ArticleNature chemistry2025
A selenoxide for single-atom protein modification of tyrosine residues enabled by water-resistant chalcogen and hydrogen bonding.
Article in Nature chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Copper-Catalyzed Enantioselective Synthesis of Chiral Selenium-Based Versatile Synthons.ACS central science · 2026Article
- Thianthrenium Salts in Photochemistry.Accounts of chemical research · 2026Article
- Cationic Selenuranes - Bench-Stable Sources of Se(III) Radicals.Angewandte Chemie (International ed. in English) · 2025Article
- On-DNA C-H functionalization of electron-rich arenes for DNA-encoded libraries.Nature chemistry · 2025Article
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13 authors.
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Abstract
Post-translational modifications such as phosphorylation and acetylation are often minor structural modifications that can have profound effects on protein structure and thus broaden protein functions. Nevertheless, studying these effects directly is often out of reach because no general chemistry exists to introduce small modifications selectively; either a large, stable linker structure is selectively installed on protein residues, or a small substituent is introduced at the risk of low selectivity due to the use of reactive, indiscriminate molecules. Here we report a C-H functionalization reaction of tyrosine residues to access peptides and proteins modified by small structural changes including single-atom substitutions. A rationally designed selenoxide introduces a versatile selenonium linchpin featuring a C
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