ArticleACS chemical biology2018
Paramagnetic Tag for Glycosylation Sites in Glycoproteins: Structural Constraints on Heparan Sulfate Binding to Robo1.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Synthesis of Spin-Labeled α-/β-Galactosylceramides and Glucosylceramides as Electron Paramagnetic Probes.The Journal of organic chemistry · 2025Article
- Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.ACS chemical biology · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Human CEACAM1 N-domain dimerization is independent from glycan modifications.Structure (London, England : 1993) · 2022Article
- Enzymatic glycoengineering-based spin labelling of cell surface sialoglycans to enable their analysis by electron paramagnetic resonance (EPR) spectroscopy.The Analyst · 2022Article
- Article
- Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review.Molecular & cellular proteomics : MCP · 2021Review
- Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020Review
- Review
- Double Nitroxide Labeling by Copper-Catalyzed Azide-Alkyne Cycloadditions with Noncanonical Amino Acids for Electron Paramagnetic Resonance Spectroscopy.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
An enzyme- and click chemistry-mediated methodology for the site-specific nitroxide spin labeling of glycoproteins has been developed and applied. The procedure relies on the presence of single N-glycosylation sites that are present natively in proteins or that can be engineered into glycoproteins by mutational elimination of all but one glycosylation site. Recombinantly expressing glycoproteins in HEK293S (GnT1-) cells results in N-glycans with high-mannose structures that can be processed to leave a single GlcNAc residue. This can in turn be modified by enzymatic addition of a GalNAz residue that is subject to reaction with an alkyne-carrying TEMPO moiety using copper(I)-catalyzed click chemistry. To illustrate the procedure, we have made an application to a two-domain construct of Robo1, a protein that carries a single N-glycosylation site in its N-terminal domains. The construct has also been labeled with
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Registered trials
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