Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes. - Wikidata - awgldk - TriplyDB

Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes.

Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes.

http://www.wikidata.org/entity/Q33755180

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Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase APOBEC3G encapsidation into HIV-1 virions: which RNA is it?HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity The localization of APOBEC3H variants in HIV-1 virions determines their antiviral activity HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factors HIV-1 Vif, APOBEC, and intrinsic immunity Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1 Inhibition of tRNA₃(Lys)-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all The APOBEC3 family of retroelement restriction factors Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1 Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components A DNA sequence recognition loop on APOBEC3A controls substrate specificity APOBEC3G: an intracellular centurion AID and Apobec3G haphazard deamination and mutational diversity Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities.Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins Leveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS.Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity Stably expressed APOBEC3F has negligible antiviral activity.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.The cellular source for APOBEC3G's incorporation into HIV-1.Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules Monomeric APOBEC3G is catalytically active and has antiviral activity.Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.The roles of APOBEC3G complexes in the incorporation of APOBEC3G into HIV-1.Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.ASK1 restores the antiviral activity of APOBEC3G by disrupting HIV-1 Vif-mediated counteraction.Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle Hydrodynamic and functional analysis of HIV-1 Vif oligomerization.Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G.

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Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes.

http://www.wikidata.org/entity/Q33755180

description

2005 nî lūn-bûn

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2005 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2005 թվականի մայիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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JVI.79.9.5870-5874.2005

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Journal of Virology

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Viral RNA is required for the ...... ype 1 nucleoprotein complexes.

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P2093

Clay L Gipson

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Eri Miyagi

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Hinh Ly

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Hiroaki Takeuchi

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Klaus Strebel

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Mohammad A Khan

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Ritu Goila-Gaur

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Sandra Kao

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Sandrine Opi

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Tristram G Parslow

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P2860

An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22

hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup

The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA

Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication

A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts

DNA deamination mediates innate immunity to retroviral infection

Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif

Hypermutation of HIV-1 DNA in the absence of the Vif protein

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5870-5874

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scholarly article

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10.1128/JVI.79.9.5870-5874.2005

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9

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79

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7910215

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15827203

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1082784

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