Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

Cited 58 time in webofscience Cited 0 time in scopus
  • Hit : 220
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorKorshavn, Kyle J.ko
dc.contributor.authorBhunia, Anirbanko
dc.contributor.authorLim, Mi Heeko
dc.contributor.authorRamamoorthy, Ayyalusamyko
dc.date.accessioned2018-02-21T06:06:14Z-
dc.date.available2018-02-21T06:06:14Z-
dc.date.created2018-02-08-
dc.date.created2018-02-08-
dc.date.created2018-02-08-
dc.date.issued2016-01-
dc.identifier.citationCHEMICAL COMMUNICATIONS, v.52, no.5, pp.882 - 885-
dc.identifier.issn1359-7345-
dc.identifier.urihttp://hdl.handle.net/10203/240275-
dc.description.abstractAggregation 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.languageEnglish-
dc.publisherROYAL SOC CHEMISTRY-
dc.titleAmyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation-
dc.typeArticle-
dc.identifier.wosid000367614000003-
dc.identifier.scopusid2-s2.0-84954048415-
dc.type.rimsART-
dc.citation.volume52-
dc.citation.issue5-
dc.citation.beginningpage882-
dc.citation.endingpage885-
dc.citation.publicationnameCHEMICAL COMMUNICATIONS-
dc.identifier.doi10.1039/c5cc08634e-
dc.contributor.localauthorLim, Mi Hee-
dc.contributor.nonIdAuthorKorshavn, Kyle J.-
dc.contributor.nonIdAuthorBhunia, Anirban-
dc.contributor.nonIdAuthorRamamoorthy, Ayyalusamy-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordPlusALZHEIMERS-DISEASE-
dc.subject.keywordPlusNMR-SPECTROSCOPY-
dc.subject.keywordPlusA-BETA-
dc.subject.keywordPlusPEPTIDE-
dc.subject.keywordPlusAGGREGATION-
dc.subject.keywordPlusRESOLUTION-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusFIBRILS-
dc.subject.keywordPlusSTATES-
Appears in Collection
CH-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 58 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0