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Published online before print December 16, 2005, doi:10.1212/01.wnl.0000192103.24796.42)
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Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis

Charles G. Glabe PhD* and Rakez Kayed PhD

From the Department of Molecular Biology and Biochemistry, University of California, Irvine, CA.


* To whom correspondence should be addressed. E-mail: cglabe{at}uci.edu.

Abstract--Recent findings indicate that soluble amyloid oligomers may represent the primary pathologic species in degenerative diseases. These amyloid oligomers share common structural features and the ability to permeabilize membranes, suggesting that they also share a common primary mechanism of pathogenesis. Membrane permeabilization by amyloid oligomers may initiate a common group of downstream pathologic processes, including intracellular calcium dyshomeostasis, production of reactive oxygen species, altered signaling pathways, and mitochondrial dysfunction that represent key effectors of cellular dysfunction and cell death in amyloid-associated degenerative disease, such as sporadic inclusion-body myositis.




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