Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.
about
The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRInositol hexakisphosphate kinase 2 mediates growth suppressive and apoptotic effects of interferon-beta in ovarian carcinoma cellsNucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKRHomologous 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 PKRPhysical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathwaysAntiviral actions of interferonsControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.Antiapoptotic and oncogenic potentials of hepatitis C virus are linked to interferon resistance by viral repression of the PKR protein kinaseHistidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitroThe 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 activityThe Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKRPKR regulates proliferation, differentiation, and survival of murine hematopoietic stem/progenitor cellsInhibition of eIF2alpha dephosphorylation inhibits ErbB2-induced deregulation of mammary acinar morphogenesisThioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid.Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.The non-structural 5A protein of hepatitis C virus.Deletion mapping of the encephalomyocarditis virus primary cleavage site.AlaArg motif in the carboxyl terminus of the gamma(1)34.5 protein of herpes simplex virus type 1 is required for the formation of a high-molecular-weight complex that dephosphorylates eIF-2alpha.Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.Translational control of viral gene expression in eukaryotesDouble-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53Inhibition of double-stranded RNA- and tumor necrosis factor alpha-mediated apoptosis by tetratricopeptide repeat protein and cochaperone P58(IPK)NF-kappaB activation by double-stranded-RNA-activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase.The protein kinase PKR: a molecular clock that sequentially activates survival and death programs.Activated MEK suppresses activation of PKR and enables efficient replication and in vivo oncolysis by Deltagamma(1)34.5 mutants of herpes simplex virus 1Characterization and mapping of the double-stranded regions involved in activation of PKR within a cellular RNA from 3T3-F442A cellsPotential role of PKR in double-stranded RNA-induced macrophage activation.Induction of CD4 expression and human immunodeficiency virus type 1 replication by mutants of the interferon-inducible protein kinase PKR.The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.Translational control in cancer etiology.Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulationTumor genotype determines susceptibility to oncolytic herpes simplex virus mutants: strategies for clinical application.Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells.Identification of the ATP binding domain of recombinant human 40-kDa 2',5'-oligoadenylate synthetase by photoaffinity labeling with 8-azido-[alpha-32P]ATP.Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).Tumor suppression by PTEN requires the activation of the PKR-eIF2alpha phosphorylation pathway
P2860
Q22254335-017859D4-658D-4468-81EB-D014F55B69EAQ24291206-5A74EA1E-AAC7-4B82-865F-BD074FA43706Q24311493-54DB3956-A505-4552-8995-D1BD8648FF75Q24321445-F29ADE35-7861-4287-8D07-9BEFAC19A131Q24324377-37742968-7938-4A1F-9560-2546D5BD040CQ24524116-673B844C-3E9F-486E-961E-35836EB04A9FQ24532129-1880A281-B1DD-40C5-BC83-410C21424C09Q24550676-DA9E47DE-85FF-4BC5-98DF-F970ECC028DBQ27469500-EAD66375-8EA1-41D4-9724-BEDD685996D0Q27469720-476C21E4-C29C-43A0-A693-FE5EB1CB32C0Q27935862-CE5C0673-E797-4962-A35B-CB428B6BC7C6Q28144828-C5681C4A-B3F1-4537-853D-72F179E5E078Q28215791-BCFA0905-AB70-472A-A63B-CA8F16ABF058Q28295453-D588D7BD-1856-449A-A4B8-201D93EB2BDDQ28306498-60967C1B-FEC0-41F3-826C-B6DED625FB92Q28595095-1A86CE75-F1DF-4162-8CE4-2AEBA2868566Q33503420-15B74B11-61AA-4920-8A2A-3ED699490A1BQ33781496-0A464929-2799-47AB-BCDC-21ECDF035C9EQ33786424-A6F3B709-E08A-4DBA-BB61-0EE01002804FQ33801346-5FB2BBB4-B7F2-4E4D-910C-212BD76A8A6EQ33844859-69F9BB0C-BF95-422E-B96C-59B69F063610Q33851189-2B5ED804-D7CC-466C-BF40-559B9B1B451FQ33886085-72719EE7-DD64-4D23-93EB-E2E0D11D3D5FQ33935121-C70DC395-C17E-4D82-8E45-97BB881D03BDQ33957610-0CEBD928-E3DB-4BC1-81CD-4FA921005D2CQ33958542-03D2190F-906F-420D-A7E3-D6706B002D44Q33961928-1872A683-E2B7-4B92-9463-27B228263ADBQ34107642-B7E0C924-8063-4600-994D-952434C77612Q34302130-CAD9CA9F-9921-432B-A88C-8D71A641D533Q34630940-DB7FD232-CBA7-4979-9993-DD66F82410FEQ35115764-A4DCA5DE-F0B2-4F2F-AADA-2DB79086E676Q35877650-7EC9EE63-B190-4908-8522-2AE546624D56Q35900773-EC5FC4E5-CCD7-4030-A635-32D2B4A979A5Q36555212-95754B9C-A30E-4C88-8B2C-5D22A9354315Q36561302-4328AAF5-BA7E-4825-8AC6-31EDBECD4109Q36967306-1AE442BD-C87E-4A3D-B8F7-8389183A12E1Q37621199-706647BE-3BD1-4D94-8C58-292131B43B58Q38353994-26807404-F449-4734-BD95-5D55C8C1EDDEQ38362637-77EB31D3-1D63-4B35-8952-E6E47F733706Q39759975-F2D90B97-7321-4839-B367-8E5D2B73DB7C
P2860
Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Mutants of the RNA-dependent p ...... duce malignant transformation.
@ast
Mutants of the RNA-dependent p ...... duce malignant transformation.
@en
type
label
Mutants of the RNA-dependent p ...... duce malignant transformation.
@ast
Mutants of the RNA-dependent p ...... duce malignant transformation.
@en
prefLabel
Mutants of the RNA-dependent p ...... duce malignant transformation.
@ast
Mutants of the RNA-dependent p ...... duce malignant transformation.
@en
P2093
P2860
P356
P1476
Mutants of the RNA-dependent p ...... duce malignant transformation.
@en
P2093
P2860
P304
P356
10.1128/MCB.15.6.3138
P407
P577
1995-06-01T00:00:00Z