ReviewInternational journal of molecular sciences2021
Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 77 citations in OpenAlex.
- Inhibitors of Mycobacterium tuberculosis methionyl-tRNA synthetase are sensitive to the mutations E24A and L293A in aminoacyl-adenylate binding site.Biotechnology letters · 2026Article
- In Vivo Efficacy and Biochemical Target Engagement of a Chromene-Based Inhibitor of Trypanosoma cruzi Lysyl-tRNA Synthetase.Journal of medicinal chemistry · 2026Article
- Breaking the antimicrobial resistance dilemma: marine natural products, a treasure trove for the development of new anti-Marine life science & technology · 2026Review
- Discovery of a triple-site inhibitor targeting bacterial methionyl-tRNA synthetase through combined drug repurposing screening and generative AI-assisted optimization.Nucleic acids research · 2026Article
- Hybrid Dual-Context Prompted Cross-Attention Framework with Language Model Guidance for Multi-Label Prediction of Human Off-Target Ligand-Protein Interactions.International journal of molecular sciences · 2026Article
- Antibacterial Drug Discovery: Deep Learning Successes and Challenges through the Structural Biology Lens.Computational and structural biotechnology journal · 2026Review
- Mechanisms and kinetic assays of aminoacyl-tRNA synthetases.FEBS letters · 2025Review
- A genome-wide CRISPR screen in Anopheles mosquito cells identifies fitness and immune cell function-related genes.Nature communications · 2025Article
- Design and Development of Lysyl tRNA Synthetase Inhibitors, for the Treatment of Tuberculosis.Journal of medicinal chemistry · 2025Article
- Antibiotics re-booted-time to kick back against drug resistance.npj antimicrobials and resistance · 2025Review
- What Are the Drivers Triggering Antimicrobial Resistance Emergence and Spread? Outlook from a One Health Perspective.Antibiotics (Basel, Switzerland) · 2025Review
- The mechanism of lineage-specific tRNA recognition by bacterial tryptophanyl-tRNA synthetase and its implications for inhibitor discovery.Nucleic acids research · 2025Article
- Identification of novelFuture medicinal chemistry · 2025Article
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
- Article
- Simultaneous determination of cytosolic aminoacyl-tRNA synthetase activities by LC-MS/MS.Nucleic acids research · 2024Article
- Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Potential Piperolactam A Isolated From Piper betle as Natural Inhibitors of Brucella Species Aminoacyl-tRNA Synthetase for Livestock Infections: In Silico Approach.Veterinary medicine and science · 2024Article
- A Review of Antibacterial Candidates with New Modes of Action.ACS infectious diseases · 2024Review
- Identification of novel antistaphylococcal hit compounds.The Journal of antibiotics · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aminoacyl-tRNA synthetases (aaRSs) catalyze the esterification of tRNA with a cognate amino acid and are essential enzymes in all three kingdoms of life. Due to their important role in the translation of the genetic code, aaRSs have been recognized as suitable targets for the development of small molecule anti-infectives. In this review, following a concise discussion of aaRS catalytic and proof-reading activities, the various inhibitory mechanisms of reported natural and synthetic aaRS inhibitors are discussed. Using the expanding repository of ligand-bound X-ray crystal structures, we classified these compounds based on their binding sites, focusing on their ability to compete with the association of one, or more of the canonical aaRS substrates. In parallel, we examined the determinants of species-selectivity and discuss potential resistance mechanisms of some of the inhibitor classes. Combined, this structural perspective highlights the opportunities for further exploration of the aaRS enzyme family as antimicrobial targets.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.