HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.

scientific article published on 14 January 2014

HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3. is …
instance of (P31):
scholarly articleQ13442814

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P6179Dimensions Publication ID1032349800
P356DOI10.1186/1742-4690-11-4
P932PMC publication ID3937519
P698PubMed publication ID24422669
P5875ResearchGate publication ID259722877

P50authorXiaohong ZhouQ58925345
P2093author name stringXiao-Fang Yu
Xue Han
Arne Schön
Ernesto Freire
Sean L Evans
Qimeng Gao
P2860cites workLow conservation of functional domains of HIV type 1 vif and vpr genes in infected mothers correlates with lack of vertical transmissionQ43680750
Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.Q52224746
Characterization of a novel Cullin5 binding domain in HIV-1 Vif.Q52582151
T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restrictionQ24300389
The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNAQ24305266
Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F.Q24544264
The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradationQ24657375
Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assemblyQ24658171
Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif proteinQ27860488
Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF ComplexQ28210666
The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complexQ28474177
Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsQ28482052
Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databasesQ29617578
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 VifQ29618938
HIV-1 accessory proteins--ensuring viral survival in a hostile environmentQ29619538
Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded VifQ33826857
Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G.Q33910672
Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complexQ34034114
Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infectionQ34242229
Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions.Q35214620
Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F.Q35947612
Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif.Q37153444
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.Q37333725
A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.Q37333859
Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging processQ39612144
Different interaction between HIV-1 Vif and its cellular target proteins APOBEC3G/APOBEC3F.Q39725954
Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interactionQ39962552
Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F.Q39964772
A zinc-binding region in Vif binds Cul5 and determines cullin selectionQ40288287
Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif.Q40306250
Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif functionQ40444285
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteinesQ40485825
Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradationQ40485830
Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathwayQ40607865
Differential requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor betaQ41878042
Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factorsQ41878273
Dissection of the HIV Vif interaction with human E3 ubiquitin ligaseQ41963681
Conservation of amino-acid sequence motifs in lentivirus Vif proteinsQ42598893
Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G bindingQ42910736
CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression.Q43239447
P304page(s)4
P577publication date2014-01-14
P1433published inRetrovirologyQ15793508
P1476titleHIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.
P478volume11