HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection - Test2 - elhamkhani - TriplyDB

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

http://www.wikidata.org/entity/Q24608690

about

The Vpr protein from HIV-1: distinct roles along the viral life cycle Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1 nuclear import and replication Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex.LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes HIV-1 Vpr induces defects in mitosis, cytokinesis, nuclear structure, and centrosomes Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest Early steps of retrovirus replicative cycle Identification of the 15FRFG domain in HIV-1 Gag p6 essential for Vpr packaging into the virion Analysis of HIV-1 Vpr determinants responsible for cell growth arrest in Saccharomyces cerevisiae HIV Genome-Wide Protein Associations: a Review of 30 Years of Research Misdelivery at the Nuclear Pore Complex-Stopping a Virus Dead in Its Tracks Nuclear trafficking of retroviral RNAs and Gag proteins during late steps of replication Formation of mobile chromatin-associated nuclear foci containing HIV-1 Vpr and VPRBP is critical for the induction of G2 cell cycle arrest NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr Solution structure of human immunodeficiency virus type 1 Vpr(13-33) peptide in micelles Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase.In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions Anti-cancer effect of HIV-1 viral protein R on doxorubicin resistant neuroblastoma Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr Synthesis of a Vpr-Binding Derivative for Use as a Novel HIV-1 Inhibitor The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest.Human immunodeficiency virus type 1 Vpr interacts with antiapoptotic mitochondrial protein HAX-1 Pathogenesis of HIV-1 infection within bone marrow cells.Characterization of the molecular determinants of primary HIV-1 Vpr proteins: impact of the Q65R and R77Q substitutions on Vpr functions.Regulation of HIV-1 transcription in cells of the monocyte-macrophage lineage.Ex vivo comparison of microbicide efficacies for preventing HIV-1 genomic integration in intraepithelial vaginal cells R77Q and Q3R HIV1-VPR mutations in an otherwise asymptomatic 5-year-old child with repeated ear infections Mutational analysis of Vpr-induced G2 arrest, nuclear localization, and cell death in fission yeast.Moloney murine leukemia virus infects cells of the developing hair follicle after neonatal subcutaneous inoculation in mice.The ataxia telangiectasia-mutated and Rad3-related protein is dispensable for retroviral integration Molecular Mechanisms of Neurodegenerative Diseases Induced by Human Retroviruses: A Review.Human immunodeficiency virus type 1 vpr induces apoptosis through caspase activation A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly

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P2860

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

http://www.wikidata.org/entity/Q24608690

description

1998 nî lūn-bûn

@nan

1998 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1998年の論文

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1998年論文

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1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@ast

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@en

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@nl

type

label

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

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HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@en

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@nl

prefLabel

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@ast

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@en

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@nl

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Genes & Development

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HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

@en

P2093

D M Koepp

http://www.w3.org/2001/XMLSchema#string

M A Vodicka

http://www.w3.org/2001/XMLSchema#string

M Emerman

http://www.w3.org/2001/XMLSchema#string

P A Silver

http://www.w3.org/2001/XMLSchema#string

P2860

A novel class of RanGTP binding proteins

Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62

Sequence and characterization of cytoplasmic nuclear protein import factor p97

Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope

A novel receptor-mediated nuclear protein import pathway

Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex

Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins

Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes

The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells

Critical role of reverse transcriptase in the inhibitory mechanism of CNI-H0294 on HIV-1 nuclear translocation

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175-85

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scholarly article

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4702219

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10.1101/GAD.12.2.175

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2

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12

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1998-01-15T00:00:00Z

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13793511

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9436978

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P932

316441

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