Viral protein R regulates nuclear import of the HIV-1 pre-integration complex - Wikidata - awgldk - TriplyDB

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

http://www.wikidata.org/entity/Q24533072

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The Vpr protein from HIV-1: distinct roles along the viral life cycle HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1 nuclear import and replication HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome Human immunodeficiency virus type 1 Vpr-dependent cell cycle arrest through a mitogen-activated protein kinase signal transduction pathway 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 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 Maedi-visna virus and caprine arthritis encephalitis virus genomes encode a Vpr-like but no Tat protein Early steps of retrovirus replicative cycle Analysis of HIV-1 Vpr determinants responsible for cell growth arrest in Saccharomyces cerevisiae Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin Visualizing Vpr-induced G2 arrest and apoptosis 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 Where in the Cell Are You? Probing HIV-1 Host Interactions through Advanced Imaging Techniques Differential effects of the SR proteins 9G8, SC35, ASF/SF2, and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA 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 The packaging signal of influenza viral RNA molecules.CNI-H0294, a nuclear importation inhibitor of the human immunodeficiency virus type 1 genome, abrogates virus replication in infected activated peripheral blood mononuclear cells.Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr A viral-human interactome based on structural motif-domain interactions captures the human infectome 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.Fluorescent protein-tagged Vpr dissociates from HIV-1 core after viral fusion and rapidly enters the cell nucleus.Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40.Human immunodeficiency virus type 1 Vpr interacts with antiapoptotic mitochondrial protein HAX-1 Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.Regulation of HIV-1 transcription in cells of the monocyte-macrophage lineage.Nuclear targeting of the cauliflower mosaic virus coat protein Flexible use of nuclear import pathways by HIV-1.Molecular Mechanisms of Neurodegenerative Diseases Induced by Human Retroviruses: A Review.A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate.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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Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

http://www.wikidata.org/entity/Q24533072

description

1998 nî lūn-bûn

@nan

1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին հրատարակված գիտական հոդված

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1998年の論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年论文

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name

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

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Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@en

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

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Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

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type

label

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@ast

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@en

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@en-gb

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@nl

prefLabel

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@ast

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@en

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

@en-gb

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

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The EMBO Journal

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Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

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P2093

C M Lane

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

G Zybarth

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

L Ratner

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

M A Lee

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M Bukrinsky

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M Rexach

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M S Moore

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

S Popov

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

P2860

Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences

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

Identification of different roles for RanGDP and RanGTP in nuclear protein import

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

Active nuclear import of human immunodeficiency virus type 1 preintegration complexes

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

The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes

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

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909-17

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

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scholarly article

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2905396

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10.1093/EMBOJ/17.4.909

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P407

P433

4

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P478

17

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Norbert Reiling

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1998-02-16T00:00:00Z

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13768231

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9463369

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1170440

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