Nucleocytoplasmic traffic disorder induced by cardioviruses. - Wikidata - thesis-toulmin - TriplyDB

Nucleocytoplasmic traffic disorder induced by cardioviruses.

Nucleocytoplasmic traffic disorder induced by cardioviruses.

http://www.wikidata.org/entity/Q34434945

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Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus Coxsackievirus B exits the host cell in shed microvesicles displaying autophagosomal markers NMR structure of the mengovirus Leader protein zinc-finger domain The Language of Life The encephalomyocarditis virus A conserved domain in the leader proteinase of foot-and-mouth disease virus is required for proper subcellular localization and function.Encephalomyocarditis virus Leader protein hinge domain is responsible for interactions with Ran GTPase.Suppression of injuries caused by a lytic RNA virus (mengovirus) and their uncoupling from viral reproduction by mutual cell/virus disarmament.Influence of heart failure on nucleocytoplasmic transport in human cardiomyocytes.Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.Fluorescent proteins and their applications in imaging living cells and tissues.SUMOylation promotes PML degradation during encephalomyocarditis virus infection.Regulation of mRNA trafficking by nuclear pore complexes.Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinases Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase Mutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site.Polypyrimidine tract binding protein-1 (PTB1) is a determinant of the tissue and host tropism of a human rhinovirus/poliovirus chimera PV1(RIPO).Rhinovirus 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 proteins A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport.Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment.The leader protein of cardioviruses inhibits stress granule assembly.Inoculation of swine with foot-and-mouth disease SAP-mutant virus induces early protection against disease.Cellular protein modification by poliovirus: the two faces of poly(rC)-binding protein.Selective Removal of FG Repeat Domains from the Nuclear Pore Complex by Enterovirus 2A(pro)PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection Analysis of Venezuelan equine encephalitis virus capsid protein function in the inhibition of cellular transcription Degradation of nuclear factor kappa B during foot-and-mouth disease virus infection.Differential targeting of nuclear pore complex proteins in poliovirus-infected cells.hnRNPs Relocalize to the cytoplasm following infection with vesicular stomatitis virus.Inhibition of mRNA export and dimerization of interferon regulatory factor 3 by Theiler's virus leader protein.Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses Mengovirus-induced rearrangement of the nuclear pore complex: hijacking cellular phosphorylation machinery.Viral subversion of the nuclear pore complex.Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus.Random mutagenesis defines a domain of Theiler's virus leader protein that is essential for antagonism of nucleocytoplasmic trafficking and cytokine gene expression.Viral and host proteins involved in picornavirus life cycle Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a requirement for subsequent phosphorylation of cellular nucleoporins.Nuclear imprisonment: viral strategies to arrest host mRNA nuclear export.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

http://www.wikidata.org/entity/Q34434945

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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type

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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Nucleocytoplasmic traffic disorder induced by cardioviruses.

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JVI.80.6.2705-2717.2006

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Journal of Virology

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Nucleocytoplasmic traffic disorder induced by cardioviruses

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Alexei G Aminev

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Ann C Palmenberg

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Maryana V Bardina

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Peter V Lidsky

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Stanleyson Hato

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Vadim I Agol

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Vladimir Y Polyakov

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P2860

Mechanisms of Receptor-Mediated Nuclear Import and Nuclear Export

Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation

Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA

The apoptotic capability of coxsackievirus B3 is influenced by the efficient interaction between the capsid protein VP2 and the proapoptotic host protein Siva

The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA

Genistein, a specific inhibitor of tyrosine-specific protein kinases

La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate

Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

Encephalomyocarditis viral protein 2A localizes to nucleoli and inhibits cap-dependent mRNA translation.

The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes.

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2705-2717

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10.1128/JVI.80.6.2705-2717.2006

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6

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Eugene V Sheval

Frank J M van Kuppeveld

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16501080

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1395435

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