ArticleGlycobiology2021
Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.
Article in Glycobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- The protein sequence modulates terminal GalNAc incorporation during N-glycan biosynthesis.Glycobiology · 2026Article
- A random fractionalMagnetic resonance letters · 2026Article
- Cupriavidus necator, an alternative source for isotopic enrichment of proteins expressed in insect cells for NMR investigations.Journal of biomolecular NMR · 2026Article
- Conformational Preferences for N-Glycans at the Surface of CEACAM1-Ig1.ACS chemical biology · 2026Article
- Chemical Shift Analysis of Oligosaccharides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- NMR Chemical Shift Prediction of Glycopeptides and Glycoproteins Aided by the Computer Program CASPER.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The impact of glycosylation on the structure, function, and interactions of CD14.Glycobiology · 2024Article
- Review
- Synthesis ofOrganic & biomolecular chemistry · 2023Article
- Primary Structure of Glycans by NMR Spectroscopy.Chemical reviews · 2023Review
- AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- NMR analysis suggests the terminal domains of Robo1 remain extended but are rigidified in the presence of heparan sulfate.Scientific reports · 2022Article
- The antibody-binding Fc gamma receptor IIIa / CD16a is N-glycosylated with high occupancy at all five sites.Current research in immunology · 2022Article
- Decoding human-macaque interspecies differences in Fc-effector functions: The structural basis for CD16-dependent effector function in Rhesus macaques.Frontiers in immunology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Preparation of samples for nuclear magnetic resonance (NMR) characterization of larger proteins requires enrichment with less abundant, NMR-active, isotopes such as 13C and 15N. This is routine for proteins that can be expressed in bacterial culture where low-cost isotopically enriched metabolic substrates can be used. However, it can be expensive for glycosylated proteins expressed in mammalian culture where more costly isotopically enriched amino acids are usually used. We describe a simple, relatively inexpensive procedure in which standard commercial media is supplemented with 13C-enriched glucose to achieve labeling of all glycans plus all alanines of the N-terminal domain of the highly glycosylated protein, CEACAM1. We demonstrate an ability to detect partially occupied N-glycan sites, sites less susceptible to processing by an endoglycosidase, and some unexpected truncation of the amino acid sequence. The labeling of both the protein (through alanines) and the glycans in a single culture requiring no additional technical expertise past standard mammalian expression requirements is anticipated to have several applications, including structural and functional screening of the many glycosylated proteins important to human health.
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