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Supramolecular Modulation of Structural Polymorphism in Pathogenic α-Synuclein Fibrils Using Copper(II) Coordination

Journal Article · · Angewandte Chemie (International Edition)
 [1];  [2];  [1];  [2];  [3];  [4];  [2];  [1]
  1. Department of Chemistry, Korea University, Seoul 02841 Republic of Korea
  2. Department of Biomedical Sciences, Neuroscience Research Institute, Seoul National University College of Medicine, Seoul 03080 Republic of Korea
  3. Department of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles CA 90095 USA; Systems Biology Center, Research Affairs, Faculty of Medicine, Chulalongkorn University, Bangkok 10330 Thailand
  4. Department of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles CA 90095 USA; Department of Biological Chemistry, David Geffen School of Medicine, University of California-Los Angeles, Los Angeles CA 90095 USA; UCLA Molecular Biology Institute, UCLA/DOE Institute for Genomics and Proteomics, University of California-Los Angeles, Los Angeles CA 90095 USA
+ Show Author Affiliations

Not provided.

Research Organization:
Univ. of California, Los Angeles, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
DOE Contract Number:
FC02-02ER63421
OSTI ID:
1537468
Journal Information:
Angewandte Chemie (International Edition), Vol. 57, Issue 12; ISSN 1433-7851
Publisher:
Wiley
Country of Publication:
United States
Language:
English

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Remote His50 Acts as a Coordination Switch in the High-Affinity N-Terminal Centered Copper(II) Site of α-Synuclein April 2015
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Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril August 2016
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