Substitutions at amino acid positions 143, 148, and 155 of HIV-1 integrase define distinct genetic barriers to raltegravir resistance in vivo.
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Resistance mutations outside the integrase coding region have an effect on human immunodeficiency virus replicative fitness but do not affect its susceptibility to integrase strand transfer inhibitorsHIV-1 integrase resistance among antiretroviral treatment naive and experienced patients from Northwestern Poland.Integrase inhibitor (INI) genotypic resistance in treatment-naive and raltegravir-experienced patients infected with diverse HIV-1 clades.Lack of impact of pre-existing T97A HIV-1 integrase mutation on integrase strand transfer inhibitor resistance and treatment outcome.Drug Susceptibility and Viral Fitness of HIV-1 with Integrase Strand Transfer Inhibitor Resistance Substitution Q148R or N155H in Combination with Nucleoside/Nucleotide Reverse Transcriptase Inhibitor Resistance Substitutions.Multiple genetic pathways involving amino acid position 143 of HIV-1 integrase are preferentially associated with specific secondary amino acid substitutions and confer resistance to raltegravir and cross-resistance to elvitegravir.The activity of the integrase inhibitor dolutegravir against HIV-1 variants isolated from raltegravir-treated adultsPharmacokinetic and pharmacodynamic evaluation of raltegravir and experience from clinical trials in HIV-positive patients.HIV drug resistance against strand transfer integrase inhibitorsLongitudinal analysis of raltegravir susceptibility and integrase replication capacity of human immunodeficiency virus type 1 during virologic failure.Collaborative update of a rule-based expert system for HIV-1 genotypic resistance test interpretation.Impact of HIV-1 Integrase L74F and V75I Mutations in a Clinical Isolate on Resistance to Second-Generation Integrase Strand Transfer Inhibitors.Drug resistance mutations in HIV-2 patients failing raltegravir and influence on dolutegravir response.Viral fitness cost prevents HIV-1 from evading dolutegravir drug pressure.Selective-advantage profile of human immunodeficiency virus type 1 integrase mutants explains in vivo evolution of raltegravir resistance genotypes.Panel of prototypical raltegravir-resistant infectious molecular clones in a novel integrase-deleted cloning vector.Quantitative prediction of integrase inhibitor resistance from genotype through consensus linear regression modeling.A safety evaluation of raltegravir for the treatment of HIV.Dolutegravir: a new option for HIV treatment
P2860
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P2860
Substitutions at amino acid positions 143, 148, and 155 of HIV-1 integrase define distinct genetic barriers to raltegravir resistance in vivo.
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Substitutions at amino acid po ...... altegravir resistance in vivo.
@ast
Substitutions at amino acid po ...... altegravir resistance in vivo.
@en
type
label
Substitutions at amino acid po ...... altegravir resistance in vivo.
@ast
Substitutions at amino acid po ...... altegravir resistance in vivo.
@en
prefLabel
Substitutions at amino acid po ...... altegravir resistance in vivo.
@ast
Substitutions at amino acid po ...... altegravir resistance in vivo.
@en
P2093
P2860
P356
P1433
P1476
Substitutions at amino acid po ...... altegravir resistance in vivo.
@en
P2093
Arne Frantzell
Signe Fransen
Soumi Gupta
P2860
P304
P356
10.1128/JVI.06618-11
P407
P577
2012-05-02T00:00:00Z