Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
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The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3GStructure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activitiesAPOBEC3G contributes to HIV-1 variation through sublethal mutagenesisHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsTurning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3)HIV-1 Vif, APOBEC, and intrinsic immunityHuman immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integrationMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allSuppression of APOBEC3-mediated restriction of HIV-1 by VifMulti-scale modeling of HIV infection in vitro and APOBEC3G-based anti-retroviral therapyAPOBEC3G: an intracellular centurionMultiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.T cells contain an RNase-insensitive inhibitor of APOBEC3G deaminase activity.APOBEC3G inhibits elongation of HIV-1 reverse transcripts.Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G.Inducible APOBEC3G-Vif double stable cell line as a high-throughput screening platform to identify antiviral compounds.APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms.Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs.In vivo HIV-1 hypermutation and viral loads among antiretroviral-naive Brazilian patients.APOBEC3G-induced hypermutation of human immunodeficiency virus type-1 is typically a discrete "all or nothing" phenomenon.Quantification of unintegrated HIV-1 DNA at the single cell level in vivo.HIV-1 Vif inhibits G to A hypermutations catalyzed by virus-encapsidated APOBEC3G to maintain HIV-1 infectivityIntensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexesAPOBEC3 has not left an evolutionary footprint on the HIV-1 genome.Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F.The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA.Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment.Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 Vif.Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1.Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G.A multi-scale mathematical modeling framework to investigate anti-viral therapeutic opportunities in targeting HIV-1 accessory proteins.Running loose or getting lost: how HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif proteinAPOBEC3G and APOBEC3F rarely co-mutate the same HIV genomeBreaking Barriers to an AIDS Model with Macaque-Tropic HIV-1 Derivatives.Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G
P2860
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P2860
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
description
2007 nî lūn-bûn
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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@ast
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@en
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@nl
type
label
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@ast
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@en
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@nl
prefLabel
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@ast
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@en
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@nl
P2093
P1433
P1476
Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
@en
P2093
David E Ott
Elena Chertova
Hongzhan Xu
James D Roser
Wei-Shau Hu
P304
P356
10.1016/J.VIROL.2006.10.036
P407
P577
2006-11-28T00:00:00Z