ArticleAnalytical chemistry2021
An Azo Coupling-Based Chemoproteomic Approach to Systematically Profile the Tyrosine Reactivity in the Human Proteome.
Article in Analytical chemistry, 2021. 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, 20 citations in OpenAlex.
- Introducing azobenzenes as solid phase peptide synthesis linkers.RSC chemical biology · 2026Article
- Global profiling of arginine reactivity and ligandability in the human proteome.Nature chemistry · 2026Article
- Recent Advances in Bioconjugation of Aromatic Amino Acid Residues by a Reactivity-Guided Approach.Chemical record (New York, N.Y.) · 2026Review
- Affinity-Driven Aryl Diazonium Labeling of Peptide Receptors on Living Cells.Journal of the American Chemical Society · 2024Article
- A global view of the human post-translational modification landscape.The Biochemical journal · 2023Review
- Recent developments in the cleavage, functionalization, and conjugation of proteins and peptides at tyrosine residues.Chemical science · 2023Review
- [Advances in applications of activity-based chemical probes in the characterization of amino acid reactivities].Se pu = Chinese journal of chromatography · 2023Review
- Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation.Biochemistry · 2022Article
- Donor-Acceptor Pyridinium Salts for Photo-Induced Electron-Transfer-Driven Modification of Tryptophan in Peptides, Proteins, and Proteomes Using Visible Light.Journal of the American Chemical Society · 2022Article
- Protein Modification via Mild Photochemical Isomerization of Triazenes to Release Aryl Diazonium Ions.Bioconjugate chemistry · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The tyrosine residue of proteins participates in a wide range of activities including enzymatic catalysis, protein-protein interaction, and protein-ligand binding. However, the functional annotation of the tyrosine residues on a large scale is still very challenging. Here, we report a novel method integrating azo coupling, bioorthogonal chemistry, and multiplexed proteomics to globally investigate the tyrosine reactivity in the human proteome. Based on the azo-coupling reaction between aryl diazonium salt and the tyrosine residue, two different probes were evaluated, and the probe with the best performance was employed to further study the tyrosine residues in the human proteome. Then, tagged tyrosine-containing peptides were selectively enriched using bioorthogonal chemistry, and after the cleavage, a small tag on the peptides perfectly fits for site-specific analysis by MS. Coupling with multiplexed proteomics, we quantified over 5000 tyrosine sites in MCF7 cells, and these quantified sites displayed a wide range of reactivity. The tyrosine residues with high reactivity were found on functionally and structurally diverse proteins, including those with the catalytic activity and binding property. This method can be extensively applied to advance our understanding of protein functions and facilitate the development of covalent drugs to regulate protein activity.
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