Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).
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Broad-spectrum antiviral therapeuticsInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRPACT, a protein activator of the interferon-induced protein kinase, PKR.The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKRAssociation of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activationTwo dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expressionThe 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 formationTranslation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationTwo heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertionDouble-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasisEncephalomyocarditis virus induces PKR-independent mitogen-activated protein kinase activation in macrophages.Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeastInhibition 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.A PKR-like eukaryotic initiation factor 2alpha kinase from zebrafish contains Z-DNA binding domains instead of dsRNA binding domainsCo-expression of miRNA targeting the expression of PERK, but not PKR, enhances cellular immunity from an HIV-1 Env DNA vaccine.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response.Analysis of PKR activation using analytical ultracentrifugationHeterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis.Localization and function of a eukaryotic-initiation-factor-2-associated 67-kDa glycoprotein.Potential role of PKR in double-stranded RNA-induced macrophage activation.Oncolytic vesicular stomatitis virus induces apoptosis via signaling through PKR, Fas, and Daxx.Duplex RNA-binding enzymes: headliners from neurobiology, virology, and development.Amyloid precursor protein and alpha synuclein translation, implications for iron and inflammation in neurodegenerative diseases.Identification of the heparin-binding domains of the interferon-induced protein kinase, PKRSpecific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties.Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.Double-stranded-RNA-activated protein kinase (PKR) regulates Ca2+ stores in Xenopus oocytesDominant negative function by an alternatively spliced form of the interferon-inducible protein kinase PKR.Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha).Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA.TOUSLED is a nuclear serine/threonine protein kinase that requires a coiled-coil region for oligomerization and catalytic activity.Mutations in the Double-stranded RNA-activated Protein Kinase Insert Region That Uncouple Catalysis from eIF2α Binding
P2860
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P2860
Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Double-stranded (ds) RNA bindi ...... ependent protein kinase (PKR).
@en
type
label
Double-stranded (ds) RNA bindi ...... ependent protein kinase (PKR).
@en
prefLabel
Double-stranded (ds) RNA bindi ...... ependent protein kinase (PKR).
@en
P2860
P356
P1476
Double-stranded (ds) RNA bindi ...... ependent protein kinase (PKR).
@en
P2860
P304
P356
10.1074/JBC.271.3.1756
P407
P577
1996-01-01T00:00:00Z