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Poliovirus-mediated disruption of cytoplasmic processing bodies

Poliovirus-mediated disruption of cytoplasmic processing bodies

http://www.wikidata.org/entity/Q30155985

about

HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies Who Regulates Whom? An Overview of RNA Granules and Viral Infections Enterovirus Control of Translation and RNA Granule Stress Responses Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses The yin and yang of hepatitis C: synthesis and decay of hepatitis C virus RNA Hepatitis C Virus Exploitation of Processing Bodies Use of Cellular Decapping Activators by Positive-Strand RNA Viruses Diverse Strategies Used by Picornaviruses to Escape Host RNA Decay Pathways Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses XRN1 Is a Species-Specific Virus Restriction Factor in Yeasts IRAV (FLJ11286), an Interferon Stimulated Gene with Antiviral Activity Against Dengue Virus, Interacts with MOV10 Multiple classes of antiviral agents exhibit in vitro activity against human rhinovirus type C Differential restriction patterns of mRNA decay factor AUF1 during picornavirus infections.A candidate approach implicates the secreted Salmonella effector protein SpvB in P-body disassembly.A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability How do viruses interact with stress-associated RNA granules?Screening of small molecules affecting mammalian P-body assembly uncovers links with diverse intracellular processes and organelle physiology.Flaviviral RNAs: weapons and targets in the war between virus and host.Cytoplasmic viruses: rage against the (cellular RNA decay) machine.Strategies for viral RNA stability: live long and prosper The leader protein of cardioviruses inhibits stress granule assembly.Virus-induced translational arrest through 4EBP1/2-dependent decay of 5'-TOP mRNAs restricts viral infection.West nile virus infections suppress early viral RNA synthesis and avoid inducing the cell stress granule response.Recent progress in understanding coxsackievirus replication, dissemination, and pathogenesis.Rabies Virus Infection Induces the Formation of Stress Granules Closely Connected to the Viral Factories.Hepatitis C virus infection alters P-body composition but is independent of P-body granules.Picornavirus modification of a host mRNA decay protein.Modulation of hepatitis C virus RNA abundance and virus release by dispersion of processing bodies and enrichment of stress granules.Diversion of stress granules and P-bodies during viral infection.Interplay between viruses and host mRNA degradation Regulation of stress granules and P-bodies during RNA virus infection.Cytoplasmic RNA Granules and Viral Infection.Cellular mRNA decay protein AUF1 negatively regulates enterovirus and human rhinovirus infections.mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain.Attacked from All Sides: RNA Decay in Antiviral Defense.Regulation of stress granules in virus systems Inhibition and avoidance of mRNA degradation by RNA viruses.Tinkering with translation: protein synthesis in virus-infected cells.The P body protein LSm1 contributes to stimulation of hepatitis C virus translation, but not replication, by microRNA-122 P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication

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P2860

Poliovirus-mediated disruption of cytoplasmic processing bodies

http://www.wikidata.org/entity/Q30155985

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Poliovirus-mediated disruption of cytoplasmic processing bodies

@ast

Poliovirus-mediated disruption of cytoplasmic processing bodies

@en

type

label

Poliovirus-mediated disruption of cytoplasmic processing bodies

@ast

Poliovirus-mediated disruption of cytoplasmic processing bodies

@en

prefLabel

Poliovirus-mediated disruption of cytoplasmic processing bodies

@ast

Poliovirus-mediated disruption of cytoplasmic processing bodies

@en

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P1433

Journal of Virology

P1476

Poliovirus-mediated disruption of cytoplasmic processing bodies

@en

P2093

James P White

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

Jonathan D Dougherty

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

Richard E Lloyd

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

P2860

Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein

Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay.

A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing.

The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.

Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures

mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes

Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry

A role for the P-body component GW182 in microRNA function

Cytoplasmic foci are sites of mRNA decay in human cells

Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

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64-75

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scholarly article

P356

10.1128/JVI.01657-10

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1

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85

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2010-10-20T00:00:00Z

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20962086

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3014174

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