ArticleJournal of the American Chemical Society2025
Chemical Carbonylation of Arginine in Peptides and Proteins.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Expanding the Chemoproteomic Toolkit to Asparagine and Glutamine.ACS chemical biology · 2026Article
- Global profiling of arginine reactivity and ligandability in the human proteome.Nature chemistry · 2026Article
- Virus Capsid Modifications Accompanying Inactivation during Iron Electrocoagulation Revealed by Proteomics, Infrared Spectroscopy, and Molecular Modeling.Environmental science & technology · 2026Article
- Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies.Beilstein journal of organic chemistry · 2026Review
- Targeting the Reactive Proteome: Recent Advances in Activity-Based Protein Profiling and Probe Design.Biomolecules · 2025Review
- Expanding Peptide Chemical Space via Acid-Mediated Arginine Modification.Organic letters · 2025Article
- PD-L1-targeted polymer-peptide-immune nanomedicine synergizes radiotherapy for durable tumor control.Bioactive materials · 2025Article
- Late-Stage Amination of Peptides on the Solid Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The chemoselective incorporation of arginine carbonylation post-translational modification (PTM) within proteins represents an underexplored frontier. This is largely due to the poor nucleophilicity and resistance to chemical oxidation of arginine. Drawing inspiration from the metal catalyzed oxidation (MCO) processes of arginine, we introduce a chemical methodology aimed at generating glutamate-5-semialdehyde from arginine residues within peptides and proteins. This innovative chemical approach capitalizes on the inherent weak nucleophilicity and oxidative properties of arginine. We also demonstrate the application of this strategy to selectively introduce both natural and unnatural post-translational modifications (PTMs) in a targeted manner. Our chemical approach offers a rapid, robust, and highly selective technique, facilitating chemoproteomic profiling of arginine sites prone to forming glutamate-5-semialdehyde PTM within the human proteome. Additionally, this methodology serves as a versatile platform for uncovering microenvironments that are susceptible to undergoing arginine carbonylation PTM, enabling the understanding of the effect of oxidative stress on arginine in proteins and the impact of these PTMs on cellular processes.
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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 Socratic graph.