Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo.
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Potent activity of the HIV-1 maturation inhibitor bevirimat in SCID-hu Thy/Liv miceThe choreography of HIV-1 proteolytic processing and virion assemblyPatterns of resistance and cross-resistance to human immunodeficiency virus type 1 reverse transcriptase inhibitors in patients treated with the nonnucleoside reverse transcriptase inhibitor lovirideGag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness lossAltered substrate specificity of drug-resistant human immunodeficiency virus type 1 protease.Identification of structural mechanisms of HIV-1 protease specificity using computational peptide docking: implications for drug resistance.A novel assay allows genotyping of the latent reservoir for human immunodeficiency virus type 1 in the resting CD4+ T cells of viremic patients.Differences in the fitness of two diverse wild-type human immunodeficiency virus type 1 isolates are related to the efficiency of cell binding and entry.Decreased processivity of human immunodeficiency virus type 1 reverse transcriptase (RT) containing didanosine-selected mutation Leu74Val: a comparative analysis of RT variants Leu74Val and lamivudine-selected Met184Val.Individual contributions of mutant protease and reverse transcriptase to viral infectivity, replication, and protein maturation of antiretroviral drug-resistant human immunodeficiency virus type 1.Changes in human immunodeficiency virus type 1 populations after treatment interruption in patients failing antiretroviral therapy.Viral evolution in response to the broad-based retroviral protease inhibitor TL-3.Antiretroviral resistance during successful therapy of HIV type 1 infection.Atazanavir signature I50L resistance substitution accounts for unique phenotype of increased susceptibility to other protease inhibitors in a variety of human immunodeficiency virus type 1 genetic backbonesHuman immunodeficiency virus type 1 cloning vectors for antiretroviral resistance testing.A bacteriophage lambda-based genetic screen for characterization of the activity and phenotype of the human immunodeficiency virus type 1 proteaseGenotypic and phenotypic resistance patterns of human immunodeficiency virus type 1 variants with insertions or deletions in the reverse transcriptase (RT): multicenter study of patients treated with RT inhibitorsSensitive genetic screen for protease activity based on a cyclic AMP signaling cascade in Escherichia coli.Drug-associated changes in amino acid residues in Gag p2, p7(NC), and p6(Gag)/p6(Pol) in human immunodeficiency virus type 1 (HIV-1) display a dominant effect on replicative fitness and drug response.Interference between D30N and L90M in selection and development of protease inhibitor-resistant human immunodeficiency virus type 1.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 precurIsolation and molecular characterization of a nelfinavir (NFV)-resistant human immunodeficiency virus type 1 that exhibits NFV-dependent enhancement of replication.Functional correlation between a novel amino acid insertion at codon 19 in the protease of human immunodeficiency virus type 1 and polymorphism in the p1/p6 Gag cleavage site in drug resistance and replication fitnessSlower uncoating is associated with impaired replicative capability of simian-tropic HIV-1Single genome sequencing of HIV-1 gag and protease resistance mutations at virologic failure during the OK04 trial of simplified versus standard maintenance therapyGag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1.Interplay between single resistance-associated mutations in the HIV-1 protease and viral infectivity, protease activity, and inhibitor sensitivityHIV-1 antiretroviral drug therapy.Elucidation of the Molecular Mechanism Driving Duplication of the HIV-1 PTAP Late Domain.Modeling within-host HIV-1 dynamics and the evolution of drug resistance: trade-offs between viral enzyme function and drug susceptibilitySignificant reductions in Gag-protease-mediated HIV-1 replication capacity during the course of the epidemic in JapanStochastic processes strongly influence HIV-1 evolution during suboptimal protease-inhibitor therapy.Role of minority populations of human immunodeficiency virus type 1 in the evolution of viral resistance to protease inhibitors.Modulation of HIV-1 infectivity and cyclophilin A-dependence by Gag sequence and target cell typeNon-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 inhibitorsNovel single-cell-level phenotypic assay for residual drug susceptibility and reduced replication capacity of drug-resistant human immunodeficiency virus type 1.Role of Gag in HIV Resistance to Protease InhibitorsResistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach.Kinetics of antiviral activity and intracellular pharmacokinetics of human immunodeficiency virus type 1 protease inhibitors in tissue culture.Constrained evolution of human immunodeficiency virus type 1 protease during sequential therapy with two distinct protease inhibitors
P2860
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P2860
Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@en
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@nl
type
label
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@en
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@nl
prefLabel
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@en
Loss of viral fitness associat ...... o protease inhibitors in vivo.
@nl
P2093
P2860
P1433
P1476
Loss of viral fitness associat ...... to protease inhibitors in vivo
@en
P2093
P2860
P304
P407
P577
1998-04-01T00:00:00Z