AI Article Synopsis
- Parkinson's disease is the second most common neurodegenerative disorder, with abnormal aggregation of α-synuclein playing a key role in its development.
- Understanding the mechanisms behind α-synuclein aggregation is vital for creating better diagnostics and treatments.
- Various post-translational modifications like phosphorylation, ubiquitination, and nitration affect α-synuclein aggregation, highlighting potential therapeutic targets.
Article Abstract
Parkinson's disease is the second most common neurodegenerative disorder. Although the pathogenesis of Parkinson's disease is not entirely clear, the aberrant aggregation of α-synuclein has long been considered as an important risk factor. Elucidating the mechanisms that influence the aggregation of α-synuclein is essential for developing an effective diagnostic, preventative and therapeutic strategy to treat this devastating disease. The aggregation of α-synuclein is influenced by several post-translational modifications. Here, we summarized the major post-translational modifications (phosphorylation, ubiquitination, truncation, nitration, -GlcNAcylation) of α-synuclein and the effect of these modifications on α-synuclein aggregation, which may provide potential targets for future therapeutics.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6482271 | PMC |
| http://dx.doi.org/10.3389/fnins.2019.00381 | DOI Listing |
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