The DOI matches its Crossref record; 114 of the 114 references it cites were found in a registry or an index.
Mucin‐type O‐glycosylation – putting the pieces together
Abstract
The O‐glycosylation of Ser and Thr by N‐acetylgalactosamine‐linked (mucin‐type) oligosaccharides is often overlooked in protein analysis. Three characteristics make O‐linked glycosylation more difficult to analyse than N‐linked glycosylation, namely: (a) no amino acid consensus sequence is known; (b) there is no universal enzyme for the release of O‐glycans from the protein backbone; and (c) the density and number of occupied sites may be very high. For significant biological conclusions to be drawn, the complete picture of O‐linked glycosylation on a protein needs to be determined. This review specifically addresses the analytical approaches that have been used, and the challenges remaining, in the characterization of both the composition and structure of mucin‐type O‐glycans, and the determination of the occupancy and heterogeneity at each amino acid attachment site.
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Glycosylation in health and disease
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The gastrointestinal mucus system in health and disease
Johansson, M. E. V., Sjövall, H., & Hansson, G. C. (2013) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2013.35 · Cited by 1,438
Click Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 380
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Fast and comprehensive N- and O-glycoproteomics analysis with MSFragger-Glyco
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Metadata
- Authors
- Jensen, P. H., Kolarich, D., & Packer, N. H.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2009-12-15
- Volume
- 277
- Issue
- 1
- Pages
- 81-94
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1505123947
- Cited by
- 252
- References
- 114
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- closed
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