ArticleJournal of the American Chemical Society2025
A Chemical Mechanistic Path Leads the Way to Cellular Argpyrimidine.
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 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- Rational Design of an Electronically Gated Dicyano-BODIPY Platform for Reversible-Covalent Imaging of Methylglyoxal.JACS Au · 2026Article
- Profiling Selectivity for theBiochemistry · 2026Article
- Oxidative Stress, Pro-Inflammatory Response, Cytotoxicity and Apoptosis Induced by Contemporary Endodontic Sealers in Human Periodontal Ligament Fibroblasts.Journal of functional biomaterials · 2026Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Argpyrimidine (APY) is a methylglyoxal-derived advanced glycation end-product (AGE) that has been associated with multiple diseases. As APY forms without an enzyme, it remains exceptionally difficult to pinpoint where APY is likely to be found, both on individual proteins and in cells. In this study, we used a peptide model system and mass spectrometry analysis to investigate the chemical mechanism through which APY arises from methylglyoxal (MGO), a biologically relevant glycating agent. Consistent with other proposed APY formation mechanisms, our results identify AGE species with a mass change of [M + 144], presumably including tetrahydropyrimidine (THP), as a direct precursor to APY. However, our results rule out previously proposed reductone or oxidative decarboxylation mechanisms. Instead, we show that a formal oxidation step is not required, and that formate is released instead of CO
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