breaking the code of amyloid-β oligomers

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ID: 236280
2013
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Ranked #51 of 61 articles by views in Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases

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Abstract
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 role(s) in the pathogenesis of neurodegenerative disorders? To further our understanding of these devastating diseases, the code of the amyloid oligomers must be broken.
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lesn2013internationalbreaking Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Sylvain E. Lesné
Journal Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases
Year 2013
DOI
10.1155/2013/950783
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