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Size and morphology of toxic oligomers of amyloidogenic proteins: a case study of human stefin B
Amyloid The Journal of Protein Folding Disorders, 10/29/08
Ceru S et al. - Critical pressure measurements showed that the toxic higher-order oligomers inserted more effectively into model lipid monolayers than dimers and tetramers. They also bound, similarly to prefibrillar aggregates, to the plasma membrane and became internalized. Taken together, results confirm the importance of membrane interaction and perforation in the phenomenon of cytotoxicity.
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