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Cited 4 time in webofscience Cited 5 time in scopus
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dc.contributor.authorHesung Now-
dc.contributor.authorYoo, JY-
dc.date.accessioned2016-03-31T09:13:41Z-
dc.date.available2016-03-31T09:13:41Z-
dc.date.created2012-02-13-
dc.date.issued2011-09-30-
dc.identifier.issn0006-291X-
dc.identifier.other2011-OAK-0000024741-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/16853-
dc.description.abstractThe cellular RIG-I-like receptor (RLR) senses pathogenic RNA molecular patterns and transmits signals for type I interferon (IFN) production. It acts as a center for antiviral responses, and large numbers of RIG-I (retinoic acid inducible gene-I) interacting proteins are identified as signaling regulators. In the present study, we report PRKRIR, a negative regulator of PKR inhibitor, as a novel RIG-I interacting protein. In HEK293FT cells, PRKRIR synergistically enhances type I IFN production mediated by a signal activated- or constitutively active form of RIG-I. The C-terminal domain of the PRKRIR was required for physical interaction and the signal augmentation. The PRKRIR blocks poly-ubiquitination and protein degradation of RIG-I, thereby increasing cellular levels of RIG-I proteins. Furthermore, overexpression of PRKRIR, along with a signal activated- or constitutively active form of RIG-I, efficiently inhibits virus replication in the infected host. In conclusion, PRKRIR provides a novel positive regulator controlling the RIG-I-IFN production system through protein stability control. (C) 2011 Elsevier Inc. All rights reserved.-
dc.description.statementofresponsibilityX-
dc.languageEnglish-
dc.publisherNew York, Academic Press.-
dc.relation.isPartOfBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.subjectRIG-I-
dc.subjectPRKRIR-
dc.subjectVirus-
dc.subjectAntiviral-
dc.subjectUbiquitination-
dc.subjectIFN-
dc.subjectAnti-viral signaling-
dc.subjectRNA virus-
dc.subjectNF-KAPPA-B-
dc.subjectIMMUNE-RESPONSES-
dc.subjectUBIQUITIN LIGASE-
dc.subjectADAPTER PROTEIN-
dc.subjectINNATE IMMUNITY-
dc.subjectGENE-I-
dc.subjectHELICASE-
dc.subjectACTIVATION-
dc.subjectISGYLATION-
dc.subjectP52(RIPK)-
dc.titleA protein-kinase, IFN-inducible double-stranded RNA dependent inhibitor and repressor of p58 (PRKRIR) enhances type I IFN-mediated antiviral response through the stability control of RIG-I protein-
dc.typeArticle-
dc.contributor.college생명과학과-
dc.identifier.doi10.1016/J.BBRC.2011.08.127-
dc.author.googleNow, H-
dc.author.googleYoo, JY-
dc.relation.volume413-
dc.relation.issue3-
dc.relation.startpage487-
dc.relation.lastpage493-
dc.contributor.id10114821-
dc.relation.journalBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.relation.indexSCI급, SCOPUS 등재논문-
dc.relation.sciSCI-
dc.collections.nameJournal Papers-
dc.type.rimsART-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.413, no.3, pp.487 - 493-
dc.identifier.wosid000295908500017-
dc.date.tcdate2019-01-01-
dc.citation.endPage493-
dc.citation.number3-
dc.citation.startPage487-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume413-
dc.contributor.affiliatedAuthorYoo, JY-
dc.identifier.scopusid2-s2.0-80053336032-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.wostc3-
dc.description.scptc3*
dc.date.scptcdate2018-05-121*
dc.type.docTypeArticle-
dc.subject.keywordPlusNF-KAPPA-B-
dc.subject.keywordPlusUBIQUITIN LIGASE-
dc.subject.keywordPlusADAPTER PROTEIN-
dc.subject.keywordPlusHELICASE-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusP58(IPK)-
dc.subject.keywordPlusLGP2-
dc.subject.keywordAuthorRIG-I-
dc.subject.keywordAuthorPRKRIR-
dc.subject.keywordAuthorVirus-
dc.subject.keywordAuthorAntiviral-
dc.subject.keywordAuthorUbiquitination-
dc.subject.keywordAuthorIFN-
dc.subject.keywordAuthorAnti-viral signaling-
dc.subject.keywordAuthorRNA virus-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-

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유주연YOO, JOO YEON
Dept of Life Sciences
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