Advances in chemical probing of protein O-GlcNAc glycosylation: structural role and molecular mechanisms
Author:
Affiliation:
1. Chemical Immunology Lab, Centre for Cooperative Research in Biosciences, CIC-bioGUNE, Basque Research and Technology Alliance (BRTA), Derio 48160, Biscay, Spain
2. Ikerbasque, Basque Foundation for Science, Bilbao 48013, Spain
Abstract
Funder
H2020 European Research Council
Ministerio de Ciencia e Innovación
European Commission
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2021/CS/D0CS01275K
Reference265 articles.
1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.
2. The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc.
3. Crosstalk between phosphorylation and O‐Glc NA cylation: friend or foe
4. O-Linked GlcNAc Transferase Is a Conserved Nucleocytoplasmic Protein Containing Tetratricopeptide Repeats
5. Dynamic Glycosylation of Nuclear and Cytosolic Proteins
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