Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection - Wikidata - wikimedia - TriplyDB

Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection

Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection

http://www.wikidata.org/entity/Q28472652

about

SAMHD1-deficient CD14+ cells from individuals with Aicardi-Goutières syndrome are highly susceptible to HIV-1 infection New insights into an X-traordinary viral protein SAMHD1-Dependent and -Independent Functions of HIV-2/SIV Vpx Protein The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover The human immunodeficiency virus type 2 Vpx protein usurps the CUL4A-DDB1 DCAF1 ubiquitin ligase to overcome a postentry block in macrophage infection HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein Formation of mobile chromatin-associated nuclear foci containing HIV-1 Vpr and VPRBP is critical for the induction of G2 cell cycle arrest The Expression of Functional Vpx during Pathogenic SIVmac Infections of Rhesus Macaques Suppresses SAMHD1 in CD4+ Memory T Cells Structural basis of lentiviral subversion of a cellular protein degradation pathway The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction Proteomic approaches to uncovering virus-host protein interactions during the progression of viral infection Hepatitis B: progress in understanding chronicity, the innate immune response, and cccDNA protection Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B Cullin4A and cullin4B are interchangeable for HIV Vpr and Vpx action through the CRL4 ubiquitin ligase complex SAMHD1 restricts HIV-1 infection in resting CD4(+) T cells.Interactions with DCAF1 and DDB1 in the CRL4 E3 ubiquitin ligase are required for Vpr-mediated G2 arrest.Interaction of Vpx and apolipoprotein B mRNA-editing catalytic polypeptide 3 family member A (APOBEC3A) correlates with efficient lentivirus infection of monocytes Host hindrance to HIV-1 replication in monocytes and macrophages.HIV-1 Vpr and G2 cell cycle arrest.The functions of the HIV1 protein Vpr and its action through the DCAF1.DDB1.Cullin4 ubiquitin ligase.Nuclear import of SAMHD1 is mediated by a classical karyopherin α/β1 dependent pathway and confers sensitivity to VpxMAC induced ubiquitination and proteasomal degradation.Effects of human SAMHD1 polymorphisms on HIV-1 susceptibility.SIV Nef proteins recruit the AP-2 complex to antagonize Tetherin and facilitate virion release.APOBEC3A is a specific inhibitor of the early phases of HIV-1 infection in myeloid cells.dNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1.Contribution of SAM and HD domains to retroviral restriction mediated by human SAMHD1.The retroviral restriction ability of SAMHD1, but not its deoxynucleotide triphosphohydrolase activity, is regulated by phosphorylation Development of monoclonal antibodies specifically recognizing the endogenous sterile alpha motif and HD domain 1 protein in porcine cell lines.Hepatitis B virus HBx protein interactions with the ubiquitin proteasome system.The inside out of lentiviral vectors Cyclin L2 is a critical HIV dependency factor in macrophages that controls SAMHD1 abundance.Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1.Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention Understanding the molecular manipulation of DCAF1 by the lentiviral accessory proteins Vpr and Vpx.Human immunodeficiency virus type 1 modified to package Simian immunodeficiency virus Vpx efficiently infects macrophages and dendritic cells.Vpx rescues HIV-1 transduction of dendritic cells from the antiviral state established by type 1 interferon.

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Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection

http://www.wikidata.org/entity/Q28472652

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Lentiviral Vpx accessory facto ...... to enable macrophage infection

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Jacek Skowronski

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Selene K Swanson

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Smita Srivastava

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P2860

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

The Vpr protein from HIV-1: distinct roles along the viral life cycle

HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase

The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage

A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1

Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases

Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infection

Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor

Localization of the Vpx packaging signal within the C terminus of the human immunodeficiency virus type 2 Gag precursor protein

Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest

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Laurence Florens

Michael P. Washburn

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2008-05-09T00:00:00Z

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5269271

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2330158

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