Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors
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Suppression of APOBEC3-mediated restriction of HIV-1 by VifThe Road Less Traveled: HIV's Use of Alternative Routes through Cellular PathwaysCharacterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsInhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3GIdentification of HIV-1 Vif regions required for CBF-β interaction and APOBEC3 suppressionA conflict of interest: the evolutionary arms race between mammalian APOBEC3 and lentiviral Vif.Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complexCore binding factor beta plays a critical role by facilitating the assembly of the Vif-cullin 5 E3 ubiquitin ligase.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.Role of cullin-elonginB-elonginC E3 complex in bovine immunodeficiency virus and maedi-visna virus Vif-mediated degradation of host A3Z2-Z3 proteinsCore-binding factor subunit beta is not required for non-primate lentiviral Vif-mediated APOBEC3 degradation.Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein. Importance of the C-terminal unstructured tail.Cellular requirements for bovine immunodeficiency virus Vif-mediated inactivation of bovine APOBEC3 proteins.Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligaseVif determines the requirement for CBF-β in APOBEC3 degradationThe HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.Evolutionarily conserved pressure for the existence of distinct G2/M cell cycle arrest and A3H inactivation functions in HIV-1 VifLineage-Specific Viral Hijacking of Non-canonical E3 Ubiquitin Ligase Cofactors in the Evolution of Vif Anti-APOBEC3 Activity.Evolutionary Paradigms from Ancient and Ongoing Conflicts between the Lentiviral Vif Protein and Mammalian APOBEC3 Enzymes.Transcriptional regulation of APOBEC3 antiviral immunity through the CBF-β/RUNX axis.Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination.Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif.Temporal proteomic analysis of HIV infection reveals remodelling of the host phosphoproteome by lentiviral Vif variantsDefining 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.Macaque-tropic human immunodeficiency virus type 1: breaking out of the host restriction factorsHost restriction of lentiviruses and viral countermeasures: APOBEC3 and Vif.APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.Clues for two-step virion infectivity factor regulation by core binding factor beta.Conserved Interaction of Lentiviral Vif Molecules with HIV-1 Gag and Differential Effects of Species-Specific Vif on Virus Production.CBFß and HIV Infection.An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation.Differential requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor beta.Making Sense of Multifunctional Proteins: Human Immunodeficiency Virus Type 1 Accessory and Regulatory Proteins and Connections to Transcription.HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor β on genetically distinct surfaces.CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression.SIVmac239 Vif and Human APOBEC3B Interactions Resemble Those Between HIV-1 Vif and Human APOBEC3G.
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P2860
Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Vif proteins of human and simi ...... de APOBEC3 restriction factors
@en
type
label
Vif proteins of human and simi ...... de APOBEC3 restriction factors
@en
prefLabel
Vif proteins of human and simi ...... de APOBEC3 restriction factors
@en
P2093
P2860
P356
P1433
P1476
Vif proteins of human and simi ...... de APOBEC3 restriction factors
@en
P2093
Judd F Hultquist
Mawuena Binka
Rebecca S LaRue
P2860
P304
P356
10.1128/JVI.06950-11
P407
P577
2011-12-28T00:00:00Z