Addition of E138K to R263K in HIV integrase increases resistance to dolutegravir, but fails to restore activity of the HIV integrase enzyme and viral replication capacity.
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Dolutegravir - a review of the pharmacology, efficacy, and safety in the treatment of HIVResistance against Integrase Strand Transfer Inhibitors and Relevance to HIV PersistenceStructural Studies of the HIV-1 Integrase Protein: Compound Screening and Characterization of a DNA-Binding InhibitorIn vitro activity of dolutegravir against wild-type and integrase inhibitor-resistant HIV-2Simian-tropic HIV as a model to study drug resistance against integrase inhibitors.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.Is resistance to dolutegravir possible when this drug is used in first-line therapy?Will drug resistance against dolutegravir in initial therapy ever occur?Effect on HIV-1 viral replication capacity of DTG-resistance mutations in NRTI/NNRTI resistant virusesThe Combination of the R263K and T66I Resistance Substitutions in HIV-1 Integrase Is Incompatible with High-Level Viral Replication and the Development of High-Level Drug Resistance.Dolutegravir maintains a durable effect against HIV replication in tissue culture even after drug washout.HIV-1 resistance to dolutegravir: update and new insights.Differential effects of the G118R, H51Y, and E138K resistance substitutions in different subtypes of HIV integrase.HIV drug resistance against strand transfer integrase inhibitorsCombination of the R263K and M184I/V resistance substitutions against dolutegravir and lamivudine decreases HIV replicative capacity.The R263K Dolutegravir Resistance-Associated Substitution Progressively Decreases HIV-1 Integration.Dolutegravir-Selected HIV-1 Containing the N155H and R263K Resistance Substitutions Does Not Acquire Additional Compensatory Mutations under Drug Pressure That Lead to Higher-Level Resistance and Increased Replicative Capacity.Polymorphic substitution E157Q in HIV-1 integrase increases R263K-mediated dolutegravir resistance and decreases DNA binding activity.Dolutegravir resistance mutation R263K cannot coexist in combination with many classical integrase inhibitor resistance substitutions.Cross-resistance to elvitegravir and dolutegravir in 502 patients failing on raltegravir: a French national study of raltegravir-experienced HIV-1-infected patients.Antiviral Activity of Bictegravir and Cabotegravir Against Integrase Inhibitor Resistant SIVmac239 and HIV-1.Absence of HIV-1 drug resistance mutations supports the use of dolutegravir in Uganda.Efficacies of Cabotegravir and Bictegravir against drug-resistant HIV-1 integrase mutants.Dolutegravir: a new option for HIV treatmentSelective resistance profiles emerging in patient-derived clinical isolates with cabotegravir, bictegravir, dolutegravir, and elvitegravir
P2860
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P2860
Addition of E138K to R263K in HIV integrase increases resistance to dolutegravir, but fails to restore activity of the HIV integrase enzyme and viral replication capacity.
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2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh
2014年學術文章
@zh-hant
name
Addition of E138K to R263K in ...... nd viral replication capacity.
@en
type
label
Addition of E138K to R263K in ...... nd viral replication capacity.
@en
prefLabel
Addition of E138K to R263K in ...... nd viral replication capacity.
@en
P2093
P2860
P356
P1476
Addition of E138K to R263K in ...... and viral replication capacity
@en
P2093
Diane N Singhroy
Kaitlin Anstett
Mark A Wainberg
Melissa Wares
Nathan Osman
Peter K Quashie
Yingshan Han
P2860
P304
P356
10.1093/JAC/DKU199
P407
P577
2014-06-10T00:00:00Z