Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones

dc.contributor.authorNarayan, Priyanka
dc.contributor.authorMeehan, Sarah
dc.contributor.authorCarver, John
dc.contributor.authorWilson, Mark
dc.contributor.authorDobson, Christopher M.
dc.contributor.authorKlenerman, David
dc.date.accessioned2015-12-13T22:41:05Z
dc.date.issued2012
dc.date.updated2016-02-24T09:32:31Z
dc.description.abstractThe aberrant aggregation of the amyloid-β peptide into β-sheet rich, fibrillar structures proceeds via a heterogeneous ensemble of oligomeric intermediates that have been associated with neurotoxicity in Alzheimers disease (AD). Of particular interest i
dc.identifier.issn0006-2960
dc.identifier.urihttp://hdl.handle.net/1885/78342
dc.publisherAmerican Chemical Society
dc.sourceBiochemistry
dc.subjectKeywords: Aggregation state; Alzheimers disease; Amyloid fibril; Biological defense; Clusterin; Extracellular; Extracellular environments; Fibrillar structures; Fluorescence technique; Mechanism of action; Molecular chaperones; Neurotoxicity; Protein misfolding; Se
dc.titleAmyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
dc.typeJournal article
local.bibliographicCitation.issue46
local.bibliographicCitation.lastpage9276
local.bibliographicCitation.startpage9270
local.contributor.affiliationNarayan, Priyanka, University of Cambridge
local.contributor.affiliationMeehan, Sarah, University of Cambridge
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationWilson, Mark, University of Wollongong
local.contributor.affiliationDobson, Christopher M., University of Cambridge
local.contributor.affiliationKlenerman, David, University of Cambridge
local.contributor.authoruidCarver, John, u1571001
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationf5625xPUB7002
local.identifier.citationvolume51
local.identifier.doi10.1021/bi301277k
local.identifier.scopusID2-s2.0-84869392249
local.identifier.thomsonID000311858400003
local.type.statusPublished Version

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