HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.
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HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchInhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatinThe nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles.The human immunodeficiency virus type 1 nonnucleoside reverse transcriptase inhibitor resistance mutation I132M confers hypersensitivity to nucleoside analogs.Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease.Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions.Mechanisms involved in the selection of HIV-1 reverse transcriptase thumb subdomain polymorphisms associated with nucleoside analogue therapy failure.
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HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.
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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 03 July 2007
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... ability in infectious virions.
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HIV-1 protease dimer interface ...... tability in infectious virions
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Alok Mulky
Isabel Olivares
John C Kappes
Peter I Boross
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10.1016/J.JMB.2007.06.073
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2007-07-03T00:00:00Z