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Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activitiesHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsPolymorphisms and splice variants influence the antiretroviral activity of human APOBEC3HCrystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding DomainMultiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G.Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics.Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.APOBEC3 inhibits DEAD-END function to regulate microRNA activityAPOBEC deaminases-mutases with defensive roles for immunity.Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif.Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization.A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerizationDefinition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase.Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.Equine infectious anemia virus resists the antiretroviral activity of equine APOBEC3 proteins through a packaging-independent mechanism.Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 18 July 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Functional domain organization of human APOBEC3G.
@en
Functional domain organization of human APOBEC3G.
@nl
type
label
Functional domain organization of human APOBEC3G.
@en
Functional domain organization of human APOBEC3G.
@nl
prefLabel
Functional domain organization of human APOBEC3G.
@en
Functional domain organization of human APOBEC3G.
@nl
P2860
P1433
P1476
Functional domain organization of human APOBEC3G.
@en
P2093
Barry D Gooch
Bryan R Cullen
P2860
P304
P356
10.1016/J.VIROL.2008.06.013
P407
P577
2008-07-18T00:00:00Z