Corbett GT, Wang Z, Hong W, et al. - Study demonstrated that the soluble aggregates of α-synuclein and tau bind to plate-immobilized prion protein (PrP) in vitro and on mouse cortical neurons, and this binding needs at least one of the alike N-terminal sites at which soluble Aβ aggregates bind. Utilizing an all-human experimental paradigm comprising that isogenic induced pluripotent cells-derived neuron expressing or requiring PRNP, aqueous extracts from brains of people who died due to Alzheimer disease, dementia with Lewy bodies, and Pick’s disease, it was shown that Aβ, α-synuclein, and tau were toxic to neurons in a pattern that needs cellular PrP. Overall it was found that PrP is suitable to perform a significant role in a diversity of late-life neurodegenerative diseases and that therapeutic targeting of PrP, rather than people disease proteins, could have more advantages for circumstances which included the aggregation of more than one protein.