Global view of human protein glycosylation pathways and functions
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
https://www.nature.com/articles/s41580-020-00294-x.pdf
Reference258 articles.
1. Fournet, M., Bonté, F. & Desmoulière, A. Glycation damage: a possible hub for major pathophysiological disorders and aging. Aging Dis. 9, 880–900 (2018).
2. Steentoft, C. et al. Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. EMBO J. 32, 1478–1488 (2013). This paper presents a deep analysis of the human GalNAc-type O-glycoproteome.
3. Zielinska, D. F., Gnad, F., Wiśniewski, J. R. & Mann, M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897–907 (2010). This paper presents a deep analysis of N-glycosites in the human proteome.
4. Hart, G. W. Nutrient regulation of signaling and transcription. J. Biol. Chem. 294, 2211–2231 (2019).
5. Hart, G. W. et al. Glycosylation of Nuclear and Cytoplasmic Proteins is as Abundant and as Dynamic as Phosphorylation. in Glyco- and Cellbiology (eds Wieland, F. & Reutter, W.) 91–103 (Springer, 1994).
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