Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.

@article{Colvin2016AtomicRS,
  title={Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.},
  author={Michael T. Colvin and Robert Silvers and Qing Zhe Ni and Thach V. Can and Ivan V. Sergeyev and M{\'e}lanie Rosay and Kevin J. Donovan and Brian Michael and Joseph S. Wall and Sara Linse and Robert G Griffin},
  journal={Journal of the American Chemical Society},
  year={2016},
  volume={138 30},
  pages={9663-74}
}
Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that are a hallmark of Alzheimer's disease (AD). The most prominent forms of Aβ are Aβ1-40 and Aβ1-42, which differ by two amino acids (I and A) at the C-terminus. However, Aβ42 is more neurotoxic and essential to the etiology of AD. Here, we present an atomic resolution structure of a monomorphic form of AβM01-42 amyloid… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 7 times over the past 90 days. VIEW TWEETS
56 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 56 extracted citations

References

Publications referenced by this paper.

Globins and Other Nitric Oxide-Reactive Proteins, Pt A

  • J. S. Wall, M. N. Simon, B. Y. Lin, S. N. Vinogradov
  • Elsevier Academic Press Inc: San Diego,
  • 2008

Similar Papers

Loading similar papers…