Narayan, PriyankaMeehan, SarahCarver, JohnWilson, MarkDobson, Christopher M.Klenerman, David2015-12-130006-2960http://hdl.handle.net/1885/78342The 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 iKeywords: Aggregation state; Alzheimers disease; Amyloid fibril; Biological defense; Clusterin; Extracellular; Extracellular environments; Fibrillar structures; Fluorescence technique; Mechanism of action; Molecular chaperones; Neurotoxicity; Protein misfolding; Se201210.1021/bi301277k2016-02-24