Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.

  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},
  volume={138 30},
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
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