Analysis of the interaction of influenza virus polymerase complex with human cell factors. - Wikidata - awgldk - TriplyDB

Analysis of the interaction of influenza virus polymerase complex with human cell factors.

Analysis of the interaction of influenza virus polymerase complex with human cell factors.

http://www.wikidata.org/entity/Q33336123

about

hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel transcription-dependent shuttling RNA-transporting complex The structure of a biologically active influenza virus ribonucleoprotein complex Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 Subunit The interactomes of influenza virus NS1 and NS2 proteins identify new host factors and provide insights for ADAR1 playing a supportive role in virus replication Generation and comprehensive analysis of an influenza virus polymerase cellular interaction network Airborne transmission of highly pathogenic H7N1 influenza virus in ferrets Cellular RNA binding proteins NS1-BP and hnRNP K regulate influenza A virus RNA splicing Chemical Genomics Identifies the PERK-Mediated Unfolded Protein Stress Response as a Cellular Target for Influenza Virus Inhibition Specific residues of PB2 and PA influenza virus polymerase subunits confer the ability for RNA polymerase II degradation and virus pathogenicity in mice Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Full factorial analysis of mammalian and avian influenza polymerase subunits suggests a role of an efficient polymerase for virus adaptation Interspecies transmission and host restriction of avian H5N1 influenza virus.Networks of Host Factors that Interact with NS1 Protein of Influenza A Virus Molecular mechanisms of interspecies transmission and pathogenicity of influenza viruses: Lessons from the 2009 pandemic.The RNA polymerase PB2 subunit of influenza A/HongKong/156/1997 (H5N1) restricts the replication of reassortant ribonucleoprotein complexes [corrected]Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis.The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication.Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication.Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein.Nucleolin interacts with influenza A nucleoprotein and contributes to viral ribonucleoprotein complexes nuclear trafficking and efficient influenza viral replication.Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complex Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I.HMGB1 protein binds to influenza virus nucleoprotein and promotes viral replication Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity A comprehensive map of the influenza A virus replication cycle Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.Generation of replication-proficient influenza virus NS1 point mutants with interferon-hyperinducer phenotype.Cellular networks involved in the influenza virus life cycle.Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules.Current approaches on viral infection: proteomics and functional validations.Targeting Viral Proteostasis Limits Influenza Virus, HIV, and Dengue Virus Infection.Thiouracil cross-linking mass spectrometry: a cell-based method to identify host factors involved in viral amplification.Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection.PB2 protein of a highly pathogenic avian influenza virus strain A/chicken/Yamaguchi/7/2004 (H5N1) determines its replication potential in pigs Exploration of binary virus-host interactions using an infectious protein complementation assay

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P2860

Analysis of the interaction of influenza virus polymerase complex with human cell factors.

http://www.wikidata.org/entity/Q33336123

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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Analysis of the interaction of ...... mplex with human cell factors.

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Eva Torreira

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Juan Ortín

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Juan Pablo Albar

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Noelia Zamarreño

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Núria Jorba

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Pablo Gastaminza

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Silvia Juarez

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P2860

A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum

hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells

Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system

Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes

Influenza virus NS1 protein interacts with viral transcription-replication complexes in vivo.

Characterization of an RNA granule from developing brain.

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2077-2088

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10.1002/PMIC.200700508

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10

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8

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18491320

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