ArticleCommunications chemistry2026
Mechanistic study on the sulfate migration in glycosaminoglycans during MS fragmentation.
Article in Communications chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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
2 citing papers in PubMed.
- Application of Post-Glycosylation Modifying Enzymes for Mass Spectrometry Imaging of ModifiedJournal of the American Society for Mass Spectrometry · 2026Article
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
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Authors and funding
5 authors.
Funding
Abstract
Glycosaminoglycans use positional sulfation to encode binding specificity onto its sequence. Understanding these sulfation patterns constitute a major challenge. Previous studies hinted that sulfate groups can migrate along glycans during collision-induced dissociation in mass spectrometry (MS) experiments, forming isomeric fragments that can lead to incorrect structural assignments. We use ion-mobility - mass spectrometry to investigate the mechanism of this phenomenon in heparin sulfate disaccharides. The sulfate group migrates from the non-reducing to reducing end of the sugar, and the degree of migration does not depend on the structure of the label. The migration product has a sulfate group attached to either 6O- or 3O-position of GlcNAc, and the migration mechanism consists of multiple steps, with the sulfate group first shifting from the iduronic acid to the 6O-position of GlcNAc, and next to the 3O-position. The presented data offer insight into the complexity and unpredictability of sulfated sugar fragmentation in tandem MS and extensive investigations is required to determine whether this represents a singular case or a general phenomenon characteristic of deprotonated sulfated glycans.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.