ArticleNature protocols2020
Large-scale site-specific mapping of the O-GalNAc glycoproteome.
Article in Nature protocols, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Review
- A Chemoenzymatic Labeling Strategy for Site-Specific Analysis of Tumor-Associated Sialyl Thomsen-Friedenreich Antigen.JACS Au · 2026Article
- GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis.Analytical chemistry · 2025Article
- Article
- Sonication-assisted protein extraction improves proteomic detection of membrane-bound and DNA-binding proteins from tumor tissues.Nature protocols · 2025Review
- AsymmetricJournal of the American Chemical Society · 2024Article
- Plasma/Serum Proteomics based on Mass Spectrometry.Protein and peptide letters · 2024Review
- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Quantitative mapping of the in vivo O-GalNAc glycoproteome in mouse tissues identifies GalNAc-T2 O-glycosites in metabolic disorder.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Large-Scale and Site-Specific Mapping of the Murine BrainAnalytical chemistry · 2023Article
- Ultraviolet Photodissociation Permits Comprehensive Characterization ofAnalytical chemistry · 2023Article
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- The next "sweet" spot for pancreatic ductal adenocarcinoma: Glycoprotein for early detection.Mass spectrometry reviews · 2023Review
- DecipheringMolecular omics · 2022Article
- Global mapping of GalNAc-T isoform-specificities and O-glycosylation site-occupancy in a tissue-forming human cell line.Nature communications · 2022Article
- Systematic analysis and comparison of O-glycosylation of five recombinant spike proteins in β-coronaviruses.Analytica chimica acta · 2022Article
- A novel role for GalNAc-T2 dependent glycosylation in energy homeostasis.Molecular metabolism · 2022Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- Putting the pieces together: mapping the O-glycoproteome.Current opinion in biotechnology · 2021Review
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein glycosylation is one of the most common protein modifications. A major type of protein glycosylation is O-GalNAcylation, in which GalNAc-type glycans are attached to protein Ser or Thr residues via an O-linked glycosidic bond. O-GalNAcylation is thought to play roles in protein folding, stability, trafficking and protein interactions, and identification of the site-specific O-GalNAc glycoproteome is a crucial step toward understanding the biological significance of the modification. However, lack of suitable methodology, absence of consensus sequon of O-GalNAcylation sites and complex O-GalNAc glycan structures pose analytical challenges. We recently developed a mass spectrometry-based method called extraction of O-linked glycopeptides (EXoO) that enables large-scale mapping of site-specific mucin-type O-GalNAcylation sites. Here we provide a detailed protocol for EXoO, which includes seven stages of: (1) extraction and proteolytic digestion of proteins to peptides, (2) sequential guanidination and de-salting of peptides, (3) enrichment of glycopeptides, (4) solid-phase peptide conjugation and release of O-GalNAc glycopeptides using the OpeRATOR protease, (5) liquid chromatography with tandem mass spectrometry analysis of O-GalNAc glycopeptides, (6) identification of O-GalNAc glycopeptides by database search and (7) quantification of O-GalNAc glycopeptides. Using this protocol, thousands of O-GalNAcylation sites from hundreds of glycoproteins with information regarding site-specific O-GalNAc glycan can be identified and quantified from complex samples. The protocol can be performed by a researcher with basic proteomics skills and takes about 4 d to complete.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.