Lashuel, Hilal A.Hartley, DeanPetre, Benjamin M.Walz, ThomasLansbury, Peter T.2009-10-282009-10-282009-10-28200210.1038/418291ahttps://infoscience.epfl.ch/handle/20.500.14299/4398512124613Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from beta-amyloid and alpha-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.text::journal::journal article::research article