Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1. - Wikidata - wikimedia - TriplyDB

Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1.

Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1.

http://www.wikidata.org/entity/Q34149318

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 HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest Early steps of retrovirus replicative cycle HIV Genome-Wide Protein Associations: a Review of 30 Years of Research Cellular and viral determinants of retroviral nuclear entry Nuclear trafficking of retroviral RNAs and Gag proteins during late steps of replication A review on computational systems biology of pathogen-host interactions Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr 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.Fluorescent protein-tagged Vpr dissociates from HIV-1 core after viral fusion and rapidly enters the cell nucleus.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.Vpr-host interactions during HIV-1 viral life cycle.Network-based prediction and analysis of HIV dependency factors HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation.Caspases target only two architectural components within the core structure of the nuclear pore complex.HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention Supervised learning and prediction of physical interactions between human and HIV proteins HIV infection of non-dividing cells: a divisive problem.HIV-1 remodels the nuclear pore complex Cellular phenotype impacts human immunodeficiency virus type 1 viral protein R subcellular localization Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages.A hard way to the nucleus Nuclear translocation as a novel target for anti-HIV drugs.Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.Localization of HIV-1 Vpr to the nuclear envelope: impact on Vpr functions and virus replication in macrophages A 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 Vpr: mechanisms of G2 arrest and apoptosis.Viral subversion of the nuclear pore complex.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Insertion of a classical nuclear import signal into the matrix domain of the Rous sarcoma virus Gag protein interferes with virus replication.HIV-1 Vpr-a still "enigmatic multitasker".The HIV-1 passage from cytoplasm to nucleus: the process involving a complex exchange between the components of HIV-1 and cellular machinery to access nucleus and successful integration.Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr).The roles of the nuclear pore complex in cellular dysfunction, aging and disease.

P2860

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P2860

Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1.

http://www.wikidata.org/entity/Q34149318

description

2002 nî lūn-bûn

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2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

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2002年論文

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2002年論文

@zh-hant

2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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type

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Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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prefLabel

Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

@ast

Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

@en

Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

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P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Docking of HIV-1 Vpr to the nu ...... ion with the nucleoporin hCG1.

@en

P2093

Cecilia Rustum

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

Erwann Le Rouzic

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

Françoise Stutz

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

P2860

A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1

The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p

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

The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human

Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to 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

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

A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus

The yeast nuclear pore complex: composition, architecture, and transport mechanism

P304

45091-45098

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scholarly article

P356

10.1074/JBC.M207439200

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P433

47

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P478

277

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P50

Catherine Dargemont

Aurelie Mousnier

P577

2002-09-12T00:00:00Z

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P5875

11161972

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P698

12228227

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