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Article type: Review Article
Authors: Moosavi, Behrooza | Mousavi, Bibimaryamb | Macreadie, Ian G.c; *
Affiliations: [a] Key Laboratory of Pesticide & Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, P.R. China | [b] Laboratory of Organometallics, Catalysis and Ordered Materials, State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, Wuhan, P.R. China | [c] School of Applied Sciences, RMIT University, Bundoora, VIC, Australia
Correspondence: [*] Correspondence to: Ian G. Macreadie, School of Applied Sciences, RMIT University, Bundoora, VIC, Australia. Tel.: +61 3 9925 6627; Fax: +61 3 9925 7100; ian.macreadie@rmit.edu.au
Abstract: The amyloid-β peptide (Aβ) and the phosphorylated protein tau have been widely implicated in Alzheimer’s disease and are the focus of most research. Both agents have been extensively studied in mammalian cell culture and in animal studies, but new research is focusing on yeast models. Yeast are eukaryotes, just like us, and are amenable to effects and expression of Aβ and tau and appear able to ‘report’ with considerable relevance on the effects of these biomolecules. The use of yeast enables powerful new approaches to understanding how to overcome the effects of Aβ and tau, and such advances could lead to new therapies to prevent the progression of Alzheimer’s disease.
Keywords: Alzheimer’s disease, amyloid, protein aggregation, tau protein, yeasts
DOI: 10.3233/JAD-150173
Journal: Journal of Alzheimer's Disease, vol. 47, no. 1, pp. 9-16, 2015
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