Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis. - Wikidata - wikimedia - TriplyDB

Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.

Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.

http://www.wikidata.org/entity/Q39762406

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Current perspectives on HIV-1 antiretroviral drug resistance Suppression of APOBEC3-mediated restriction of HIV-1 by Vif Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.A single amino acid in human APOBEC3F alters susceptibility to HIV-1 Vif Ex vivo gene therapy for HIV-1 treatment.Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.Inhibition of APOBEC3G activity impedes double-stranded DNA repair HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G Dispersed sites of HIV Vif-dependent polyubiquitination in the DNA deaminase APOBEC3F.A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.Binding of RNA by APOBEC3G controls deamination-independent restriction of retroviruses Crystal structures of APOBEC3G N-domain alone and its complex with DNA.Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3G APOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotransposition The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.Determinants of efficient degradation of APOBEC3 restriction factors by HIV-1 Vif.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.SIVmac239 Vif and Human APOBEC3B Interactions Resemble Those Between HIV-1 Vif and Human APOBEC3G.Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.

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Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.

http://www.wikidata.org/entity/Q39762406

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Definition of the interacting ...... g MAPPIT mutagenesis analysis.

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Bertrand Van Schoubroeck

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Delphine Lavens

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Dominiek Catteeuw

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Frank Peelman

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Isabel Uyttendaele

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Jan Tavernier

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José Van der Heyden

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Julia Kurth

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Reginald Clayton

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P2860

Model structure of human APOBEC3G

Design and application of a cytokine-receptor-based interaction trap

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

APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G

MAFFT version 5: improvement in accuracy of multiple sequence alignment

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

A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion

An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model

Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications

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10.1093/NAR/GKP1154

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