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Cited 118 time in webofscience Cited 115 time in scopus
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dc.contributor.authorLee, HH-
dc.contributor.authorChoi, TS-
dc.contributor.authorLee, SJC-
dc.contributor.authorLee, JW-
dc.contributor.authorPark, J-
dc.contributor.authorKo, YH-
dc.contributor.authorKim, WJ-
dc.contributor.authorKim, K-
dc.contributor.authorKim, HI-
dc.date.accessioned2016-03-31T07:33:52Z-
dc.date.available2016-03-31T07:33:52Z-
dc.date.created2015-02-04-
dc.date.issued2014-07-14-
dc.identifier.issn1433-7851-
dc.identifier.other2014-OAK-0000031884-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/13768-
dc.description.abstractAmyloid fibrils are insoluble protein aggregates comprised of highly ordered beta-sheet structures and they are involved in the pathology of amyloidoses, such as Alzheimer's disease. A supramolecular strategy is presented for inhibiting amyloid fibrillation by using cucurbit[7]uril (CB[7]). CB[7] prevents the fibrillation of insulin and beta-amyloid by capturing phenylalanine (Phe) residues, which are crucial to the hydrophobic interactions formed during amyloid fibrillation. These results suggest that the Phe-specific binding of CB[7] can modulate the intermolecular interaction of amyloid proteins and prevent the transition from monomeric to multimeric states. CB[7] thus has potential for the development of a therapeutic strategy for amyloidosis.-
dc.description.statementofresponsibilityX-
dc.languageEnglish-
dc.publisherWILEY-V C H VERLAG GMBH-
dc.relation.isPartOfANGEWANDTE CHEMIE-INTERNATIONAL EDITION-
dc.subjectaggregation-
dc.subjectbeta-amyloid-
dc.subjectcucurbit[7]uril-
dc.subjectinsulin-
dc.subjectsupramolecular chemistry-
dc.subjectINSULIN-
dc.subjectCOMPLEXES-
dc.subjectCHEMISTRY-
dc.subjectPROTEINS-
dc.titleSupramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril-
dc.typeArticle-
dc.contributor.college첨단재료과학부-
dc.identifier.doi10.1002/ANIE.201402496-
dc.author.googleLee, HH-
dc.author.googleChoi, TS-
dc.author.googleLee, SJC-
dc.author.googleLee, JW-
dc.author.googlePark, J-
dc.author.googleKo, YH-
dc.author.googleKim, WJ-
dc.author.googleKim, K-
dc.author.googleKim, HI-
dc.relation.volume53-
dc.relation.issue29-
dc.relation.startpage7461-
dc.relation.lastpage7465-
dc.contributor.id10652893-
dc.relation.journalANGEWANDTE CHEMIE-INTERNATIONAL EDITION-
dc.relation.indexSCI급, SCOPUS 등재논문-
dc.relation.sciSCI-
dc.collections.nameJournal Papers-
dc.type.rimsART-
dc.identifier.bibliographicCitationANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.53, no.29, pp.7461 - 7465-
dc.identifier.wosid000339564800006-
dc.date.tcdate2019-01-01-
dc.citation.endPage7465-
dc.citation.number29-
dc.citation.startPage7461-
dc.citation.titleANGEWANDTE CHEMIE-INTERNATIONAL EDITION-
dc.citation.volume53-
dc.contributor.affiliatedAuthorKim, WJ-
dc.contributor.affiliatedAuthorKim, K-
dc.contributor.affiliatedAuthorKim, HI-
dc.identifier.scopusid2-s2.0-84904467104-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.wostc62-
dc.description.scptc51*
dc.date.scptcdate2018-05-121*
dc.type.docTypeArticle-
dc.subject.keywordPlusINSULIN-
dc.subject.keywordPlusCOMPLEXES-
dc.subject.keywordPlusCHEMISTRY-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordAuthoraggregation-
dc.subject.keywordAuthorbeta-amyloid-
dc.subject.keywordAuthorcucurbit[7]uril-
dc.subject.keywordAuthorinsulin-
dc.subject.keywordAuthorsupramolecular chemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-

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김기문KIM, KIMOON
Dept of Chemistry
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