Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.
about
Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRp58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacityThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRModular structure of PACT: distinct domains for binding and activating PKRControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.The Crystal Structure of the Human Co-Chaperone P58IPKDistinct Z-DNA binding mode of a PKR-like protein kinase containing a Z-DNA binding domain (PKZ)Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNATwo dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expressionDeath-associated protein 4 binds MST1 and augments MST1-induced apoptosisThe 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 phosphorylationThe cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activityER chaperones in mammalian development and human diseasesInduction of unfolded protein response during neuronal induction of rat bone marrow stromal cells and mouse embryonic stem cellsInfluenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activationFunctional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Andes virus nucleocapsid protein interrupts protein kinase R dimerization to counteract host interference in viral protein synthesis.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.DNA and RNA-based vaccines: principles, progress and prospects.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Translational control of viral gene expression in eukaryotesInhibition of double-stranded RNA- and tumor necrosis factor alpha-mediated apoptosis by tetratricopeptide repeat protein and cochaperone P58(IPK)Analysis of PKR activation using analytical ultracentrifugationHeterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Quasispecies evolution in NS5A region of hepatitis C virus genotype 1b during interferon or combined interferon-ribavirin therapy.Molecular chaperone Hsp90 is important for vaccinia virus growth in cellsReovirus induces and benefits from an integrated cellular stress response.Resistance of mRNA translation to acute endoplasmic reticulum stress-inducing agents in herpes simplex virus type 1-infected cells requires multiple virus-encoded functions.PKR activation in neurodegenerative disease.Expression of PACT is regulated by Sp1 transcription factor.The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanismRobust expression of vault RNAs induced by influenza A virus plays a critical role in suppression of PKR-mediated innate immunity.Identification of the heparin-binding domains of the interferon-induced protein kinase, PKRAuto-phosphorylation Represses Protein Kinase R Activity.Gene expression profiling identifies FKBP39 as an inhibitor of autophagy in larval Drosophila fat body.Long noncoding RNA EGOT negatively affects the antiviral response and favors HCV replication.Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1.Mechanism of activation of the double-stranded-RNA-dependent protein kinase, PKR: role of dimerization and cellular localization in the stimulation of PKR phosphorylation of eukaryotic initiation factor-2 (eIF2).
P2860
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P2860
Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@ast
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@en
type
label
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@ast
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@en
prefLabel
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@ast
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@en
P2093
P2860
P356
P1476
Double-stranded RNA-independen ...... the cellular P58IPK inhibitor.
@en
P2093
P2860
P304
P356
10.1128/MCB.18.5.2431
P407
P577
1998-05-01T00:00:00Z