Next Article in Journal
Microbial β C-S Lyases: Enzymes with Multifaceted Roles in Flavor Generation
Previous Article in Journal
Cla4A, a Novel Regulator of Gene Expression Networks Required for Asexual and Insect-Pathogenic Lifecycles of Beauveria bassiana
Previous Article in Special Issue
Different Dynamics in 6aJL2 Proteins Associated with AL Amyloidosis, a Conformational Disease
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Correction

Correction: Sulatskaya et al. 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

by
Anna I. Sulatskaya
1,
Natalia P. Rodina
1,
Dmitry S. Polyakov
2,3,
Maksim I. Sulatsky
1,
Tatyana O. Artamonova
4,
Mikhail A. Khodorkovskii
4,
Mikhail M. Shavlovsky
2,3,
Irina M. Kuznetsova
1 and
Konstantin K. Turoverov
1,5,*
1
Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, St. Petersburg 194064, Russia
2
Department of Molecular Genetics, Institute of Experimental Medicine, Pavlov str. 12, St. Petersburg 197376, Russia
3
Chair of Medical Genetics, North-Western State Medical University named after I.I. Mechnikov, Piskarevskij prospect 47, St. Petersburg 195067, Russia
4
Research Center of Nanobiotechnologies, Peter the Great St. Petersburg Polytechnic University, Polytechnicheskaya 29, St. Petersburg 195251, Russia
5
Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, Polytechnicheskaya 29, St. Petersburg 195251, Russia
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2024, 25(12), 6411; https://doi.org/10.3390/ijms25126411
Submission received: 6 May 2024 / Accepted: 8 May 2024 / Published: 11 June 2024
(This article belongs to the Special Issue Amyloid Fibrils and Methods for Their Study)
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

  1. 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] [PubMed]
  2. 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] [PubMed]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content.

Share and Cite

MDPI and ACS Style

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. Correction: Sulatskaya et al. 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. Int. J. Mol. Sci. 2024, 25, 6411. https://doi.org/10.3390/ijms25126411

AMA Style

Sulatskaya AI, Rodina NP, Polyakov DS, Sulatsky MI, Artamonova TO, Khodorkovskii MA, Shavlovsky MM, Kuznetsova IM, Turoverov KK. Correction: Sulatskaya et al. 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. International Journal of Molecular Sciences. 2024; 25(12):6411. https://doi.org/10.3390/ijms25126411

Chicago/Turabian Style

Sulatskaya, Anna I., Natalia P. Rodina, Dmitry S. Polyakov, Maksim I. Sulatsky, Tatyana O. Artamonova, Mikhail A. Khodorkovskii, Mikhail M. Shavlovsky, Irina M. Kuznetsova, and Konstantin K. Turoverov. 2024. "Correction: Sulatskaya et al. 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" International Journal of Molecular Sciences 25, no. 12: 6411. https://doi.org/10.3390/ijms25126411

APA Style

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. (2024). Correction: Sulatskaya et al. 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. International Journal of Molecular Sciences, 25(12), 6411. https://doi.org/10.3390/ijms25126411

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop