DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, D | - |
dc.contributor.author | Paik, SR | - |
dc.contributor.author | Choi, KY | - |
dc.date.accessioned | 2016-03-31T12:11:39Z | - |
dc.date.available | 2016-03-31T12:11:39Z | - |
dc.date.created | 2009-03-18 | - |
dc.date.issued | 2004-10-08 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.other | 2004-OAK-0000004625 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/17652 | - |
dc.description.abstract | beta-Synuclein exhibits high sequence homology and structural similarity with alpha-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of beta-synuclein and its anti-fibrillar activity in comparison with alpha-synuclein. beta-Synuclein suppressed the heat-induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of alpha-synuclein. Heat-induced inactivation of citrate synthase was significantly protected by beta-synuclein. Moreover, beta-synuclein inhibited the amyloid formation of both Abeta(1-40) and alpha-synuclein. It is, therefore, suggested that beta-synuclein can prevent abnormal protein aggregations more effectively than alpha-synuclein by acting as a molecular chaperone. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.subject | beta-synuclein | - |
dc.subject | chaperone activity | - |
dc.subject | protein aggregation | - |
dc.subject | fibril formation | - |
dc.subject | PARKINSONS-DISEASE | - |
dc.subject | NEURODEGENERATIVE DISORDERS | - |
dc.subject | SYNTHETIC MEMBRANES | - |
dc.subject | LEWY BODY | - |
dc.subject | MICE | - |
dc.subject | GENE | - |
dc.subject | IDENTIFICATION | - |
dc.subject | EXPRESSION | - |
dc.subject | MUTATION | - |
dc.subject | PROTEIN | - |
dc.title | beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1016/J.FEBSLET.2004.08.075 | - |
dc.author.google | Lee, D | - |
dc.author.google | Paik, SR | - |
dc.author.google | Choi, KY | - |
dc.relation.volume | 576 | - |
dc.relation.issue | 1-2 | - |
dc.relation.startpage | 256 | - |
dc.relation.lastpage | 260 | - |
dc.contributor.id | 10052985 | - |
dc.relation.journal | FEBS LETTERS | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.576, no.1-2, pp.256 - 260 | - |
dc.identifier.wosid | 000224607800049 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 260 | - |
dc.citation.number | 1-2 | - |
dc.citation.startPage | 256 | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 576 | - |
dc.contributor.affiliatedAuthor | Choi, KY | - |
dc.identifier.scopusid | 2-s2.0-4944251287 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 23 | - |
dc.description.scptc | 25 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | PARKINSONS-DISEASE | - |
dc.subject.keywordPlus | NEURODEGENERATIVE DISORDERS | - |
dc.subject.keywordPlus | SYNTHETIC MEMBRANES | - |
dc.subject.keywordPlus | LEWY BODY | - |
dc.subject.keywordPlus | MICE | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | MUTATION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordAuthor | beta-synuclein | - |
dc.subject.keywordAuthor | chaperone activity | - |
dc.subject.keywordAuthor | protein aggregation | - |
dc.subject.keywordAuthor | fibril formation | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
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