Loss of raltegravir susceptibility by human immunodeficiency virus type 1 is conferred via multiple nonoverlapping genetic pathways.
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Identification of novel mutations responsible for resistance to MK-2048, a second-generation HIV-1 integrase inhibitorHIV-1 integrase inhibitor resistance and its clinical implicationsActivities, Crystal Structures, and Molecular Dynamics of Dihydro-1 H -isoindole Derivatives, Inhibitors of HIV-1 IntegraseStructure-analysis of the HIV-1 integrase Y143C/R raltegravir resistance mutation in association with the secondary mutation T97ADevelopment of elvitegravir resistance and linkage of integrase inhibitor mutations with protease and reverse transcriptase resistance mutationsResistance 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 inhibitorsBiochemical and pharmacological analyses of HIV-1 integrase flexible loop mutants resistant to raltegravirAltered viral fitness and drug susceptibility in HIV-1 carrying mutations that confer resistance to nonnucleoside reverse transcriptase and integrase strand transfer inhibitors.Effect of HIV-1 integrase resistance mutations when introduced into SIVmac239 on susceptibility to integrase strand transfer inhibitors.Resistance to integrase inhibitors.Bicyclic hydroxy-1H-pyrrolopyridine-trione containing HIV-1 integrase inhibitors.Secondary integrase resistance mutations found in HIV-1 minority quasispecies in integrase therapy-naive patients have little or no effect on susceptibility to integrase inhibitors.Structure-based modeling of the functional HIV-1 intasome and its inhibitionEffect of raltegravir resistance mutations in HIV-1 integrase on viral fitnessS/GSK1349572, a new integrase inhibitor for the treatment of HIV: promises and challenges.Rapid screening of HIV reverse transcriptase and integrase inhibitors.Physical trapping of HIV-1 synaptic complex by different structural classes of integrase strand transfer inhibitors.HIV-1 antiretroviral resistance: scientific principles and clinical applicationsComparison of the Mechanisms of Drug Resistance among HIV, Hepatitis B, and Hepatitis C.Elvitegravir: a once-daily, boosted, HIV-1 integrase inhibitor.Analysis of low-frequency mutations associated with drug resistance to raltegravir before antiretroviral treatment.Extended use of raltegravir in the treatment of HIV-1 infection: optimizing therapyRaltegravir in combination with other antiretroviral agents for the treatment of HIV infection.Performance of the Abbott RealTime HIV-1 viral load assay is not impacted by integrase inhibitor resistance-associated mutations.HIV-1 integrase strand transfer inhibitors stabilize an integrase-single blunt-ended DNA complexInfluence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study.Role of raltegravir in the management of HIV-1 infection.Emerging integrase inhibitor resistance mutations in raltegravir-treated HIV-1-infected patients with low-level viremia.Study of genotypic and phenotypic HIV-1 dynamics of integrase mutations during raltegravir treatment: a refined analysis by ultra-deep 454 pyrosequencing.HIV-1 antiretroviral drug therapy.Switching between raltegravir resistance pathways analyzed by deep sequencingAnalysis of transmitted resistance to raltegravir and selective pressure among HIV-1-infected patients on a failing HAART in Sao Paulo, Brazil.Substitutions at amino acid positions 143, 148, and 155 of HIV-1 integrase define distinct genetic barriers to raltegravir resistance in vivo.Safety, Pharmacokinetics and Efficacy of Dolutegravir in Treatment-experienced HIV-1 Infected Adolescents: Forty-eight-week Results from IMPAACT P1093Lack of impact of pre-existing T97A HIV-1 integrase mutation on integrase strand transfer inhibitor resistance and treatment outcome.Genetic diversity and naturally polymorphisms in HIV type 1 integrase isolates from Maputo, Mozambique: implications for integrase inhibitorsDrug 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.Prevalent polymorphisms in wild-type HIV-1 integrase are unlikely to engender drug resistance to dolutegravir (S/GSK1349572).Comprehensive in vitro analysis of simian retrovirus type 4 susceptibility to antiretroviral agentsPhenotypic susceptibility of HIV-2 to raltegravir: integrase mutations Q148R and N155H confer raltegravir resistance.
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P2860
Loss of raltegravir susceptibility by human immunodeficiency virus type 1 is conferred via multiple nonoverlapping genetic pathways.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 16 September 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@en
Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
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type
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Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@en
Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@nl
prefLabel
Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@en
Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@nl
P2093
P2860
P356
P1433
P1476
Loss of raltegravir susceptibi ...... noverlapping genetic pathways.
@en
P2093
Daria Hazuda
Marc Witmer
Michael Miller
Robert Danovich
Signe Fransen
Soumi Gupta
P2860
P304
11440-11446
P356
10.1128/JVI.01168-09
P407
P577
2009-09-16T00:00:00Z