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Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin

DC Field Value Language
dc.contributor.author김종선-
dc.date.accessioned2016-02-19T11:10:27Z-
dc.date.available2016-02-19T11:10:27Z-
dc.date.issued2001-
dc.identifier.issn0006-8993-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/142563-
dc.description.abstractVarious protein aggregates of α-synuclein developed by way of the common protein self-oligomerization in the presence of Aβ25-35, copper, and eosin were examined. All the aggregates exhibited congo red birefringence although the actual amounts of the aggregates were varied as determined by thioflavin T binding fluorescence. When their morphologies were analyzed in relation to in vitro cytotoxicity, the smallest granular aggregates obtained with copper exhibited the highest cytotoxicity, while the fibrous structures by eosin did not affect the cell.-
dc.description.statementOfResponsibilityopen-
dc.format.extent93~98-
dc.relation.isPartOfBRAIN RESEARCH-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAmyloid beta-Peptides/metabolism*-
dc.subject.MESHCells, Cultured/drug effects-
dc.subject.MESHCells, Cultured/metabolism-
dc.subject.MESHCopper/metabolism*-
dc.subject.MESHEosine Yellowish-(YS)/metabolism*-
dc.subject.MESHFluorescent Dyes/chemistry*-
dc.subject.MESHFluorescent Dyes/toxicity-
dc.subject.MESHLigands-
dc.subject.MESHMicroscopy, Electron-
dc.subject.MESHNerve Tissue Proteins/drug effects-
dc.subject.MESHNerve Tissue Proteins/metabolism*-
dc.subject.MESHNerve Tissue Proteins/ultrastructure-
dc.subject.MESHNeurodegenerative Diseases/metabolism*-
dc.subject.MESHNeurodegenerative Diseases/pathology-
dc.subject.MESHNeurodegenerative Diseases/physiopathology-
dc.subject.MESHPeptide Fragments/metabolism*-
dc.subject.MESHPolymers/chemical synthesis-
dc.subject.MESHProtein Structure, Tertiary/drug effects-
dc.subject.MESHProtein Structure, Tertiary/physiology-
dc.subject.MESHSynucleins-
dc.subject.MESHThiazoles/metabolism-
dc.subject.MESHalpha-Synuclein-
dc.titleMultiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Microbiology (미생물학)-
dc.contributor.googleauthorYoung-Sik Kim-
dc.contributor.googleauthorDaekyun Lee-
dc.contributor.googleauthorEun-Kyung Lee-
dc.contributor.googleauthorJee Young Sung-
dc.contributor.googleauthorKwang Chul Chung-
dc.contributor.googleauthorJongsun Kim-
dc.contributor.googleauthorSeung R Paik-
dc.identifier.doi10.1016/S0006-8993(01)02575-6-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA00921-
dc.relation.journalcodeJ00392-
dc.identifier.eissn1872-6240-
dc.identifier.pmid11457435-
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S0006899301025756-
dc.subject.keywordα-Synuclein-
dc.subject.keywordSelf-oligomerization-
dc.subject.keywordProtein aggregation-
dc.subject.keywordCytotoxicity-
dc.subject.keywordParkinson’s disease-
dc.contributor.alternativeNameKim, Jong Sun-
dc.contributor.affiliatedAuthorKim, Jong Sun-
dc.rights.accessRightsnot free-
dc.citation.volume908-
dc.citation.number1-
dc.citation.startPage93-
dc.citation.endPage98-
dc.identifier.bibliographicCitationBRAIN RESEARCH, Vol.908(1) : 93-98, 2001-
dc.identifier.rimsid31094-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers

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