A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.
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Differential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypesHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsA single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivityMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allSuppression of APOBEC3-mediated restriction of HIV-1 by VifThe SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complexCharacterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsStructural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloBMultiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Identification of HIV-1 Vif regions required for CBF-β interaction and APOBEC3 suppressionLeveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS.Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics.Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded VifIdentification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity.Evolutionarily conserved requirement for core binding factor beta in the assembly of the human immunodeficiency virus/simian immunodeficiency virus Vif-cullin 5-RING E3 ubiquitin ligase.Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity.HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinantsLong-term restriction by APOBEC3F selects human immunodeficiency virus type 1 variants with restored Vif functionN-terminal hemagglutinin tag renders lysine-deficient APOBEC3G resistant to HIV-1 Vif-induced degradation by reduced polyubiquitination.Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif.Insights into the dual activity of SIVmac239 Vif against human and African green monkey APOBEC3G.Cellular requirements for bovine immunodeficiency virus Vif-mediated inactivation of bovine APOBEC3 proteins.Codon pairs of the HIV-1 vif gene correlate with CD4+ T cell countRequirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligaseAPOBEC3G: a double agent in defenseAPOBEC3G polymorphism as a selective barrier to cross-species transmission and emergence of pathogenic SIV and AIDS in a primate host.Identification of a Cullin5-ElonginB-ElonginC E3 complex in degradation of feline immunodeficiency virus Vif-mediated feline APOBEC3 proteinsStructural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities.Structure of the Vif-binding domain of the antiviral enzyme APOBEC3GCoevolutionary analyses require phylogenetically deep alignments and better null models to accurately detect inter-protein contacts within and between species.Hydrodynamic and functional analysis of HIV-1 Vif oligomerization.Evolutionarily conserved pressure for the existence of distinct G2/M cell cycle arrest and A3H inactivation functions in HIV-1 VifIdentification of the HIV-1 Vif and Human APOBEC3G Protein Interface.Host restriction factors in retroviral infection: promises in virus-host interaction.Human cellular restriction factors that target HIV-1 replication.Defining HIV-1 Vif residues that interact with CBFβ by site-directed mutagenesis.HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.Dispersed and conserved hydrophobic residues of HIV-1 Vif are essential for CBFβ recruitment and A3G suppression.CBFβ enhances de novo protein biosynthesis of its binding partners HIV-1 Vif and RUNX1 and potentiates the Vif-induced degradation of APOBEC3G.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.
P2860
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P2860
A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 17 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
A patch of positively charged ...... its interaction with APOBEC3G.
@en
A patch of positively charged ...... its interaction with APOBEC3G.
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type
label
A patch of positively charged ...... its interaction with APOBEC3G.
@en
A patch of positively charged ...... its interaction with APOBEC3G.
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prefLabel
A patch of positively charged ...... its interaction with APOBEC3G.
@en
A patch of positively charged ...... its interaction with APOBEC3G.
@nl
P2093
P2860
P356
P1433
P1476
A patch of positively charged ...... its interaction with APOBEC3G.
@en
P2093
Gongying Chen
Rongzhen Xu
Xiao-Fang Yu
P2860
P304
P356
10.1128/JVI.00653-09
P407
P577
2009-06-17T00:00:00Z