HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
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Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminaseMutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificitiesStructural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3GHIV-1 Vif, APOBEC, and intrinsic immunityAPOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replicationIdentification of APOBEC3DE as another antiretroviral factor from the human APOBEC family7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3GAPOBEC3G & HTLV-1: inhibition without deaminationSuppression of APOBEC3-mediated restriction of HIV-1 by VifRoles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactionsNewly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase HCharacterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsA DNA sequence recognition loop on APOBEC3A controls substrate specificityAID and Apobec3G haphazard deamination and mutational diversityDistinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteinsViral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes.Expression of IMP1 enhances production of murine leukemia virus vector by facilitating viral genomic RNA packaging.APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3GMonomeric APOBEC3G is catalytically active and has antiviral activity.Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.Heat-stable molecule derived from Streptococcus cristatus induces APOBEC3 expression and inhibits HIV-1 replicationResistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsidStructure of the Vif-binding domain of the antiviral enzyme APOBEC3GAPOBEC3G levels predict rates of progression to AIDSBiochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycleHydrodynamic and functional analysis of HIV-1 Vif oligomerization.Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation.Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virionsHuman immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variantVirion packaging determinants and reverse transcription of SRP RNA in HIV-1 particles.APOBEC3 cytidine deaminases: distinct antiviral actions along the retroviral life cycle.Host restriction factors blocking retroviral replicationCharacterization of APOBEC3G binding to 7SL RNAHuman Discs Large is a new negative regulator of human immunodeficiency virus-1 infectivity.Distinct viral determinants for the packaging of human cytidine deaminases APOBEC3G and APOBEC3CIntracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.
P2860
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P2860
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@en
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@nl
type
label
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@en
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@nl
prefLabel
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@en
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@nl
P2093
P1476
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
@en
P2093
Gilles Bessou
Marc Douaisi
Marianne Courcoul
Robert Vigne
Sylvie Dussart
P304
P356
10.1016/J.BBRC.2004.07.005
P407
P577
2004-08-01T00:00:00Z