Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation
about
Homologous regions of the alpha subunit of eukaryotic translational initiation factor 2 (eIF2alpha) and the vaccinia virus K3L gene product interact with the same domain within the dsRNA-activated protein kinase (PKR)Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPKA new double-stranded RNA-binding protein that interacts with PKRCharacterization of the interaction between the interferon-induced protein P56 and the Int6 protein encoded by a locus of insertion of the mouse mammary tumor virus.The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.Acute hepatitis C virus infection: A chronic problemThe Crystal Structure of the Human Co-Chaperone P58IPKNuclear 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 formationThe cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activityTetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidaseThe tetratricopeptide repeat: a structural motif mediating protein-protein interactionsP58(IPK): a novel "CIHD" member of the host innate defense response against pathogenic virus infection.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.Translational 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)Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Molecular chaperone Hsp90 is important for vaccinia virus growth in cellssmg-7 is required for mRNA surveillance in Caenorhabditis elegans.RNA interference: on the road to an alternate therapeutic strategy!The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR.The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanismThe molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alpha.Protein kinase PKR mutants resistant to the poxvirus pseudosubstrate K3L protein.Auto-phosphorylation Represses Protein Kinase R Activity.Recombinant human peroxisomal targeting signal receptor PEX5. Structural basis for interaction of PEX5 with PEX14.Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1.Cell-based models of sustained, interferon-sensitive hepatitis C virus genotype 1 replication.Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway.Protein kinase R is increased and is functional in hepatitis C virus-related hepatocellular carcinoma.Sequence and phylogenetic analysis of host-range (E3L, K3L, and C7L) and structural protein (B5R) genes of buffalopox virus isolates from buffalo, cattle, and human in India.
P2860
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P2860
Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Interaction of the interferon- ...... ications for kinase regulation
@ast
Interaction of the interferon- ...... ications for kinase regulation
@en
type
label
Interaction of the interferon- ...... ications for kinase regulation
@ast
Interaction of the interferon- ...... ications for kinase regulation
@en
prefLabel
Interaction of the interferon- ...... ications for kinase regulation
@ast
Interaction of the interferon- ...... ications for kinase regulation
@en
P2093
P2860
P356
P1476
Interaction of the interferon- ...... ications for kinase regulation
@en
P2093
P2860
P304
P356
10.1128/MCB.16.8.4172
P407
P577
1996-08-01T00:00:00Z