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| 100 | 1 | _ | |a Röder, Christine |0 P:(DE-Juel1)174309 |b 0 |
| 245 | _ | _ | |a Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils |
| 260 | _ | _ | |a London [u.a.] |c 2020 |b Nature Publishing Group |
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| 520 | _ | _ | |a Amyloid deposits consisting of fibrillar islet amyloid polypeptide (IAPP) in pancreatic islets are associated with beta-cell loss and have been implicated in type 2 diabetes (T2D). Here, we applied cryo-EM to reconstruct densities of three dominant IAPP fibril polymorphs, formed in vitro from synthetic human IAPP. An atomic model of the main polymorph, built from a density map of 4.2-Å resolution, reveals two S-shaped, intertwined protofilaments. The segment 21-NNFGAIL-27, essential for IAPP amyloidogenicity, forms the protofilament interface together with Tyr37 and the amidated C terminus. The S-fold resembles polymorphs of Alzheimer's disease (AD)-associated amyloid-β (Aβ) fibrils, which might account for the epidemiological link between T2D and AD and reports on IAPP-Aβ cross-seeding in vivo. The results structurally link the early-onset T2D IAPP genetic polymorphism (encoding Ser20Gly) with the AD Arctic mutation (Glu22Gly) of Aβ and support the design of inhibitors and imaging probes for IAPP fibrils. |
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| 700 | 1 | _ | |a Schäfer, Luisa U. |0 P:(DE-Juel1)178773 |b 3 |
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| 700 | 1 | _ | |a Schröder, Gunnar F. |0 P:(DE-Juel1)132018 |b 8 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s41594-020-0442-4 |g Vol. 27, no. 7, p. 660 - 667 |0 PERI:(DE-600)2131437-8 |n 7 |p 660 - 667 |t Nature structural & molecular biology |v 27 |y 2020 |x 1545-9985 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/878602/files/s41594-020-0442-4-1.pdf |y Restricted |
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