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• W2104849621 abstract "It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease." @default.
• W2104849621 created "2016-06-24" @default.
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• W2104849621 date "2004-07-01" @default.
• W2104849621 modified "2023-10-16" @default.
• W2104849621 title "Observation of sequence specificity in the seeding of protein amyloid fibrils" @default.
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• W2104849621 doi "https://doi.org/10.1110/ps.04707004" @default.
• W2104849621 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2279934" @default.
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