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- W3137250723 endingPage "1071" @default.
- W3137250723 startingPage "1061" @default.
- W3137250723 abstract "α-Synuclein (α-syn), a small highly conserved presynaptic protein containing 140 amino acids, is thought to be the main pathological hallmark in related neurodegenerative disorders. Although the normal function of α-syn is closely involved in the regulation of vesicular neurotransmission in these diseases, the underlying mechanisms of post-translational modifications (PTMs) of α-syn in the pathogenesis of Parkinson's disease (PD) have not been fully characterized. The pathological accumulation of misfolded α-syn has a critical role in PD pathogenesis. Recent studies of factors contributing to α-syn-associated aggregation and misfolding have expanded our understanding of the PD disease process. In this Review, we summarize the structure and physiological function of α-syn, and we further highlight the major PTMs (namely phosphorylation, ubiquitination, nitration, acetylation, truncation, SUMOylation, and O-GlcNAcylation) of α-syn and the effects of these modifications on α-syn aggregation, which may elucidate mechanisms for PD pathogenesis and lay a theoretical foundation for clinical treatment of PD." @default.
- W3137250723 created "2021-03-29" @default.
- W3137250723 creator A5016715629 @default.
- W3137250723 creator A5037623893 @default.
- W3137250723 creator A5044906953 @default.
- W3137250723 creator A5065566476 @default.
- W3137250723 creator A5071981968 @default.
- W3137250723 date "2021-03-26" @default.
- W3137250723 modified "2023-10-16" @default.
- W3137250723 title "Effects of α-Synuclein-Associated Post-Translational Modifications in Parkinson’s Disease" @default.
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