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Mycosporine-like amino acids (MAAs) 처리에 따른 배양세포 내 스크래피 프리온 단백질의 형성증가

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dc.contributor.authorLee, J.-
dc.contributor.authorMoh, S.-H.-
dc.contributor.authorRyou, C.-
dc.contributor.authorKim, D.-H.-
dc.date.accessioned2021-06-22T21:42:38Z-
dc.date.available2021-06-22T21:42:38Z-
dc.date.issued2015-06-
dc.identifier.issn1598-642X-
dc.identifier.urihttps://scholarworks.bwise.kr/erica/handle/2021.sw.erica/20585-
dc.description.abstractPrions are proteinaceous infectious particles that cause neurodegenerative diseases, such as scrapie in sheep, bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease (CJD) in humans. Although the detailed process, regarding the abnormal conversion of prion proteins (PrP), remains to be fully elucidated, a number of environmental factors appear to affect the formation of misfolded PrP, termed PrPSc. Because oceanic algae contain mycosporine-like amino acids (MAAs), which exhibit cellular defensive activities under a variety of stress conditions, we investigated the level of PrPSc in prion-infected neuroblastoma cells using mycosporine-glycine, porphyra-334 and shinorine. When judged by the level of protease-resistant PrPSc in western blots, porphyra-334 and shinorine increased the level of PrPSc in cells, but mycosporine-glycine did not. The current results indicate that the MAAs tested in this study enhance the formation of PrPSc. © 2015, The Korean Society for Microbiology and Biotechnology.-
dc.format.extent6-
dc.language한국어-
dc.language.isoKOR-
dc.publisherKorean Society for Microbiolog and Biotechnology-
dc.titleMycosporine-like amino acids (MAAs) 처리에 따른 배양세포 내 스크래피 프리온 단백질의 형성증가-
dc.title.alternativeEnhanced formation of scrapie prion protein in cultured ceils by treatment with mycosporine-like amino acids (MAAs)-
dc.typeArticle-
dc.publisher.location대한민국-
dc.identifier.doi10.4014/mbl.1503.03002-
dc.identifier.scopusid2-s2.0-84938352296-
dc.identifier.bibliographicCitationKorean Journal of Microbiology and Biotechnology, v.43, no.2, pp 91 - 96-
dc.citation.titleKorean Journal of Microbiology and Biotechnology-
dc.citation.volume43-
dc.citation.number2-
dc.citation.startPage91-
dc.citation.endPage96-
dc.type.docTypeArticle-
dc.identifier.kciidART002005744-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.subject.keywordPlusamino acid-
dc.subject.keywordPlusmycosporine like amino acid-
dc.subject.keywordPlusprion protein-
dc.subject.keywordPlusproteinase-
dc.subject.keywordPlusunclassified drug-
dc.subject.keywordPlusamino acid-
dc.subject.keywordPlusglycine-
dc.subject.keywordPlusmycosporine glycine-
dc.subject.keywordPlusmycosporine like amino acid-
dc.subject.keywordPlusporphyra 334-
dc.subject.keywordPlusprion protein-
dc.subject.keywordPlusshinorine-
dc.subject.keywordPlusArticle-
dc.subject.keywordPluscell culture-
dc.subject.keywordPlusCreutzfeldt Jakob disease-
dc.subject.keywordPlusenvironmental factor-
dc.subject.keywordPlusneuroblastoma cell-
dc.subject.keywordPlusnonhuman-
dc.subject.keywordPlusprion-
dc.subject.keywordPlusprotein aggregation-
dc.subject.keywordPlusscrapie-
dc.subject.keywordPlusWestern blotting-
dc.subject.keywordPlusPorphyra-
dc.subject.keywordPlusprotein folding-
dc.subject.keywordPlusprotein structure-
dc.subject.keywordPlusalgae-
dc.subject.keywordPlusBos-
dc.subject.keywordPlusBovinae-
dc.subject.keywordPlusOvis aries-
dc.subject.keywordPlusPorphyra-
dc.subject.keywordPlusPrions (infective agents)-
dc.subject.keywordPlusScrapie prion-
dc.subject.keywordAuthorMycosporine-like amino acids-
dc.subject.keywordAuthorPrion-
dc.subject.keywordAuthorProtein aggregation-
dc.subject.keywordAuthorPrP-
dc.identifier.urlhttps://www.mbl.or.kr/journal/view.html?doi=10.4014/mbl.1503.03002-
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