Membrane-anchored Aβ accelerates amyloid formation and exacerbates amyloid-associated toxicity in mice.

@article{Nagarathinam2013MembraneanchoredAA,
  title={Membrane-anchored Aβ accelerates amyloid formation and exacerbates amyloid-associated toxicity in mice.},
  author={Amudha Nagarathinam and Philip Hoeflinger and Anika Buehler and Claudia Schaefer and Gillian McGovern and M Haddad Jeffrey and Matthias Staufenbiel and Mathias Jucker and Frank Baumann},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2013},
  volume={33 49},
  pages={19284-94}
}
Pathological, genetic, and biochemical hallmarks of Alzheimer's disease (AD) are linked to amyloid-β (Aβ) peptide aggregation. Especially misfolded Aβ42 peptide is sufficient to promote amyloid plaque formation. However, the cellular compartment facilitating the conversion of monomeric Aβ to aggregated toxic Aβ species remains unknown. In vitro models… CONTINUE READING