Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex.
about
The Vpr protein from HIV-1: distinct roles along the viral life cycleLEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexesThe human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrestEarly steps of retrovirus replicative cycleIdentification of the 15FRFG domain in HIV-1 Gag p6 essential for Vpr packaging into the virionHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchNuclear trafficking of retroviral RNAs and Gag proteins during late steps of replicationNuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 VprThe functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.Activation of the ATR pathway by human immunodeficiency virus type 1 Vpr involves its direct binding to chromatin in vivoCharacterization 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.Molecular Mechanisms of Neurodegenerative Diseases Induced by Human Retroviruses: A Review.Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr.Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cellsVpr-host interactions during HIV-1 viral life cycle.Functional analysis of the simian immunodeficiency virus Vpx protein: identification of packaging determinants and a novel nuclear targeting domain.Nucleocytoplasmic shuttling by human immunodeficiency virus type 1 Vpr.Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1.Equine infectious anemia virus Gag p9 function in early steps of virus infection and provirus productionViruses, microorganisms and scientists meet the nuclear pore. Leysin, VD, Switzerland, February 26-March 1, 1998.The functions of the HIV1 protein Vpr and its action through the DCAF1.DDB1.Cullin4 ubiquitin ligase.Nup124p is a nuclear pore factor of Schizosaccharomyces pombe that is important for nuclear import and activity of retrotransposon Tf1.Nuclear import of the retrotransposon Tf1 is governed by a nuclear localization signal that possesses a unique requirement for the FXFG nuclear pore factor Nup124p.Novel nuclear herniations induced by nuclear localization of a viral proteinSubcellular localization and integration activities of rous sarcoma virus reverse transcriptase.Reassessment of the roles of integrase and the central DNA flap in human immunodeficiency virus type 1 nuclear importSimian immunodeficiency virus Vpx is imported into the nucleus via importin alpha-dependent and -independent pathwaysInsights into cellular factors that regulate HIV-1 replication in human cellsImpact of the central polypurine tract on the kinetics of human immunodeficiency virus type 1 vector transduction.HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic interventionEffect on HIV-1 gene expression, Tat-Vpr interaction and cell apoptosis by natural variants of HIV-1 Tat exon 1 and Vpr from Northern IndiaHIV infection of non-dividing cells: a divisive problem.Nuclear export of Vpr is required for efficient replication of human immunodeficiency virus type 1 in tissue macrophagesNovel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages.Host Factors in Retroviral Integration and the Selection of Integration Target Sites.A hard way to the nucleusEpstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.Characterization of HIV-1 vpr nuclear import: analysis of signals and pathways.
P2860
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P2860
Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
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
Interaction of the human immun ...... with the nuclear pore complex
@nl
Interaction of the human immun ...... with the nuclear pore complex.
@ast
Interaction of the human immun ...... with the nuclear pore complex.
@en
Interaction of the human immun ...... with the nuclear pore complex.
@en-gb
type
label
Interaction of the human immun ...... with the nuclear pore complex
@nl
Interaction of the human immun ...... with the nuclear pore complex.
@ast
Interaction of the human immun ...... with the nuclear pore complex.
@en
Interaction of the human immun ...... with the nuclear pore complex.
@en-gb
prefLabel
Interaction of the human immun ...... with the nuclear pore complex
@nl
Interaction of the human immun ...... with the nuclear pore complex.
@ast
Interaction of the human immun ...... with the nuclear pore complex.
@en
Interaction of the human immun ...... with the nuclear pore complex.
@en-gb
P2093
P2860
P1433
P1476
Interaction of the human immun ...... with the nuclear pore complex
@en
P2093
A V Albright
F González-Scarano
R A Fouchier
P2860
P304
P407
P577
1998-07-01T00:00:00Z