The most infectious prion protein particles

By J. Silveira, G. J. Raymond, A. Hughson, R. Race, Valerie L. Sim, S. F. Hayes, B. Caughey. Nature, 2005

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Molecular chaperones and protein quality control. (2006, neutral): “Correspondingly, a recent comparison of size versus toxicity for aggregates of the prion protein PrP suggested that small aggregates containing one to two dozen molecules were the most toxic to cells (Silveira et al., 2005).”
The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, result): “These studies are in accordance with the observation that sonicated prion fibrils caused more potent seeding than unsonicated ones (Silveira et al., 2005).”
Eigenelements of a General Aggregation-Fragmentation Model (2009, background): “The aim of this article is to consider more general τ as [10, 37] suggest.”
Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders (2011, background): “Because the most potent A β seeds, like prions 97 , appear to be relatively small 54 , soluble A β seeds could serve as informative biomarkers in bodily fluids.”