Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport. - Wikidata - thesis-toulmin - TriplyDB

Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport.

Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport.

http://www.wikidata.org/entity/Q37247979

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Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells Respiratory virus modulation of host nucleocytoplasmic transport; target for therapeutic intervention?Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export Multiple classes of antiviral agents exhibit in vitro activity against human rhinovirus type C Assembly of recombinant Israeli Acute Paralysis Virus capsids.Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease Volatile emanations from in vitro airway cells infected with human rhinovirus.Rhinovirus 3C protease facilitates specific nucleoporin cleavage and mislocalisation of nuclear proteins in infected host cells.Impact of Leishmania infection on host macrophage nuclear physiology and nucleopore complex integrity.Measles Virus Matrix Protein Inhibits Host Cell Transcription.Chromatinized Protein Kinase C-θ: Can It Escape the Clutches of NF-κB?Selective Removal of FG Repeat Domains from the Nuclear Pore Complex by Enterovirus 2A(pro)Rhinovirus 16 2A Protease Affects Nuclear Localization of 3CD during Infection Nuclear imprisonment: viral strategies to arrest host mRNA nuclear export.Viral subversion of nucleocytoplasmic trafficking Differential processing of nuclear pore complex proteins by rhinovirus 2A proteases from different species and serotypes.Enteroviral proteases: structure, host interactions and pathogenicity.PKC-Theta is a Novel SC35 Splicing Factor Regulator in Response to T Cell Activation Picornaviruses and Apoptosis: Subversion of Cell Death Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation.VPg unlinkase/TDP2 in cardiovirus infected cells: Re-localization and proteolytic cleavage.Exploitation of nuclear functions by human rhinovirus, a cytoplasmic RNA virus

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Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport.

http://www.wikidata.org/entity/Q37247979

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 29 April 2009

@en

vedecký článok

@sk

vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

name

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

@en

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

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type

label

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

@en

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

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prefLabel

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

@en

Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

@nl

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Journal of Virology

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Rhinovirus 3C protease can loc ...... e nucleocytoplasmic transport.

@en

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Benjamin Jordan

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

David A Jans

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

Dongsheng Li

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

Hayat Dagher

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

James E Gern

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

Phillip G Bardin

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

Reena Ghildyal

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

P2860

Novel properties of the protein kinase CK2-site-regulated nuclear- localization sequence of the interferon-induced nuclear factor IFI 16

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Role of prodomain in importin-mediated nuclear localization and activation of caspase-2

Transport into and out of the nucleus.

Nuclear targeting signal recognition: a key control point in nuclear transport?

Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus.

Rhinovirus 3C protease precursors 3CD and 3CD' localize to the nuclei of infected cells.

Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition.

Differential targeting of nuclear pore complex proteins in poliovirus-infected cells.

P304

7349-7352

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scholarly article

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10.1128/JVI.01748-08

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14

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83

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2009-04-29T00:00:00Z

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19403669

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2704779

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