Drugging tRNA aminoacylation
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Summary
This work reviews available data regarding known aminoacylation inhibitors as well as key amino-acid residues in aminoacyl-tRNA synthetases (aaRSs) and nucleotides in tRNA that determine the specificity and strength of the aaRS-t RNA interaction.
- Type
- article
- Published
- 2018-02-02
- Cited by
- 60
- References
- 119
- Access
- Open access
- OpenAlex
- https://openalex.org/W29345185
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:38527939
Keywords
Valencia, Humanities, Art, Biology
References
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- 11th IUBMB Focused Meeting on the Aminoacyl-tRNA Synthetases: Sailing a New Sea of Complex Functions in Human Biology and Disease
- Aminoacyl-tRNA synthetases, therapeutic targets for infectious diseases
- Transfer RNA function and evolution
- Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli
- Uncovering Deep Phylogenetic Signal in Plastid Genomes
- Discovery of Small‐Molecule Antibiotics against a Unique tRNA‐Mediated Regulation of Transcription in Gram‐Positive Bacteria
- Structure-guided enhancement of selectivity of chemical probe inhibitors targeting bacterial seryl-tRNA synthetase
- Translational control of antibiotic resistance
- Self-immunity guided identification of threonyl-tRNA synthetase as the molecular target of obafluorin, a β-lactone antibiotic
- Targeting tRNA-synthetase interactions towards novel therapeutic discovery against eukaryotic pathogens
- Dual-targeted hit identification using pharmacophore screening
- Molecular evidence for the evolution of the eukaryotic mitochondrial arginyl‐tRNA synthetase from the prokaryotic suborder Cystobacterineae
- Dual-target inhibitors of mycobacterial aminoacyl-tRNA synthetases among N-benzylidene-N'-thiazol-2-yl-hydrazines.
- Discovery of novel tRNA-amino acid dual-site inhibitors against threonyl-tRNA synthetase by fragment-based target hopping.
- Mutations in ArgS Arginine-tRNA Synthetase Confer Additional Antibiotic Tolerance Protection to Extended-Spectrum-β-Lactamase-Producing Burkholderia thailandensis
- Aminoacyl-tRNA synthetases
- Molecular investigation of pathogenic bacteria in the presence of phenolic acids
- The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases
- Pseudomonas aeruginosa Presents Multiple Vital Changes in Its Proteome in the Presence of 3-Hydroxyphenylacetic Acid, a Promising Antimicrobial Agent
- A Label-Free Cellular Proteomics Approach to Decipher the Antifungal Action of DiMIQ, a Potent Indolo[2,3-b]Quinoline Agent, against Candida albicans Biofilms
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