ArticleScientific reports2017
Characterization of O-acetylation in sialoglycans by MALDI-MS using a combination of methylamidation and permethylation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Profiling O-Acetylation in Sialoglycans Using MALDI-TOF and LC-MS/MS with Methylamidation and Permethylation Derivatization.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Efficient Detection of N-sialoglycans in N-glycomics Using Mass Spectrometry by nMatch.Applied biochemistry and biotechnology · 2025Article
- The Ulcerative Colitis-Associated Gene NXPE1 Catalyzes Glycan Modifications on Colonic Mucin.Journal of the American Chemical Society · 2025Article
- Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry.Nature communications · 2023Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- An Integrated Strategy Reveals Complex Glycosylation of Erythropoietin Using Mass Spectrometry.Journal of proteome research · 2021Article
- Glycomics studies using sialic acid derivatization and mass spectrometry.Nature reviews. Chemistry · 2020Review
- Isolation and characterization of glycosylated neuropeptides.Methods in enzymology · 2019Article
- Sialic acid derivatization for glycan analysis by mass spectrometry.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
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6 authors.
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Abstract
O-Acetylation of sialic acid in protein N-glycans is an important modification and can occur at either 4-, 7-, 8- or 9-position in various combinations. This modification is usually labile under alkaline reaction conditions. Consequently, a permethylation-based analytical method, which has been widely used in glycomics studies, is not suitable for profiling O-acetylation of sialic acids due to the harsh reaction conditions. Alternatively, methylamidation can be used for N-glycan analysis without affecting the base-labile modification of sialic acid. In this report, we applied both permethylation and methylamidation approaches to the analysis of O-acetylation in sialic acids. It has been demonstrated that methylamidation not only stabilizes sialic acids during MALDI processing but also allow for characterization of their O-acetylation pattern. In addition, LC-MS/MS experiments were carried out to distinguish between the O-acetylated glycans with potential isomeric structures. The repeatability of methylamidation was examined to evaluate the applicability of the approach to profiling of O-acetylation in sialic acids. In conclusion, the combination of methylamidation and permethylation methodology is a powerful MALDI-TOF MS-based tool for profiling O-acetylation in sialic acids applicable to screening of N-glycans.
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