ArticleJournal of the American Chemical Society2024
A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Biocompatible ligand balancing in transition metal coordination enables benign in-cell protein arylation.Nature chemistry · 2026Article
- Biocompatible organometallics for in-cell protein arylation.Nature chemistry · 2026Article
- Engineering Light-Responsive Transcription Factors via Strategic Masking of Post-translational Modification Residues.Bioconjugate chemistry · 2026Article
- Hydrophilic BIPHEPHOS Ligand for Pd-Mediated Cysteine Allylation of Peptides and Proteins in Water.Organic letters · 2025Article
- Chemical Engineering of Transcription Factors Uncovered Cell-Permeable μMax Modulators.Journal of the American Chemical Society · 2025Article
- Late-Stage Aromatic C-H Bond Functionalization for Cysteine/Selenocysteine Bioconjugation.Journal of the American Chemical Society · 2025Article
- One-Pot Total Synthesis of a Post-translationally Modified Max Transcription Factor Sheds Light on Ser-Phosphorylation and Lys-Acetylation Crosstalk in DNA Binding.Organic letters · 2025Article
- Ligand-Enabled Selective Coupling of MIDA Boronates to Dehydroalanine-Containing Peptides and Proteins.Journal of the American Chemical Society · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modifications (PTMs) of proteins play central roles in regulating the protein structure, interactome, and functions. A notable modification site is the aromatic side chain of Tyr, which undergoes modifications such as phosphorylation and nitration. Despite the biological and physiological importance of Tyr-PTMs, our current understanding of the mechanisms by which these modifications contribute to human health and disease remains incomplete. This knowledge gap arises from the absence of natural amino acids that can mimic these PTMs and the lack of synthetic tools for the site-specific introduction of aromatic PTMs into proteins. Herein, we describe a facile method for the site-specific chemical installation of aromatic PTMs into proteins through palladium-mediated S-C(sp
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