Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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The Host RNAs in Retroviral ParticlesHost RNA Packaging by Retroviruses: A Newly Synthesized StoryImmune evasion activities of accessory proteins Vpu, Nef and Vif are conserved in acute and chronic HIV-1 infection.The RNA Binding Specificity of Human APOBEC3 Proteins Resembles That of HIV-1 NucleocapsidAPOBEC3 Proteins in Viral Immunity.Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.A multi-scale mathematical modeling framework to investigate anti-viral therapeutic opportunities in targeting HIV-1 accessory proteins.Movements of HIV-1 genomic RNA-APOBEC3F complexes and PKR reveal cytoplasmic and nuclear PKR defenses and HIV-1 evasion strategies.APOBEC3 proteins can copackage and comutate HIV-1 genomes.The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme.APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular MechanismsMechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.APOBECs and virus restriction.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.Analysis of the human immunodeficiency virus-1 RNA packageome.Structural and functional assessment of APOBEC3G macromolecular complexes.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.Nanoscale Characterization of Interaction of APOBEC3G with RNA.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and Deamination.APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA.Recruitment of 7SL RNA to assembling HIV-1 virus-like particles.The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism.Deep sequencing of HIV-1 reverse transcripts reveals the multifaceted antiviral functions of APOBEC3G.Understanding the Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H.CLIP-related methodologies and their application to retrovirology.Feline APOBEC3s, Barriers to Cross-Species Transmission of FIV?Strategy of Human Cytomegalovirus To Escape Interferon Beta-Induced APOBEC3G Editing Activity
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P2860
Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2015 թվականի հունվարին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
@ast
Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
@en
Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
@ast
Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
@en
Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
@nl
P2860
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Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
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P2860
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10.1371/JOURNAL.PPAT.1004609
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P577
2015-01-15T00:00:00Z