ArticleThe Journal of biological chemistry2021
Decoding the impact of disease-causing mutations in an essential aminoacyl-tRNA synthetase.
Article in The Journal of biological chemistry, 2021. 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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3 citing papers in PubMed, 4 citations in OpenAlex.
- Strategies for detecting aminoacylation and aminoacyl-tRNA editingIsrael journal of chemistry · 2024Article
- Metabolomic analysis of Agkistrodon haly venom poisoning mouse treatment by Jidesheng snake pill based on GC-MS.Frontiers in pharmacology · 2024Article
- Aminoacyl-tRNA synthetases in human health and disease.Frontiers in physiology · 2022Review
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Abstract
Aminoacyl-tRNA synthetases are housekeeping enzymes that catalyze the specific attachment of amino acids onto cognate tRNAs, providing building blocks for ribosomal protein synthesis. Owing to the absolutely essential nature of these enzymes, the possibility that mutations in their sequence could be the underlying cause of diseases had not been foreseen. However, we are learning of patients bearing familial mutations in aminoacyl-tRNA synthetases at an exponential rate. In a recent issue of JBC, Jin et al. analyzed the impact of two such mutations in the very special bifunctional human glutamyl-prolyl-tRNA synthetase and convincingly decode how these mutations elicit the integrated stress response.
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