DC Field | Value | Language |
---|---|---|
dc.contributor.author | Korshavn, Kyle J. | ko |
dc.contributor.author | Bhunia, Anirban | ko |
dc.contributor.author | Lim, Mi Hee | ko |
dc.contributor.author | Ramamoorthy, Ayyalusamy | ko |
dc.date.accessioned | 2018-02-21T06:06:14Z | - |
dc.date.available | 2018-02-21T06:06:14Z | - |
dc.date.created | 2018-02-08 | - |
dc.date.created | 2018-02-08 | - |
dc.date.created | 2018-02-08 | - |
dc.date.issued | 2016-01 | - |
dc.identifier.citation | CHEMICAL COMMUNICATIONS, v.52, no.5, pp.882 - 885 | - |
dc.identifier.issn | 1359-7345 | - |
dc.identifier.uri | http://hdl.handle.net/10203/240275 | - |
dc.description.abstract | Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-beta (Ab) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of A beta(40) on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22). | - |
dc.language | English | - |
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.identifier.wosid | 000367614000003 | - |
dc.identifier.scopusid | 2-s2.0-84954048415 | - |
dc.type.rims | ART | - |
dc.citation.volume | 52 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | 882 | - |
dc.citation.endingpage | 885 | - |
dc.citation.publicationname | CHEMICAL COMMUNICATIONS | - |
dc.identifier.doi | 10.1039/c5cc08634e | - |
dc.contributor.localauthor | Lim, Mi Hee | - |
dc.contributor.nonIdAuthor | Korshavn, Kyle J. | - |
dc.contributor.nonIdAuthor | Bhunia, Anirban | - |
dc.contributor.nonIdAuthor | Ramamoorthy, Ayyalusamy | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
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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