ArticleAnalytical chemistry2026
Cross-Linking and Covalent Labeling Mass Spectrometry Reveal Proteoform-Driven Conformational Changes in Alpha Synuclein.
Article in Analytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Proteoform-Resolved Cross-Linking Reveals Environment-Dependent Structural Effects of α-Synuclein S129 Phosphorylation.Journal of the American Chemical Society · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Phosphorylation of serine 129 (pS129) in the intrinsically disordered protein alpha synuclein has long been associated with neurodegenerative diseases. In recent years, the functional relevance of pS129 has been uncovered by electrophysiology, immunoprecipitation, and proteomics, revealing its intricate connection to neurotransmitter release and synaptic vesicle (SV) cycling. In this study, chemical cross-linking and covalent labeling of alpha synuclein and pS129, as well as an additional form encountered in the brain, oxidized M1, M5, M116, and M127 α-synuclein, are examined utilizing tandem mass spectrometry. Covalent labeling of proteins identifies solvent accessible residues and reveals the hydrophobicity (or hydrophilicity) of their microenvironment, while cross-linking of proteins maps the proximity of residue pairs. This work investigates how biologically relevant post-translational modifications alter the structural ensembles of alpha synuclein proteoforms. The combination of covalent labeling and cross-linking unequivocally demonstrates that phosphorylation at S129 stabilizes a more compact alpha synuclein conformation.
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Registered trials
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