Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies.

@article{OMalley2014ADD,
  title={Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies.},
  author={Tiernan T O'Malley and Nur Alia Oktaviani and Dainan Zhang and Aleksey Lomakin and Brian O'Nuallain and Sara Linse and George B. Benedek and Michael J. Rowan and Frans A. A. Mulder and Dominic M Walsh},
  journal={The Biochemical journal},
  year={2014},
  volume={461 3},
  pages={413-26}
}
Dimers of Aβ (amyloid β-protein) are believed to play an important role in Alzheimer's disease. In the absence of sufficient brain-derived dimers, we studied one of the only possible dimers that could be produced in vivo, [Aβ](DiY) (dityrosine cross-linked Aβ). For comparison, we used the Aβ monomer and a design dimer cross-linked by replacement of Ser²⁶ with cystine [AβS26C]₂. We showed that similar to monomers, unaggregated dimers lack appreciable structure and fail to alter long-term… CONTINUE READING
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