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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
Kang Zhou
2California Nano Systems Institute, UCLA, Los Angeles, CA 90095, USA
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
Woo Shik Shin
4Department of Pharmaceutical Sciences, College of Pharmacy, Northeast Ohio Medical University, Rootstown, OH 44272, USA
Trae Hillyer
4Department of Pharmaceutical Sciences, College of Pharmacy, Northeast Ohio Medical University, Rootstown, OH 44272, USA
Michael R. Sawaya
3Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA
Z. Hong Zhou
2California Nano Systems Institute, UCLA, Los Angeles, CA 90095, USA
Lin Jiang
1Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA

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Posted March 30, 2022.
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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