Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.
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Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfacesP body-associated protein Mov10 inhibits HIV-1 replication at multiple stagesHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allHost APOBEC3G protein inhibits HCV replication through direct binding at NS3Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Live cell visualization of the interactions between HIV-1 Gag and the cellular RNA-binding protein Staufen1Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulationsLeveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS.Identification of a dominant negative inhibitor of human zinc finger antiviral protein reveals a functional endogenous pool and critical homotypic interactions.Completion of hepatitis C virus replication cycle in heterokaryons excludes dominant restrictions in human non-liver and mouse liver cell lines.The cellular source for APOBEC3G's incorporation into HIV-1.APOBEC3 inhibits DEAD-END function to regulate microRNA activityThe roles of APOBEC3G complexes in the incorporation of APOBEC3G into HIV-1.Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexesThe role of amino-terminal sequences in cellular localization and antiviral activity of APOBEC3B.Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.Characterization of the Catalytic Domain of Human APOBEC3B and the Critical Structural Role for a Conserved Methionine.Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.The RNA Binding Specificity of Human APOBEC3 Proteins Resembles That of HIV-1 NucleocapsidFunctional requirements of AID's higher order structures and their interaction with RNA-binding proteinsMov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity.Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes.Human cellular restriction factors that target HIV-1 replication.A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function.Biochemical and biological studies of mouse APOBEC3.The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.Mechanisms of HIV-1 Control.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.Structural and functional assessment of APOBEC3G macromolecular complexes.The APOBEC Protein Family: United by Structure, Divergent in Function.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.A Comparison of Two Single-Stranded DNA Binding Models by Mutational Analysis of APOBEC3G.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.The rabbit as an orthologous small animal model for APOBEC3A oncogenesis.Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands
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Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 04 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Intracellular interactions bet ...... t on its association with RNA.
@en
Intracellular interactions bet ...... t on its association with RNA.
@nl
type
label
Intracellular interactions bet ...... t on its association with RNA.
@en
Intracellular interactions bet ...... t on its association with RNA.
@nl
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Intracellular interactions bet ...... t on its association with RNA.
@en
Intracellular interactions bet ...... t on its association with RNA.
@nl
P2093
P2860
P356
P1433
P1476
Intracellular interactions bet ...... nt on its association with RNA
@en
P2093
Vitaly Boyko
Wei-Shau Hu
Yeshitila N Friew
P2860
P2888
P356
10.1186/1742-4690-6-56
P577
2009-06-04T00:00:00Z
P5875
P6179
1034807278