O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics
Author:
Affiliation:
1. Department of Physics and Astronomy, Michigan State University, East Lansing, Michigan 48824, United States
2. Department of Chemistry, University of Southern California, Los Angeles, California 90089, United States
Funder
Division of Molecular and Cellular Biosciences
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Link
https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.4c00301
Reference39 articles.
1. Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein
2. Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies
3. Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation
4. Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O‐GlcNAc)
5. Analytical and Biochemical Perspectives of Protein O-GlcNAcylation
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