The fold of alpha-synuclein fibrils.

  title={The fold of alpha-synuclein fibrils.},
  author={Marçal Vilar and Hui-Ting Chou and Thorsten L{\"u}hrs and Samir K Maji and Dominique Riek-Loher and Ren{\'e} Verel and Gerard Manning and Henning Stahlberg and Roland Riek},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={105 25},
The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of alpha-synuclein (alpha-syn) from monomers by intermediates into amyloid fibrils is the toxic disease-causative mechanism. Here, we studied the structure of alpha-syn in its amyloid state by using various biophysical approaches. Quenched hydrogen/deuterium exchange NMR spectroscopy identified five beta-strands within the fibril core… CONTINUE READING
Highly Influential
This paper has highly influenced 10 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
133 Citations
53 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 133 extracted citations


Publications referenced by this paper.
Showing 1-10 of 53 references

Similar Papers

Loading similar papers…