Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.

@article{Kotler2014DifferencesBA,
  title={Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.},
  author={Samuel A. Kotler and Patrick M. Walsh and Jeffrey R. Brender and Ayyalusamy Ramamoorthy},
  journal={Chemical Society reviews},
  year={2014},
  volume={43 19},
  pages={6692-700}
}
The association of the amyloid-β (Aβ) peptide with cellular membranes is hypothesized to be the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins and peptides, as is the case with Aβ, follows a progression from a monomeric state, through intermediates, ending at long, unbranched amyloid fibers. This tutorial review offers a perspective on the association of toxic Aβ structures with membranes as well as details of membrane-associated mechanisms of toxicity. 
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