ArticleIsrael journal of chemistry2024
Strategies for detecting aminoacylation and aminoacyl-tRNA editing
Article in Israel journal of chemistry, 2024. 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.
- Mechanisms and kinetic assays of aminoacyl-tRNA synthetases.FEBS letters · 2025Review
- Monitoring monomer-specific acyl-tRNA levels in cells with PARTI.Nucleic acids research · 2025Article
- Kinetic characterization of amino acid activation by aminoacyl-tRNA synthetases using radiolabelled γ-[FEBS open bio · 2025Article
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
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Authors and funding
3 authors.
Funding
Abstract
Aminoacyl-tRNA synthetases (aaRSs) maintain translational fidelity by ensuring the formation of correct aminoacyl-tRNA pairs. Numerous point mutations in human aaRSs have been linked to disease phenotypes. Structural studies of aaRSs from human pathogens encoding unique domains support these enzymes as potential candidates for therapeutics. Studies have shown that the identity of tRNA pools in cells changes between different cell types and under stress conditions. While traditional radioactive aminoacylation analyses can determine the effect of disease-causing mutations on aaRS function, these assays are not amenable to drug discovery campaigns and do not take into account the variability of the intracellular tRNA pools. Here, we review modern techniques to characterize aaRS activity
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