the human immunodeficiency virus type 1 protease inhibitor BMS-232632

Genotypic and phenotypic characterization of human immunodeficiency virus type 1 variants isolated from patients treated with the protease inhibitor nelfinavir.

Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor

Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors

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

Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection

Viral dynamics in human immunodeficiency virus type 1 infection

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8659-8666

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10.1128/JVI.76.17.8659-8666.2002

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17

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76

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Ronald Swanstrom

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12163585

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136408

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