Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
about
Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase.Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portionAntiviral actions of interferonsDouble-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivoAutophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKRThe structure of the PERK kinase domain suggests the mechanism for its activationHistidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinaseThe direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formationTwo phosphorylation sites on eIF-2 alphaThe Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKRFunctional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Characterization of the hemin-sensitive eukaryotic initiation factor 2alpha kinase from mouse nonerythroid cells.Double-stranded RNA-dependent protein kinase is involved in 2-methoxyestradiol-mediated cell death of osteosarcoma cells.The 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR.In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA from the 3' untranslated regions of human alpha-tropomyosin.Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain.Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.Adenovirus inhibition of cellular protein synthesis is prevented by the drug 2-aminopurine.Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded-RNA-activated protein kinase.Role of the apical stem in maintaining the structure and function of adenovirus virus-associated RNA.The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo.Regulation of PKR by HCV IRES RNA: importance of domain II and NS5AAutophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2Unactivated PKR exists in an open conformation capable of binding nucleotidesAnalysis of PKR activation using analytical ultracentrifugationHeterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Protection from interferon-induced apoptosis by Epstein-Barr virus small RNAs is not mediated by inhibition of PKR.Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor.Expanded CUG repeat RNAs form hairpins that activate the double-stranded RNA-dependent protein kinase PKRSynthesis and processing of small B2 transcripts in mouse embryonal carcinoma cells.Structural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI.Positional effect of phosphorylation sites 266 and 267 in the cytoplasmic domain of the E2 protein of hepatitis C virus 3a genotype: interferon resistance analysis via sequence alignment.Comparative analysis of the regulation of the interferon-inducible protein kinase PKR by Epstein-Barr virus RNAs EBER-1 and EBER-2 and adenovirus VAI RNATAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKRHeparin activates PKR by inducing dimerization.Mechanism of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase.Structure, function, and evolution of adenovirus-associated RNA: a phylogenetic approach.
P2860
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P2860
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@ast
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@en
type
label
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@ast
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@en
prefLabel
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@ast
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@en
P2860
P356
P1476
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
@en
P2093
M B Mathews
P2860
P304
P356
10.1128/MCB.9.4.1576
P407
P577
1989-04-01T00:00:00Z