Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures
Author:
Funder
Det Frie Forskningsråd
Danmarks Grundforskningsfond
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-40483-z.pdf
Reference90 articles.
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2. Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24, 329–332 (1999).
3. Giehm, L. & Otzen, D. In Amyloid Fibrils and Prefibrillar Aggregates 295–320 (Wiley-VCH Verlag GmbH & Co. KGaA), https://doi.org/10.1002/9783527654185.ch14 (2013).
4. Sipe, J. D. et al. Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. Amyloid 23, 209–213 (2016).
5. Hardy, J. & Allsop, D. Amyloid deposition as the central event in the aetiology of Alzheimer’s disease. Trends Pharmacol. Sci. 12, 383–388 (1991).
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