Post-translational glycosylation diminishes α-synuclein pathology formation
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Publisher
Springer Science and Business Media LLC
Link
https://www.nature.com/articles/s41589-024-01553-0.pdf
Reference6 articles.
1. Eisenberg, D. & Jucker, M. The amyloid state of proteins in human diseases. Cell 148, 1188–1203 (2012). A review article on the fundamentals of amyloid fibril formation and pathogenesis.
2. Volpicelli-Daley, L. & Brundin, P. Prion-like propagation of pathology in Parkinson disease. Handb. Clin. Neurol. 153, 321–335 (2018). A review article on the evidence for progressive neurodegeneration by α-synuclein seeding mechanisms.
3. Ma, J., Wu, C. & Hart, G. W. Analytical and biochemical perspectives of protein O-GlcNAcylation. Chem. Rev. 121, 1513–1581 (2021). A review article on the biology of the O-GlcNAc modification.
4. Balana, A. T. & Pratt, M. R. Mechanistic roles for altered O-GlcNAcylation in neurodegenerative disorders. Biochem. J. 478, 2733–2758 (2021). A review article on the roles of O-GlcNAc in neurodegenerative diseases, including Parkinson’s disease.
5. Permanne, B. et al. O-GlcNAcase inhibitor ASN90 is a multimodal drug candidate for tau and α-synuclein proteinopathies. ACS Chem. Neurosci. 13, 1296–1314 (2022). A research paper that shows α-synuclein O-GlcNAc modification levels and reduced pathology after a drug-induced increase in O-GlcNAc.
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