Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores.
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Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusionUbiquitylation-dependent localization of PLK1 in mitosisPicornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virusRe-localization of cellular protein SRp20 during poliovirus infection: bridging a viral IRES to the host cell translation apparatusStable formation of compositionally unique stress granules in virus-infected cells.A conserved domain in the leader proteinase of foot-and-mouth disease virus is required for proper subcellular localization and function.Viable polioviruses that encode 2A proteins with fluorescent protein tags.A critical role of a cellular membrane traffic protein in poliovirus RNA replicationHormonal regulation of nuclear permeabilitySpecific cleavage of the nuclear pore complex protein Nup62 by a viral proteasePoliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1.Nucleocytoplasmic traffic disorder induced by cardioviruses.Polypyrimidine tract binding protein-1 (PTB1) is a determinant of the tissue and host tropism of a human rhinovirus/poliovirus chimera PV1(RIPO).Increased long chain acyl-Coa synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organellesRhinovirus 3C protease facilitates specific nucleoporin cleavage and mislocalisation of nuclear proteins in infected host cells.BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteinsA picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport.Impact of Leishmania infection on host macrophage nuclear physiology and nucleopore complex integrity.Far upstream element binding protein 1 binds the internal ribosomal entry site of enterovirus 71 and enhances viral translation and viral growth.Inoculation of swine with foot-and-mouth disease SAP-mutant virus induces early protection against disease.Alterations in nuclear pore architecture allow cancer cell entry into or exit from drug-resistant dormancy.Cellular protein modification by poliovirus: the two faces of poly(rC)-binding protein.Additive Promotion of Viral Internal Ribosome Entry Site-Mediated Translation by Far Upstream Element-Binding Protein 1 and an Enterovirus 71-Induced Cleavage Product.Selective Removal of FG Repeat Domains from the Nuclear Pore Complex by Enterovirus 2A(pro)Cardiovirus 2A protein associates with 40S but not 80S ribosome subunits during infection.Differential targeting of nuclear pore complex proteins in poliovirus-infected cells.Monitoring the disruption of nuclear envelopes in interphase cells with GFP-beta-galactosidase.Viral proteinase requirements for the nucleocytoplasmic relocalization of cellular splicing factor SRp20 during picornavirus infections.Thiouracil cross-linking mass spectrometry: a cell-based method to identify host factors involved in viral amplification.Poliovirus infection induces the co-localization of cellular protein SRp20 with TIA-1, a cytoplasmic stress granule protein.Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardiovirusesMengovirus-induced rearrangement of the nuclear pore complex: hijacking cellular phosphorylation machinery.Viral subversion of the nuclear pore complex.Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport.Nuclear imprisonment: viral strategies to arrest host mRNA nuclear export.Viral subversion of nucleocytoplasmic traffickingEnterovirus 2Apro targets MDA5 and MAVS in infected cells.Functional roles of HIV-1 Tat protein in the nucleus.Cytoplasmic translocation, aggregation, and cleavage of TDP-43 by enteroviral proteases modulate viral pathogenesisThe multifaceted poliovirus 2A protease: regulation of gene expression by picornavirus proteases.
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P2860
Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on September 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Bidirectional increase in perm ...... alterations of nuclear pores.
@en
Bidirectional increase in perm ...... alterations of nuclear pores.
@nl
type
label
Bidirectional increase in perm ...... alterations of nuclear pores.
@en
Bidirectional increase in perm ...... alterations of nuclear pores.
@nl
prefLabel
Bidirectional increase in perm ...... alterations of nuclear pores.
@en
Bidirectional increase in perm ...... alterations of nuclear pores.
@nl
P2093
P2860
P1433
P1476
Bidirectional increase in perm ...... g alterations of nuclear pores
@en
P2093
Denise Egger
Kurt Bienz
Olga V Mikitas
Peter V Lidsky
Vadim I Agol
P2860
P304
10166-10177
P356
10.1128/JVI.78.18.10166-10177.2004
P407
P577
2004-09-01T00:00:00Z