Regulation of the interferon-induced PKR: can viruses cope?
about
DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKRThe herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domainInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRRegulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPKInterferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNA-activated transcription factor DRAF1.Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathwaysThe molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirusThe C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRAntiviral actions of interferonsA herpesvirus genetic element which affects translation in the absence of the viral GADD34 functionImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionAntiapoptotic and oncogenic potentials of hepatitis C virus are linked to interferon resistance by viral repression of the PKR protein kinaseHepatitis C virus nonstructural 5A protein induces interleukin-8, leading to partial inhibition of the interferon-induced antiviral response.PKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.PKR and RNase L Contribute to Protection against Lethal West Nile Virus Infection by Controlling Early Viral Spread in the Periphery and Replication in NeuronsRNA-protein interactions in regulation of picornavirus RNA translationThe double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitroEnhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKRTranslation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationEvidence for a newly discovered cellular anti-HIV-1 phenotypeProapoptotic protein PACT is expressed at high levels in colonic epithelial cells in miceXBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein responseMacaque proteome response to highly pathogenic avian influenza and 1918 reassortant influenza virus infectionsVirology research and virulent human pandemics.Role of PKR and Type I IFNs in viral control during primary and secondary infection.B-myb promoter retargeting of herpes simplex virus gamma34.5 gene-mediated virulence toward tumor and cycling cellsRequirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeastEukaryotic elongation factor 1delta is hyperphosphorylated by the protein kinase encoded by the U(L)13 gene of herpes simplex virus 1The second-site mutation in the herpes simplex virus recombinants lacking the gamma134.5 genes precludes shutoff of protein synthesis by blocking the phosphorylation of eIF-2alphaThe herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2.Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.The non-structural 5A protein of hepatitis C virus.Hepatitis C virus NS5A physically associates with p53 and regulates p21/waf1 gene expression in a p53-dependent mannerDouble-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53NF-kappaB activation by double-stranded-RNA-activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase.Interferon regulatory factor-3 is an in vivo target of DNA-PK.The protein kinase PKR: a molecular clock that sequentially activates survival and death programs.Tissue selectivity of interferon-stimulated gene expression in mice infected with Dam(+) versus Dam(-) Salmonella enterica serovar Typhimurium strains
P2860
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P2860
Regulation of the interferon-induced PKR: can viruses cope?
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Regulation of the interferon-induced PKR: can viruses cope?
@en
type
label
Regulation of the interferon-induced PKR: can viruses cope?
@en
prefLabel
Regulation of the interferon-induced PKR: can viruses cope?
@en
P1476
Regulation of the interferon-induced PKR: can viruses cope?
@en
P2093
P356
10.1016/S0966-842X(00)88880-0
P577
1995-02-01T00:00:00Z