Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.

@article{Comellas2011StructuredRO,
  title={Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.},
  author={Gemma Comellas and Luisel R. Lemkau and Andrew J Nieuwkoop and Kathryn D. Kloepper and Daniel T. Ladror and Reika Ebisu and W. S. Woods and Andrew S Lipton and Julia M. George and Chad M Rienstra},
  journal={Journal of molecular biology},
  year={2011},
  volume={411 4},
  pages={881-95}
}
α-Synuclein (AS) fibrils are the major component of Lewy bodies, the pathological hallmark of Parkinson's disease (PD). Here, we use results from an extensive investigation employing solid-state NMR to present a detailed structural characterization and conformational dynamics quantification of full-length AS fibrils. Our results show that the core extends with a repeated structural motif. This result disagrees with the previously proposed fold of AS fibrils obtained with limited solid-state NMR… CONTINUE READING
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