Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA.
about
The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRThe RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cellsInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRPACT, a protein activator of the interferon-induced protein kinase, PKR.Recognition of 5'-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2.The 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 PKRInhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.Molecular basis for PKR activation by PACT or dsRNAModular structure of PACT: distinct domains for binding and activating PKRPathogen recognition and inflammatory signaling in innate immune defensesImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionDoes protein kinase R mediate TNF-alpha- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism?Pro-Apoptotic Kinase Levels in Cerebrospinal Fluid as Potential Future Biomarkers in Alzheimer's DiseaseControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNAThe 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 formationPhosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosisRNA-binding proteins: modular design for efficient functionTranslational control by eIF2α kinases in long-lasting synaptic plasticity and long-term memory.Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.An antiviral response directed by PKR phosphorylation of the RNA helicase ARequirement 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.Mechanism of interferon action: identification of essential positions within the novel 15-base-pair KCS element required for transcriptional activation of the RNA-dependent protein kinase pkr geneDouble-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Translational control of viral gene expression in eukaryotesNF-kappaB activation by double-stranded-RNA-activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase.Unactivated PKR exists in an open conformation capable of binding nucleotidesLow 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.Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15.Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding.Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modificationDuplex RNA-binding enzymes: headliners from neurobiology, virology, and development.Exosomes from HIV-1-infected Cells Stimulate Production of Pro-inflammatory Cytokines through Trans-activating Response (TAR) RNAActivation of PKR: an open and shut case?Translational control of retroviruses.
P2860
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P2860
Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Characterization of the soluti ...... I trans-activating region RNA.
@en
Characterization of the soluti ...... I trans-activating region RNA.
@nl
type
label
Characterization of the soluti ...... I trans-activating region RNA.
@en
Characterization of the soluti ...... I trans-activating region RNA.
@nl
prefLabel
Characterization of the soluti ...... I trans-activating region RNA.
@en
Characterization of the soluti ...... I trans-activating region RNA.
@nl
P2093
P2860
P356
P1476
Characterization of the soluti ...... -I trans-activating region RNA
@en
P2093
P2860
P304
P356
10.1074/JBC.272.14.9510
P407
P577
1997-04-01T00:00:00Z