Decrease of Protease-Resistant PrPSc Level in ScN2a Cells by Polyornithine and Polyhistidine
DC Field | Value | Language |
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dc.contributor.author | Waqas, Muhammad | - |
dc.contributor.author | Huyen Trang Trinh | - |
dc.contributor.author | Lee, Sungeun | - |
dc.contributor.author | Kim, Dae-Hwan | - |
dc.contributor.author | Lee, Sang Yeol | - |
dc.contributor.author | Choe, Kevin K. | - |
dc.contributor.author | Ryou, Chongsuk | - |
dc.date.accessioned | 2021-06-22T11:21:15Z | - |
dc.date.available | 2021-06-22T11:21:15Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2018-12 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/5080 | - |
dc.description.abstract | Based on previous studies reporting the anti-prion activity of poly-L-lysine and poly-L-arginine, we investigated cationic poly-L-ornithine (PLO), poly-L-histidine (PLH), anionic poly-L-glutamic acid (PLE) and uncharged poly-L-threonine (PLT) in cultured cells chronically infected by prions to determine their anti-prion efficacy. While PLE and PLT did not alter the level of PrPSc, PLO and PLH exhibited potent PrP Sc inhibition in ScN2a cells. These results suggest that the anti-prion activity of poly-basic amino acids is correlated with the cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that the anti-prion activity of poly-basic amino acids is associated with their acidic cellular compartments. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | 한국미생물·생명공학회 | - |
dc.title | Decrease of Protease-Resistant PrPSc Level in ScN2a Cells by Polyornithine and Polyhistidine | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Ryou, Chongsuk | - |
dc.identifier.doi | 10.4014/jmb.1807.07045 | - |
dc.identifier.scopusid | 2-s2.0-85059304127 | - |
dc.identifier.wosid | 000454507700020 | - |
dc.identifier.bibliographicCitation | Journal of Microbiology and Biotechnology, v.28, no.12, pp.2141 - 2144 | - |
dc.relation.isPartOf | Journal of Microbiology and Biotechnology | - |
dc.citation.title | Journal of Microbiology and Biotechnology | - |
dc.citation.volume | 28 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 2141 | - |
dc.citation.endPage | 2144 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART002424558 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.subject.keywordPlus | SCRAPIE PRION PROTEIN | - |
dc.subject.keywordPlus | BRANCHED POLYAMINES | - |
dc.subject.keywordPlus | POLYLYSINE | - |
dc.subject.keywordPlus | DENDRIMERS | - |
dc.subject.keywordAuthor | Prion | - |
dc.subject.keywordAuthor | polyornithine | - |
dc.subject.keywordAuthor | polyhistidine | - |
dc.subject.keywordAuthor | cationic amino acid polymer | - |
dc.identifier.url | https://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.1807.07045 | - |
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