Ontology highlight
ABSTRACT:
SUBMITTER: Ahmed M
PROVIDER: S-EPMC2922021 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Ahmed Mahiuddin M Davis Judianne J Aucoin Darryl D Sato Takeshi T Ahuja Shivani S Aimoto Saburo S Elliott James I JI Van Nostrand William E WE Smith Steven O SO
Nature structural & molecular biology 20100411 5
The amyloid-beta(1-42) (Abeta42) peptide rapidly aggregates to form oligomers, protofibils and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's disease. We show that low-temperature and low-salt conditions can stabilize disc-shaped oligomers (pentamers) that are substantially more toxic to mouse cortical neurons than protofibrils and fibrils. We find that these neurotoxic oligomers do not have the beta-sheet structure characteristic of fibrils. Rather, the oligom ...[more]