DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, HH | - |
dc.contributor.author | Choi, TS | - |
dc.contributor.author | Lee, SJC | - |
dc.contributor.author | Lee, JW | - |
dc.contributor.author | Park, J | - |
dc.contributor.author | Ko, YH | - |
dc.contributor.author | Kim, WJ | - |
dc.contributor.author | Kim, K | - |
dc.contributor.author | Kim, HI | - |
dc.date.accessioned | 2016-03-31T07:33:52Z | - |
dc.date.available | 2016-03-31T07:33:52Z | - |
dc.date.created | 2015-02-04 | - |
dc.date.issued | 2014-07-14 | - |
dc.identifier.issn | 1433-7851 | - |
dc.identifier.other | 2014-OAK-0000031884 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/13768 | - |
dc.description.abstract | Amyloid 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.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.relation.isPartOf | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | - |
dc.subject | aggregation | - |
dc.subject | beta-amyloid | - |
dc.subject | cucurbit[7]uril | - |
dc.subject | insulin | - |
dc.subject | supramolecular chemistry | - |
dc.subject | INSULIN | - |
dc.subject | COMPLEXES | - |
dc.subject | CHEMISTRY | - |
dc.subject | PROTEINS | - |
dc.title | Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril | - |
dc.type | Article | - |
dc.contributor.college | 첨단재료과학부 | - |
dc.identifier.doi | 10.1002/ANIE.201402496 | - |
dc.author.google | Lee, HH | - |
dc.author.google | Choi, TS | - |
dc.author.google | Lee, SJC | - |
dc.author.google | Lee, JW | - |
dc.author.google | Park, J | - |
dc.author.google | Ko, YH | - |
dc.author.google | Kim, WJ | - |
dc.author.google | Kim, K | - |
dc.author.google | Kim, HI | - |
dc.relation.volume | 53 | - |
dc.relation.issue | 29 | - |
dc.relation.startpage | 7461 | - |
dc.relation.lastpage | 7465 | - |
dc.contributor.id | 10652893 | - |
dc.relation.journal | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.53, no.29, pp.7461 - 7465 | - |
dc.identifier.wosid | 000339564800006 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 7465 | - |
dc.citation.number | 29 | - |
dc.citation.startPage | 7461 | - |
dc.citation.title | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | - |
dc.citation.volume | 53 | - |
dc.contributor.affiliatedAuthor | Kim, WJ | - |
dc.contributor.affiliatedAuthor | Kim, K | - |
dc.contributor.affiliatedAuthor | Kim, HI | - |
dc.identifier.scopusid | 2-s2.0-84904467104 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 62 | - |
dc.description.scptc | 51 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | INSULIN | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | CHEMISTRY | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordAuthor | aggregation | - |
dc.subject.keywordAuthor | beta-amyloid | - |
dc.subject.keywordAuthor | cucurbit[7]uril | - |
dc.subject.keywordAuthor | insulin | - |
dc.subject.keywordAuthor | supramolecular chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
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