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Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation

Chuanqi Sun, Kang Zhou, Peter DePaola IV, Woo Shik Shin, Trae Hillyer, Michael R. Sawaya, View ORCID ProfileZ. Hong Zhou, Lin Jiang
doi: https://doi.org/10.1101/2022.03.11.483992
Chuanqi Sun
1Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA
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Kang Zhou
2California Nano Systems Institute, UCLA, Los Angeles, CA 90095, USA
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Peter DePaola IV
1Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA
3Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA
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Woo Shik Shin
4Department of Pharmaceutical Sciences, College of Pharmacy, Northeast Ohio Medical University, Rootstown, OH 44272, USA
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Trae Hillyer
4Department of Pharmaceutical Sciences, College of Pharmacy, Northeast Ohio Medical University, Rootstown, OH 44272, USA
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Michael R. Sawaya
3Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA
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Z. Hong Zhou
2California Nano Systems Institute, UCLA, Los Angeles, CA 90095, USA
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  • ORCID record for Z. Hong Zhou
Lin Jiang
1Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA
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  • For correspondence: jianglin@ucla.edu
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Article Information

doi 
https://doi.org/10.1101/2022.03.11.483992
History 
  • March 30, 2022.

Article Versions

  • Version 1 (March 12, 2022 - 14:01).
  • You are viewing Version 2, the most recent version of this article.
Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.

Author Information

  1. Chuanqi Sun1,†,
  2. Kang Zhou2,†,
  3. Peter DePaola IV1,3,
  4. Woo Shik Shin4,
  5. Trae Hillyer4,
  6. Michael R. Sawaya3,
  7. Z. Hong Zhou2 and
  8. Lin Jiang1,*
  1. 1Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA
  2. 2California Nano Systems Institute, UCLA, Los Angeles, CA 90095, USA
  3. 3Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA
  4. 4Department of Pharmaceutical Sciences, College of Pharmacy, Northeast Ohio Medical University, Rootstown, OH 44272, USA
  1. ↵*For correspondence:
    Lin Jiang, email: jianglin{at}ucla.edu
  1. ↵† These authors contributed equally to this work.

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Posted March 30, 2022.
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Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation
Chuanqi Sun, Kang Zhou, Peter DePaola IV, Woo Shik Shin, Trae Hillyer, Michael R. Sawaya, Z. Hong Zhou, Lin Jiang
bioRxiv 2022.03.11.483992; doi: https://doi.org/10.1101/2022.03.11.483992
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Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation
Chuanqi Sun, Kang Zhou, Peter DePaola IV, Woo Shik Shin, Trae Hillyer, Michael R. Sawaya, Z. Hong Zhou, Lin Jiang
bioRxiv 2022.03.11.483992; doi: https://doi.org/10.1101/2022.03.11.483992

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