APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages. - Wikidata - awgldk - TriplyDB

APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages.

APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages.

http://www.wikidata.org/entity/Q36506765

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AID and APOBECs span the gap between innate and adaptive immunity Links between Human LINE-1 Retrotransposons and Hepatitis Virus-Related Hepatocellular Carcinoma Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all Suppression of APOBEC3-mediated restriction of HIV-1 by Vif Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms Quantification of deaminase activity-dependent and -independent restriction of HIV-1 replication mediated by APOBEC3F and APOBEC3G through experimental-mathematical investigation.R88-APOBEC3Gm Inhibits the Replication of Both Drug-resistant Strains of HIV-1 and Viruses Produced From Latently Infected Cells HIV-1 competition experiments in humanized mice show that APOBEC3H imposes selective pressure and promotes virus adaptation The virus-induced protein APOBEC3G inhibits anoikis by activation of Akt kinase in pancreatic cancer cells.APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinants APOBEC3D and APOBEC3F potently promote HIV-1 diversification and evolution in humanized mouse model.Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C.HIV-1 Vpu accessory protein induces caspase-mediated cleavage of IRF3 transcription factor Lack of association between intact/deletion polymorphisms of the APOBEC3B gene and HIV-1 risk Identification of a novel HIV-1 inhibitor targeting Vif-dependent degradation of human APOBEC3G protein.Anti-APOBEC3G activity of HIV-1 Vif protein is attenuated in elite controllers HIV-1 Tropism Determines Different Mutation Profiles in Proviral DNA.Incomplete APOBEC3G/F Neutralization by HIV-1 Vif Mutants Facilitates the Genetic Evolution from CCR5 to CXCR4 Usage.Role of APOBEC3F Gene Variation in HIV-1 Disease Progression and Pneumocystis Pneumonia.A Single Nucleotide Polymorphism in Human APOBEC3C Enhances Restriction of Lentiviruses DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B.APOBEC3 Proteins in Viral Immunity.Host restriction factors in retroviral infection: promises in virus-host interaction.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G APOBEC3G and APOBEC3F Act in Concert To Extinguish HIV-1 Replication The effect of HIV-1 Vif polymorphisms on A3G anti-viral activity in an in vivo mouse model.APOBEC3 proteins can copackage and comutate HIV-1 genomes.Simian foamy virus infection of rhesus macaques in Bangladesh: relationship of latent proviruses and transcriptionally active viruses.APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular Mechanisms Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Catalytic activity of APOBEC3F is required for efficient restriction of Vif-deficient human immunodeficiency virus.Identification of a tripartite interaction between the N-terminus of HIV-1 Vif and CBFβ that is critical for Vif function Host restriction of lentiviruses and viral countermeasures: APOBEC3 and Vif.The assembly of Vif ubiquitin E3 ligase for APOBEC3 degradation.Mechanisms of HIV-1 Control.Long-term passage of Vif-null HIV-1 in CD4+ T cells expressing sub-lethal levels of APOBEC proteins fails to develop APOBEC resistance.The APOBEC Protein Family: United by Structure, Divergent in Function.Possible footprints of APOBEC3F and/or other APOBEC3 deaminases, but not APOBEC3G, on HIV-1 from patients with acute/early and chronic infections.The Structural Interface between HIV-1 Vif and Human APOBEC3H.

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P2860

APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages.

http://www.wikidata.org/entity/Q36506765

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2012 nî lūn-bûn

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P2093

Chawaree Chaipan

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Jessica L Smith

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Vinay K Pathak

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Wei-Shau Hu

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P2860

Antiretroelement activity of APOBEC3H was lost twice in recent human evolution

Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H.

Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1

Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1

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

The localization of APOBEC3H variants in HIV-1 virions determines their antiviral activity

Human cytidine deaminase APOBEC3H restricts HIV-1 replication

The range of human APOBEC3H sensitivity to lentiviral Vif proteins

Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H

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10.1128/JVI.00676-12

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1

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87

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232700497

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23097438

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3536366

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