In the original publication [1], some representative images of different amyloids published by us earlier [2] were used for a comparison with the main objects of study [1]. The citation to our previous publication has now been inserted into the caption of Figure 1 in [1] and should read: “Electron micrographs of the amyloid fibrils formed from (A) beta-2-microglobulin (β2m), (B) ΔN6β2m, (C) ΔN10β2m, (D) insulin, and (E) lysozyme. (A,D,E) are adapted from [40]. Scale bar is 1 μm.”. With this correction, the order of other references has been adjusted accordingly.
The authors state that the scientific conclusions are unaffected. This correction was approved by the Academic Editor. The original publication has also been updated.
References
- Sulatskaya, A.I.; Rodina, N.P.; Polyakov, D.S.; Sulatsky, M.I.; Artamonova, T.O.; Khodorkovskii, M.A.; Shavlovsky, M.M.; Kuznetsova, I.M.; Turoverov, K.K. Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T. Int. J. Mol. Sci. 2018, 19, 2762. [Google Scholar] [CrossRef] [Scilit] [PubMed]
- Sulatskaya, A.I.; Kuznetsova, I.M.; Belousov, M.V.; Bondarev, S.A.; Zhouravleva, G.A.; Turoverov, K.K. Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils. PLoS ONE 2016, 11, e0156314. [Google Scholar] [CrossRef] [Scilit] [PubMed]
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