Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.
about
Mutations within the conserved NS1 nuclear export signal lead to inhibition of influenza A virus replicationInhibition of nuclear import by the proapoptotic protein CC3Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signalingInfluenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 proteinDeciphering the cellular pathway for transport of poly(A)-binding protein IISequence of the 1918 pandemic influenza virus nonstructural gene (NS) segment and characterization of recombinant viruses bearing the 1918 NS genes3' end mRNA processing: molecular mechanisms and implications for health and diseasePoly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expressionProcessing and transcriptome expansion at the mRNA 3' end in health and disease: finding the right endA Tale of Two RNAs during Viral Infection: How Viruses Antagonize mRNAs and Small Non-Coding RNAs in The Host CellShutoff of Host Gene Expression in Influenza A Virus and Herpesviruses: Similar Mechanisms and Common ThemesInduction of innate immunity and its perturbation by influenza virusesControl of poly(A) tail lengthNegative regulation of cytoplasmic RNA-mediated antiviral signalingConserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B virusesThe 3'-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo.Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.The Saccharomyces cerevisiae RNA-binding protein Rbp29 functions in cytoplasmic mRNA metabolism.The Influenza NS1 Protein: What Do We Know in Equine Influenza Virus Pathogenesis?The interactomes of influenza virus NS1 and NS2 proteins identify new host factors and provide insights for ADAR1 playing a supportive role in virus replicationStructural biology of poly(A) site definitionTristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that contains AU-rich elements by interacting with poly(A)-binding protein nuclear 1Alteration of protein levels during influenza virus H1N1 infection in host cells: a proteomic survey of host and virus reveals differential dynamicsA recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in miceFormation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesisInfluenza virus non-structural protein 1 (NS1) disrupts interferon signalingAntiviral therapy of influenza.The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target.Specific residues of PB2 and PA influenza virus polymerase subunits confer the ability for RNA polymerase II degradation and virus pathogenicity in miceConserved features of the PB2 627 domain impact influenza virus polymerase function and replicationMultiple anti-interferon actions of the influenza A virus NS1 proteinPathogenic influenza viruses and coronaviruses utilize similar and contrasting approaches to control interferon-stimulated gene responses.Persistent host markers in pandemic and H5N1 influenza virusesInfluenza A virus acquires enhanced pathogenicity and transmissibility after serial passages in swineProgress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses.Interspecies transmission and host restriction of avian H5N1 influenza virus.The NS1 protein of the 1918 pandemic influenza virus blocks host interferon and lipid metabolism pathwaysComplete-proteome mapping of human influenza A adaptive mutations: implications for human transmissibility of zoonotic strains.Differential effects of NS1 proteins of human pandemic H1N1/2009, avian highly pathogenic H5N1, and low pathogenic H5N2 influenza A viruses on cellular pre-mRNA polyadenylation and mRNA translation.The influenza virus NS1 protein as a therapeutic target.
P2860
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P2860
Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Influenza A virus NS1 protein ...... ar 3'-end processing machinery
@nl
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@ast
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en-gb
type
label
Influenza A virus NS1 protein ...... ar 3'-end processing machinery
@nl
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@ast
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en-gb
prefLabel
Influenza A virus NS1 protein ...... ar 3'-end processing machinery
@nl
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@ast
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en-gb
P2093
P2860
P3181
P356
P1433
P1476
Influenza A virus NS1 protein ...... r 3'-end processing machinery.
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/18.8.2273
P407
P577
1999-04-01T00:00:00Z