Related Experiment Video
Updated: Jun 26, 2025

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
Published on: June 23, 2022
Post-translational Modification of α-Synuclein Modifies Monomer Dynamics and Aggregation Kinetics
Posttranslational modifications, like O-GlcNAcylation, impact alpha-Synuclein aggregation differently. Glycosylation at T72 slows aggregation, while S87 may accelerate early stages, showing modifications don't uniformly affect protein clumping in neurodegenerative diseases.
Area of Science:
- Biochemistry
- Neuroscience
- Protein Dynamics
Background:
- Alpha-Synuclein (α-Syn) aggregation is central to Parkinson's disease pathogenesis.
- Posttranslational modifications (PTMs) influence α-Syn aggregation kinetics.
- O-GlcNAcylation is a PTM observed to inhibit α-Syn aggregation.
Conclusions:
- Posttranslational modifications exert site-specific effects on α-Synuclein aggregation.
- O-GlcNAcylation at T72 inhibits aggregation, while S87 may promote early oligomerization.
- These findings highlight the complexity of α-Synuclein aggregation modulation by PTMs.
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Published on: May 30, 2021
09:16Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
Published on: June 26, 2018
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