HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
about
Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assayStructural Evidence for Effectiveness of Darunavir and Two Related Antiviral Inhibitors against HIV-2 ProteaseCritical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitorsRevealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 proteaseThree main mutational pathways in HIV-2 lead to high-level raltegravir and elvitegravir resistance: implications for emerging HIV-2 treatment regimensRevealing origin of decrease in potency of darunavir and amprenavir against HIV-2 relative to HIV-1 protease by molecular dynamics simulations.Mutation V111I in HIV-2 reverse transcriptase increases the fitness of the nucleoside analogue-resistant K65R and Q151M viruses.Human immunodeficiency virus type 2 in two Saudi families.A modular system to evaluate the efficacy of protease inhibitors against HIV-2The Nucleoside Analog BMS-986001 Shows Greater In Vitro Activity against HIV-2 than against HIV-1.Phenotypic susceptibility of HIV-2 to raltegravir: integrase mutations Q148R and N155H confer raltegravir resistance.A genotypic method for determining HIV-2 coreceptor usage enables epidemiological studies and clinical decision support.Comparative studies on retroviral proteases: substrate specificity.MK-8591 (4'-Ethynyl-2-Fluoro-2'-Deoxyadenosine) Exhibits Potent Activity against HIV-2 Isolates and Drug-Resistant HIV-2 Mutants in Culture.Inhibition Profiling of Retroviral Protease Inhibitors Using an HIV-2 Modular System.Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.Antiretroviral drug resistance in HIV-2: three amino acid changes are sufficient for classwide nucleoside analogue resistance.Amino acid residues in HIV-2 reverse transcriptase that restrict the development of nucleoside analogue resistance through the excision pathway.Exploring the Reasons for Decrease in Binding Affinity of HIV-2 Against HIV-1 Protease Complex Using Interaction Entropy Under Polarized Force FieldHIV-2 Infection, End-Stage Renal Disease and Protease Inhibitor Intolerance
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P2860
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 04 December 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@en
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@nl
type
label
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@en
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@nl
prefLabel
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@en
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@nl
P1476
HIV-1 protease inhibitors: effects on HIV-2 replication and resistance.
@en
P2093
József Tözsér
Luis Menéndez-Arias
P356
10.1016/J.TIPS.2007.10.013
P577
2007-12-04T00:00:00Z