A technical feat achieved by two independent groups has enabled resolution of the molecular structure of a form of the amyloid-β protein that is thought to play a major part in Alzheimer's disease.
This is a preview of subscription content, log in via an institution to check access.
Notes
References
Colvin, M. T. et al. J. Am. Chem. Soc. 138, 9663–9674 (2016).
Wälti, M. A. et al. Proc. Natl Acad. Sci. USA 113, E4976–E4984 (2016).
Gravina, S. A. et al. J. Biol. Chem. 270, 7013–7016 (1995).
Paravastu, A. K., Leapman, R. D., Yau, W.-M. & Tycko, R. Proc. Natl Acad. Sci. USA 105, 18349–18354 (2008).
Tycko, R. Neuron 86, 632–645 (2015).
Colvin, M. T. et al. J. Am. Chem. Soc. 137, 7509–7518 (2015).
Eanes, E. D. & Glenner, G. G. J. Histochem. Cytochem. 16, 673–677 (1968).
Xiao, Y. et al. Nature Struct. Mol. Biol. 22, 499–505 (2015).
Bertini, I., Gonnelli, L., Luchinat, C., Mao, J. & Nesi, A. J. Am. Chem. Soc. 133, 16013–16022 (2011).
Lu, J.-X. et al. Cell 154, 1257–1268 (2013).
Author information
Authors and Affiliations
Corresponding author
Related links
Rights and permissions
About this article
Cite this article
Tycko, R. Structure of aggregates revealed. Nature 537, 492–493 (2016). https://doi.org/10.1038/nature19470
Published:
Issue Date:
DOI: https://doi.org/10.1038/nature19470
- Springer Nature Limited
This article is cited by
-
Structure of amyloid β25–35 in lipid environment and cholesterol-dependent membrane pore formation
Scientific Reports (2019)
-
Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin
Scientific Reports (2016)