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dc.citation.endPage 885 -
dc.citation.number 5 -
dc.citation.startPage 882 -
dc.citation.title CHEMICAL COMMUNICATIONS -
dc.citation.volume 52 -
dc.contributor.author Lim, Mi Hee -
dc.contributor.author Korshavn, Kyle J. -
dc.contributor.author Ramamoorthy, Ayyalusamy -
dc.contributor.author Bhunia, Anirban -
dc.date.accessioned 2023-12-22T00:14:53Z -
dc.date.available 2023-12-22T00:14:53Z -
dc.date.created 2016-01-05 -
dc.date.issued 2016-01 -
dc.description.abstract Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of Aβ40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22). -
dc.identifier.bibliographicCitation CHEMICAL COMMUNICATIONS, v.52, no.5, pp.882 - 885 -
dc.identifier.doi 10.1039/C5CC08634E -
dc.identifier.issn 1359-7345 -
dc.identifier.scopusid 2-s2.0-84954048415 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/18092 -
dc.identifier.url http://pubs.rsc.org/en/Content/ArticleLanding/2015/CC/C5CC08634E#!divAbstract -
dc.identifier.wosid 000367614000003 -
dc.language 영어 -
dc.publisher ROYAL SOC CHEMISTRY -
dc.title Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Chemistry, Multidisciplinary -
dc.relation.journalResearchArea Chemistry -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus ALZHEIMERS-DISEASE -
dc.subject.keywordPlus NMR-SPECTROSCOPY -
dc.subject.keywordPlus A-BETA -
dc.subject.keywordPlus PEPTIDE -
dc.subject.keywordPlus AGGREGATION -
dc.subject.keywordPlus RESOLUTION -
dc.subject.keywordPlus MECHANISM -
dc.subject.keywordPlus FIBRILS -
dc.subject.keywordPlus STATES -

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