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International Journal of Cell BiologyVolume 2013 2013, Article ID 950783, 6 pages

Review Article

Department of Neuroscience, University of Minnesota, Minneapolis, MN 55414, USA

N. Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis, MN 55414, USA

Institute for Translational Neuroscience Scholar, University of Minnesota, Minneapolis, MN 55414, USA

Received 17 May 2013; Accepted 1 August 2013

Academic Editor: Alessio Cardinale

Copyright © 2013 Sylvain E. Lesné. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Departing from the original postulates that defined various neurodegenerative disorders, accumulating evidence supports a major role for soluble forms of amyloid proteins as initiator toxins in Alzheimer’s disease, Parkinson’s disease, frontotemporal dementias, and prion diseases. Soluble multimeric assemblies of amyloid-β, tau, α-synuclein, and the prion protein are generally englobed under the term oligomers. Due to their biophysical properties, soluble amyloid oligomers can adopt multiple conformations and sizes that potentially confer differential biological activities. Therein lies the problem: with sporadic knowledge and limited tools to identify, characterize, and study amyloid oligomers, how can we solve the enigma of their respective roles in the pathogenesis of neurodegenerative disorders? To further our understanding of these devastating diseases, the code of the amyloid oligomers must be broken.

Author: Sylvain E. Lesné



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