The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
about
New insights into an X-traordinary viral proteinStructural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolaseTetramerization of SAMHD1 is required for biological activity and inhibition of HIV infectionThe mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTPDistinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4BCullin4A and cullin4B are interchangeable for HIV Vpr and Vpx action through the CRL4 ubiquitin ligase complexImmune Activation Influences SAMHD1 Expression and Vpx-mediated SAMHD1 Degradation during Chronic HIV-1 InfectionThe ribonuclease activity of SAMHD1 is required for HIV-1 restrictionIdentification of cellular proteins interacting with the retroviral restriction factor SAMHD1Nuclear 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.dNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.Development of monoclonal antibodies specifically recognizing the endogenous sterile alpha motif and HD domain 1 protein in porcine cell lines.Host factor SAMHD1 restricts DNA viruses in non-dividing myeloid cellsIdentification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradationSAMHD1 restricts HIV-1 replication and regulates interferon production in mouse myeloid cells.Molecular determinants for recognition of divergent SAMHD1 proteins by the lentiviral accessory protein Vpx.SAMHD1 specifically restricts retroviruses through its RNase activity.SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation.Restriction of HIV-1 Requires the N-Terminal Region of MxB as a Capsid-Binding Motif but Not as a Nuclear Localization SignalPhosphorylation of mouse SAMHD1 regulates its restriction of human immunodeficiency virus type 1 infection, but not murine leukemia virus infection.Host restriction factors in retroviral infection: promises in virus-host interaction.Interferon block to HIV-1 transduction in macrophages despite SAMHD1 degradation and high deoxynucleoside triphosphates supplyRestriction of diverse retroviruses by SAMHD1.Mouse SAMHD1 has antiretroviral activity and suppresses a spontaneous cell-intrinsic antiviral response.HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradationAnti-HIV host factor SAMHD1 regulates viral sensitivity to nucleoside reverse transcriptase inhibitors via modulation of cellular deoxyribonucleoside triphosphate (dNTP) levels.The HIV-1 protein Vpr targets the endoribonuclease Dicer for proteasomal degradation to boost macrophage infectionMacrophages in Progressive Human Immunodeficiency Virus/Simian Immunodeficiency Virus Infections.Host Factors and HIV-1 Replication: Clinical Evidence and Potential Therapeutic ApproachesInhibition of CUL4A Neddylation causes a reversible block to SAMHD1-mediated restriction of HIV-1TLR7/8 agonist induces a post-entry SAMHD1-independent block to HIV-1 infection of monocytes.Host SAMHD1 protein promotes HIV-1 recombination in macrophages.HIV type 1 infection of plasmacytoid and myeloid dendritic cells is restricted by high levels of SAMHD1 and cannot be counteracted by Vpx.Cellular and Biochemical Mechanisms of the Retroviral Restriction Factor SAMHD1.Macaque-tropic human immunodeficiency virus type 1: breaking out of the host restriction factorsDegradation of SAMHD1 by Vpx Is Independent of Uncoating.Current views on HIV-1 latency, persistence, and cure.A Highly Active Isoform of Lentivirus Restriction Factor SAMHD1 in Mouse.Roles of SAMHD1 in antiviral defense, autoimmunity and cancer.
P2860
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P2860
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@ast
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@en
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@nl
type
label
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@ast
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@en
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@nl
prefLabel
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@ast
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@en
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@nl
P2093
P2860
P356
P1433
P1476
The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.
@en
P2093
Eric C Logue
Henning Hofmann
Megan L Schultz
Nathaniel R Landau
Nicolin Bloch
Sylvie B Polsky
Waaqo Daddacha
P2860
P304
12552-12560
P356
10.1128/JVI.01657-12
P407
P577
2012-09-12T00:00:00Z