title: Molecular mechanisms of amyloid oligomers toxicity.
abstract: Amyloid oligomers have emerged as the most toxic species of amyloid-β (Aβ). This hypothesis might explain the lack of correlation between amyloid plaques and memory impairment or cellular dysfunction. However, despite the numerous published research articles supporting the critical role Aβ oligomers in synaptic dysfunction and cell death, the exact definition and mechanism of amyloid oligomers formation and toxicity still elusive. Here we review the evidence supporting the many molecular mechanisms proposed for amyloid oligomers toxicity and suggest that the complexity and dynamic nature of amyloid oligomers may be responsible for the discrepancy among these mechanisms and the proposed cellular targets for amyloid oligomers.
authors.affiliation: The George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, Department of Neurology, University of Texas Medical Branch, Galveston, TX 77555, USA. rakayed@utmb.edu
authors.forename: Rakez
authors.initials: R
authors.lastname: Kayed
authors.forename: Cristian A
authors.initials: CA
authors.lastname: Lasagna-Reeves
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D000682:Amyloid / Q000378:metabolism* / Q000633:toxicity; D016229:Amyloid beta-Peptides / Q000378:metabolism* / Q000633:toxicity; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism* / Q000633:toxicity; D058225:Plaque, Amyloid / Q000378:metabolism
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments