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dc.contributor.authorHaque, Md. Mamunul-
dc.contributor.authorKim, Dohee-
dc.contributor.authorYu, Young Hyun-
dc.contributor.authorLim, Sungsu-
dc.contributor.authorKim, Dong Jin-
dc.contributor.authorChang, Young-Tae-
dc.contributor.authorHa, Hyung-Ho-
dc.contributor.authorKim, Yun Kyung-
dc.date.accessioned2024-01-20T09:01:52Z-
dc.date.available2024-01-20T09:01:52Z-
dc.date.created2022-01-10-
dc.date.issued2014-09-
dc.identifier.issn1350-6129-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/126381-
dc.description.abstractAbnormal tau aggregates are presumed to be neurotoxic and are an important therapeutic target for multiple neurodegenerative disorders including Alzheimer's disease. Growing evidence has shown that tau intermolecular disulfide cross-linking is critical in generating tau oligomers that serve as a building block for higher-order aggregates. Here we report that a small molecule inhibitor prevents tau aggregation by blocking the generation of disulfide cross-linked tau oligomers. Among the compounds tested, a rosamine derivative bearing mild thiol reactivity selectively labeled tau and effectively inhibited oligomerization and fibrillization processes in vitro. Our data suggest that controlling tau oxidation status could be a new therapeutic strategy for prevention of abnormal tau aggregation.-
dc.languageEnglish-
dc.publisherTAYLOR & FRANCIS LTD-
dc.titleInhibition of tau aggregation by a rosamine derivative that blocks tau intermolecular disulfide cross-linking-
dc.typeArticle-
dc.identifier.doi10.3109/13506129.2014.929103-
dc.description.journalClass1-
dc.identifier.bibliographicCitationAmyloid: The Journal of Protein Folding Disorders, v.21, no.3, pp.185 - 190-
dc.citation.titleAmyloid: The Journal of Protein Folding Disorders-
dc.citation.volume21-
dc.citation.number3-
dc.citation.startPage185-
dc.citation.endPage190-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000340428000006-
dc.identifier.scopusid2-s2.0-84906279142-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryMedicine, General & Internal-
dc.relation.journalWebOfScienceCategoryMedicine, Research & Experimental-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaGeneral & Internal Medicine-
dc.relation.journalResearchAreaResearch & Experimental Medicine-
dc.type.docTypeArticle-
dc.subject.keywordPlusPROTEIN-TAU-
dc.subject.keywordPlusIN-VITRO-
dc.subject.keywordPlusOLIGOMERS-
dc.subject.keywordPlusBETA(2)-MICROGLOBULIN-
dc.subject.keywordPlusNEURODEGENERATION-
dc.subject.keywordPlusPATHOLOGY-
dc.subject.keywordPlusTANGLES-
dc.subject.keywordPlusDOMAIN-
dc.subject.keywordAuthorIn-gel fluorescence-
dc.subject.keywordAuthorintermolecular disulfide bond-
dc.subject.keywordAuthorrosamine-
dc.subject.keywordAuthorsmall molecule inhibitor-
dc.subject.keywordAuthorTau oligomerization-
dc.subject.keywordAuthorthiol reactivity-
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