Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells
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The Vpr protein from HIV-1: distinct roles along the viral life cycleHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchThe β-Lactamase Assay: Harnessing a FRET Biosensor to Analyse Viral Fusion MechanismsLentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infectionCharacterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assayThe inhibition of assembly of HIV-1 virus-like particles by 3-O-(3',3'-dimethylsuccinyl) betulinic acid (DSB) is counteracted by Vif and requires its Zinc-binding domain.Fluorescent protein-tagged Vpr dissociates from HIV-1 core after viral fusion and rapidly enters the cell nucleus.The immunosuppressive properties of the HIV Vpr protein are linked to a single highly conserved residue, R90HIV-1 Vpr oligomerization but not that of Gag directs the interaction between Vpr and Gag.R88-APOBEC3Gm Inhibits the Replication of Both Drug-resistant Strains of HIV-1 and Viruses Produced From Latently Infected CellsHIV-1 Vpr stimulates NF-κB and AP-1 signaling by activating TAK1.Vif is largely absent from human immunodeficiency virus type 1 mature virions and associates mainly with viral particles containing unprocessed gag.Protein kinase A phosphorylation activates Vpr-induced cell cycle arrest during human immunodeficiency virus type 1 infection.Site-specific gene insertion mediated by a Cre-loxP-carrying lentiviral vector.The stoichiometry of Gag protein in HIV-1.The late-domain-containing protein p6 is the predominant phosphoprotein of human immunodeficiency virus type 1 particles.Understanding the molecular manipulation of DCAF1 by the lentiviral accessory proteins Vpr and Vpx.Nuclear export of Vpr is required for efficient replication of human immunodeficiency virus type 1 in tissue macrophagesCharacterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.Super-resolution imaging of ESCRT-proteins at HIV-1 assembly sites.Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesisVisualization of the intracellular behavior of HIV in living cells.Localization of HIV-1 Vpr to the nuclear envelope: impact on Vpr functions and virus replication in macrophagesA protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsid-condensed RNA to Vpr-bridged DNA.HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradationHuman immunodeficiency virus type 1 Vpr modulates cellular expression of UNG2 via a negative transcriptional effect.Limelight on two HIV/SIV accessory proteins in macrophage infection: is Vpx overshadowing Vpr?Delineating HIV-associated neurocognitive disorders using transgenic models: the neuropathogenic actions of Vpr.HIV-1 assembly, budding, and maturation.HIV1-viral protein R (Vpr) mutations: associated phenotypes and relevance for clinical pathologies.The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention.Proline 35 of human immunodeficiency virus type 1 (HIV-1) Vpr regulates the integrity of the N-terminal helix and the incorporation of Vpr into virus particles and supports the replication of R5-tropic HIV-1 in human lymphoid tissue ex vivo.Biochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag).Nuclear export of human immunodeficiency virus type 1 Vpr is not required for virion packaging.Human immunodeficiency virus type 1 Vpr: oligomerization is an essential feature for its incorporation into virus particles.Primate lentiviruses use at least three alternative strategies to suppress NF-κB-mediated immune activation.HIV-1 Vpr protein activates the NF-κB pathway to promote G2/M cell cycle arrest.Virion-Associated Vpr Alleviates a Postintegration Block to HIV-1 Infection of Dendritic Cells.Rodent cells support key functions of the human immunodeficiency virus type 1 pathogenicity factor Nef3D molecular models of whole HIV-1 virions generated with cellPACK.
P2860
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P2860
Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells
description
2000 nî lūn-bûn
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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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name
Human immunodeficiency virus t ...... osphorylated in infected cells
@ast
Human immunodeficiency virus t ...... osphorylated in infected cells
@en
type
label
Human immunodeficiency virus t ...... osphorylated in infected cells
@ast
Human immunodeficiency virus t ...... osphorylated in infected cells
@en
prefLabel
Human immunodeficiency virus t ...... osphorylated in infected cells
@ast
Human immunodeficiency virus t ...... osphorylated in infected cells
@en
P2093
P2860
P1433
P1476
Human immunodeficiency virus t ...... osphorylated in infected cells
@en
P2093
Kräusslich HG
Schubert U
P2860
P304
P356
10.1128/JVI.74.20.9727-9731.2000
P577
2000-10-01T00:00:00Z