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. 2023 Nov 16;26(12):2073–2080. doi: 10.1038/s41593-023-01484-4

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a, Comparison of murine type III Aβ fibrils (blue, APP/PS1; lavender, ARTE10) with the cryo-EM structure of human brain-extracted Aß filaments with the E693G (E22G) mutation (gray; PDB 8BG0). b, Comparison of the DI1 Aβ fibril (light blue) with the cryo-EM structure of Aβ40 fibrils extracted from the meninges of human brain tissue from a patient with Alzheimer’s disease (gray; PDB 6SHS). c, Comparison of the APP23 (yellow), tg-APP_Swe (orange) and ARTE10 (burgundy) Aβ42 fibril fold with human type II Aβ42 filaments (gray; PDB 7Q4M). d, Comparison of the murine_Arc type I (green) Aβ40 fibril fold with human type I Aβ42 filament fold (gray; PDB 7Q4B).