Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase.
about
The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteinsTranslational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinaseMutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cellsInfluenza virus NS1 protein counteracts PKR-mediated inhibition of replication.Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinaseInfluenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activationMolecular signatures associated with Mx1-mediated resistance to highly pathogenic influenza virus infection: mechanisms of survivalInnate immune evasion strategies of influenza virusesPurification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells.Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/Caspase-8 death signaling pathwayProtein synthesis shut-off induced by influenza virus infection is independent of PKR activityTranslational control of viral gene expression in eukaryotesAntisense RNA: function and fate of duplex RNA in cells of higher eukaryotes.Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor.The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties.Intra-host versus inter-host selection: viral strategies of immune function impairmentAntiviral effects of geranylgeranylacetone: enhancement of MxA expression and phosphorylation of PKR during influenza virus infection.The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanismInfluenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs.The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.PKR Transduces MDA5-Dependent Signals for Type I IFN Induction.The NS1 protein of influenza A virus suppresses interferon-regulated activation of antigen-presentation and immune-proteasome pathways.Robust expression of vault RNAs induced by influenza A virus plays a critical role in suppression of PKR-mediated innate immunity.Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulationDegradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNAModification of eukaryotic initiation factor 4F during infection by influenza virus.The integrity of the stem structure of human immunodeficiency virus type 1 Tat-responsive sequence of RNA is required for interaction with the interferon-induced 68,000-Mr protein kinaseFunctional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free systemThe phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs.The alpha subunit of eucaryotic initiation factor 2 is phosphorylated in mengovirus-infected mouse L cells.The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation.Nucleic acid sensing and innate immunity: signaling pathways controlling viral pathogenesis and autoimmunity.The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation.Tyrosine phosphorylation of measles virus nucleocapsid protein in persistently infected neuroblastoma cells.Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway.Identification of proteins differentially expressed in human monocytes exposed to Porphyromonas gingivalis and its purified components by high-throughput immunoblotting.Influenza A Virus M2 Protein: Roles from Ingress to Egress.
P2860
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P2860
Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Influenza virus regulates prot ...... ular 68,000-Mr protein kinase.
@en
type
label
Influenza virus regulates prot ...... ular 68,000-Mr protein kinase.
@en
prefLabel
Influenza virus regulates prot ...... ular 68,000-Mr protein kinase.
@en
P2093
P2860
P1433
P1476
Influenza virus regulates prot ...... lular 68,000-Mr protein kinase
@en
P2093
P2860
P304
P407
P577
1988-10-01T00:00:00Z