The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex - Test2 - elhamkhani - TriplyDB

The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex

The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex

http://www.wikidata.org/entity/Q28474177

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Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all Suppression of APOBEC3-mediated restriction of HIV-1 by Vif Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif.APOBEC3A is a specific inhibitor of the early phases of HIV-1 infection in myeloid cells.Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity.Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC.Role of cullin-elonginB-elonginC E3 complex in bovine immunodeficiency virus and maedi-visna virus Vif-mediated degradation of host A3Z2-Z3 proteins Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif.Structural insights for HIV-1 therapeutic strategies targeting Vif.The role of BST2/tetherin in feline retrovirus infection Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligase Identification of a Cullin5-ElonginB-ElonginC E3 complex in degradation of feline immunodeficiency virus Vif-mediated feline APOBEC3 proteins Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination.Hydrodynamic and functional analysis of HIV-1 Vif oligomerization.HIV Restriction Factors and Mechanisms of Evasion.The Role of Elongin BC-Containing Ubiquitin Ligases.Running loose or getting lost: how HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif protein Host restriction factors in retroviral infection: promises in virus-host interaction.Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource.APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.HIV-host interactome revealed directly from infected cells.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 variants HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.Immune regulator ABIN1 suppresses HIV-1 transcription by negatively regulating the ubiquitination of Tat.Dispersed and conserved hydrophobic residues of HIV-1 Vif are essential for CBFβ recruitment and A3G suppression.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.Determinants of efficient degradation of APOBEC3 restriction factors by HIV-1 Vif.An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation.Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif Control of HIV infection by IFN-α: implications for latency and a cure.Gene loss and adaptation to hominids underlie the ancient origin of HIV-1.CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression.[The adaptation of lentiviruses to apes was a crucial step in the origin of HIV-1].Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway.

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The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex

http://www.wikidata.org/entity/Q28474177

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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type

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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JOURNAL.PPAT.1000925

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The SOCS-box of HIV-1 Vif inte ...... ining ubiquitin ligase complex

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Dennis A Veselkov

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Hendrik Huthoff

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Julien R C Bergeron

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Mark R Sanderson

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Peter J Simpson

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Rebecca L Beavil

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P2860

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F.

The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly

Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation

Structure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR Degradation

The SOCS Box Domain of SOCS3: Structure and Interaction with the ElonginBC-Cullin5 Ubiquitin Ligase

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

Using NMRView to visualize and analyze the NMR spectra of macromolecules

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e1000925

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scholarly article

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2266341

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10.1371/JOURNAL.PPAT.1000925

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6

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6

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Michael Henry Malim

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2010-06-03T00:00:00Z

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44657906

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20532212

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2880568

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