ArticleBiochemistry2018
Optimization of Chemoenzymatic Mass Tagging by Strain-Promoted Cycloaddition (SPAAC) for the Determination of O-GlcNAc Stoichiometry by Western Blotting.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.
- Tools for investigating O-GlcNAc in signaling and other fundamental biological pathways.The Journal of biological chemistry · 2024Pooled it
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Functional analysis of O-GlcNAcylation by networking of OGT interactors and substrates.Nature chemical biology · 2026Article
- A cysteine reactive chloroalkane probe enables HaloTag ligation for downstream chemical proteomics analysis.RSC chemical biology · 2026Article
- Chemoenzymatic Labeling Method for Detection of O-GlcNAcylated α-Synuclein Proteins by Western Blot.Bio-protocol · 2026Article
- Modulation of O-GlcNAc cycling influences α-synuclein amplification, degradation, and associated neuroinflammatory pathology.Molecular neurodegeneration · 2025Article
- Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein.Journal of virology · 2025Article
- A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice.Glycobiology · 2025Article
- O-GlcNAcylation of enolase 1 serves as a dual regulator of aerobic glycolysis and immune evasion in colorectal cancer.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone.Protein science : a publication of the Protein Society · 2024Article
- Studying the O-GlcNAcome of human placentas using banked tissue samples.Glycobiology · 2024Article
- Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.Journal of the American Chemical Society · 2024Article
- Cu-Catalyzed Azide-Alkyne-Thiol Reaction Forms Ubiquitous Background in Chemical Proteomic Studies.Journal of the American Chemical Society · 2024Article
- Improved deconvolution of natural products' protein targets using diagnostic ions from chemical proteomics linkers.Beilstein journal of organic chemistry · 2024Review
- O-GlcNAc regulates YTHDF1 and YTHDF3 activity.Nature cell biology · 2023Article
- O-GlcNAcylation determines the translational regulation and phase separation of YTHDF proteins.Nature cell biology · 2023Article
- The s-oph enzyme for efficient degradation of polyvinyl alcohol: soluble expression and catalytic properties.Molecular biology reports · 2023Article
- Chemical Biology Approaches to Understanding Neuronal O-GlcNAcylation.Israel journal of chemistry · 2023Article
- Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The dynamic modification of intracellular proteins by O-linked β -N-acetylglucosamine (O-GlcNAcylation) plays critical roles in many cellular processes. Although various methods have been developed for O-GlcNAc detection, there are few techniques for monitoring glycosylation stoichiometry and state (i.e., mono-, di-, etc., O-GlcNAcylated). Measuring the levels of O-GlcNAcylation on a given substrate protein is important for understanding the biology of this critical modification and for prioritizing substrates for functional studies. One powerful solution to this limitation involves the chemoenzymatic installation of polyethylene glycol polymers of defined molecular mass onto O-GlcNAcylated proteins. These "mass tags" produce shifts in protein migration during sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that can be detected by Western blotting. Broad adoption of this method by the scientific community has been limited, however, by a lack of commercially available reagents and well-defined protein standards. Here, we develop a "click chemistry" approach to this method using entirely commercial reagents and confirm the accuracy of the approach using a semisynthetic O-GlcNAcylated protein. Our studies establish a new, expedited experimental workflow and standardized methods that can be readily utilized by non-experts to quantify the O-GlcNAc stoichiometry and state on endogenous proteins in any cell or tissue lysate.
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Registered trials
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