Turn plasticity distinguishes different modes of amyloid-β aggregation.

@article{RezaeiGhaleh2014TurnPD,
  title={Turn plasticity distinguishes different modes of amyloid-β aggregation.},
  author={Nasrollah Rezaei-Ghaleh and Mehriar Amininasab and Karin Giller and Sathish Kumar and Anne Stuendl and Anja Schneider and Stefan Becker and Jochen Walter and Markus Zweckstetter},
  journal={Journal of the American Chemical Society},
  year={2014},
  volume={136 13},
  pages={4913-9}
}
Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-β (Aβ) peptide into oligomeric and fibrillar assemblies; however, little is known about the molecular basis of aggregation of Aβ into distinct assembly states. Here we demonstrate that phosphorylation at serine 26 (S26) impairs Aβ fibrillization while stabilizing its monomers and nontoxic soluble assemblies of nonfibrillar morphology. NMR spectroscopy and replica-exchange molecular dynamics indicate that… CONTINUE READING
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