ArticleJournal of the American Chemical Society2026
Expanding the Genetic Code with Lysine Aminoacylation.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Mechanistic and functional integration of sirtuin deacylases: from substrate specificity to biological outcomes.Glycoconjugate journal · 2026Review
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3 authors.
Funding
Abstract
Lysine aminoacylation is a newly discovered protein post-translational modification that is found in humans. However, few studies have been implemented to further investigate its function, possibly due to limited tools to produce target proteins with homogeneously aminoacylated lysine residues at specific sites. To achieve this goal, we applied the genetic code expansion strategy, engineered pyrrolysyl-tRNA synthetase, and established orthogonal translation systems for ten types of lysine aminoacylation compatible for both bacterial and mammalian cells. Because metabolic enzymes are preferred substrate proteins of lysine aminoacylation, we tested the effect of lysine aminoacylation on metabolic enzymes and demonstrated that lysine valylation and tyrosylation impaired pyruvate kinase and glucose-6-phosphate dehydrogenase activities, respectively. Further
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