Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12
| Författare |
C. Pett W. Nasir Carina Sihlbom Britt-Marie Olsson V. Caixeta M. Schorlemer R. P. Zahedi G. Larson J. Nilsson U. Westerlind |
|---|---|
| Publicerad i | Angewandte Chemie International Edition |
| Volym | 57 |
| Nummer/häfte | 30 |
| Sidor | 9320-9324 |
| ISSN | 1433-7851 |
| Publiceringsår | 2018 |
| Publicerad vid |
Core Facilities, Proteomics |
| Sidor | 9320-9324 |
| Språk | en |
| Länkar |
dx.doi.org/10.1002/anie.201803540 |
| Ämnesord | glycopeptides, glycosylation, isomers, mass spectrometry, sialic acids, mass-spectrometry, damsela alpha-2,6-sialyltransferase, glycan, structure, linkage isomers, n-glycans, glycopeptides, identification, derivatization, strategy, sialyltransferase, Chemistry |
| Ämneskategorier | Biokemi och molekylärbiologi |
Distinct structural changes of the alpha 2,3/alpha 2,6-sialic acid glycosidic linkages on glycoproteins are of importance in cancer biology, inflammatory diseases, and virus tropism. Current glycoproteomic methodologies are, however, not amenable toward high-throughput characterization of sialic acid isomers. To enable such assignments, a mass spectrometry method utilizing synthetic model glycopeptides for the analysis of oxonium ion intensity ratios was developed. This method was successfully applied in large-scale glycoproteomics, thus allowing the site-specific structural characterization of sialic acid isomers.
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