Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
about
Viral hepatitis and hepatocellular carcinomaDRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKRThe B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRLatently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase.Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRExpression cloning of an interferon-inducible 17-kDa membrane protein implicated in the control of cell growthNucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKRThe translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genomePACT, a protein activator of the interferon-induced protein kinase, PKR.Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPKInterferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNA-activated transcription factor DRAF1.Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational controlA new double-stranded RNA-binding protein that interacts with PKROncogenic role of Epstein-Barr virus-encoded RNAs in Burkitt's lymphoma cell line AkataPhysical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathwaysThe 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)Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3.The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRTyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alphaAntiviral actions of interferonsA herpesvirus genetic element which affects translation in the absence of the viral GADD34 functionMammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeastDouble-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivoThe Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBV-infected human B lymphocytesA dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferonRelatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufenConjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal patternPrecursor miR-886, a novel noncoding RNA repressed in cancer, associates with PKR and modulates its activity.Cytoplasmic p53 polypeptide is associated with ribosomesbic, a novel gene activated by proviral insertions in avian leukosis virus-induced lymphomas, is likely to function through its noncoding RNAAutophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKRRAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infectionImpact 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.Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesisAntiapoptotic and oncogenic potentials of hepatitis C virus are linked to interferon resistance by viral repression of the PKR protein kinasePKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2.
P2860
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P2860
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
@en
type
label
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
@en
prefLabel
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
@en
P2093
P356
P1433
P1476
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
@en
P2093
P304
P356
10.1126/SCIENCE.1382315
P407
P577
1992-09-01T00:00:00Z