Nature Reviews Molecular Cell Biology 15, 384–396 (2014)
In the legend of figure 2 of the above article (page 388), the sentence “The spacing between polypeptide chains along the fibril axis is constant to a good approximation even for very different polypeptide sequences, a generic property arising from the common inter-side chain hydrogen bonding constraints (orange line in part b).” incorrectly referred to 'inter-side chain' hydrogen bonding constraints, whereas it should have referred to 'inter-main chain' hydrogen bonding constraints. This has been corrected online. The authors apologize for any confusion caused to readers.
Additional information
The online version of the original article can be found at 10.1038/nrm3810
Rights and permissions
About this article
Cite this article
Knowles, T., Vendruscolo, M. & Dobson, C. Erratum: The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol 15, 496 (2014). https://doi.org/10.1038/nrm3826
Published:
Issue Date:
DOI: https://doi.org/10.1038/nrm3826
This article is cited by
-
Diverse antithetical effects of the bio-compatible Ag-NPs on the hen egg lysozyme amyloid aggregation: from an efficient inhibitor to obscure inducer
Journal of the Iranian Chemical Society (2019)
-
Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation
Biophysical Reviews (2017)
-
Nanoscale studies link amyloid maturity with polyglutamine diseases onset
Scientific Reports (2016)
