The authors of the article listed below1 have determined that, although the data presented in the paper noted below are correct, the interpretation of the data is incorrect based on new experiments; thus they publish this corrigendum.
In a subsequent paper in Protein Science,2 the authors explain how the data in the previous “cellular disaggregase activity” paper were misinterpreted. Briefly, time-dependent amyloid fibril adsorption to the walls of multi-well plates or individual tubes was misinterpreted as fibril disaggregation. Methodology to quantitatively correct for this problem is presented in the subsequent paper.
The authors apologize to the scientific community for their serious mistake of misinterpreting a decrease in thioflavin T fluorescence in the presence of biological extracts as Aβ1-40 amyloid fibril disaggregation. It is important to stress that the results in the subsequent article do not call into question the existence of a disaggregase activity in multi-cellular organisms. However, the thioflavin T-based Aβ1-40 amyloid fibril kinetic disaggregation assay carried out in standard plates at 37°C is invalid when used as evidence for a disaggregation activity.
References
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- 2.Murray AN, Palhano FL, Bieschke J, Kelly JW. Surface adsorption considerations when working with amyloid fibrils in multi-well plates and Eppendorf tubes. Protein Sci. 2013;22:1531–1541. doi: 10.1002/pro.2339. [DOI] [PMC free article] [PubMed] [Google Scholar]