ReviewNature reviews. Drug discovery2019
Aminoacyl-tRNA synthetases as therapeutic targets.
Review in Nature reviews. Drug discovery, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
165 citing papers in PubMed, 260 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
- Atomic-Level Structures Reveal How a Repurposed 3‑Aminopyrazine-2-carboxamide Scaffold InhibitsACS omega · 2026Article
- Computational Modeling and MM-PBSA-Based Molecular Dynamics Investigation of Unexplored tRNA Isoleucine Lysidine Synthetase from Mycobacterium tuberculosis with Hyperbranched Amoxicilloyl-Poly-L-Lysine.Journal of molecular modeling · 2026Article
- In Vivo Efficacy and Biochemical Target Engagement of a Chromene-Based Inhibitor of Trypanosoma cruzi Lysyl-tRNA Synthetase.Journal of medicinal chemistry · 2026Article
- Unveiling isoleucyl-tRNA synthetase 2 as a novel driver of breast cancer via β-catenin pathway activation.Journal of cell communication and signaling · 2026Article
- Nuclear localization of the glutaminyl-tRNA synthetase QARS reveals its role in DNA damage response in ovarian cancer.Nature communications · 2026Article
- Advances in Research onGenes · 2026Review
- Rapid Fragment Screening byAngewandte Chemie (International ed. in English) · 2026Article
- Metabolomic profiling in IgA nephropathy: urinary and salivary biomarker insights.BMC nephrology · 2026Article
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Host mature tRNAome as a decoding switch regulates antiviral and proviral responses.Nature communications · 2026Article
- Nanomedicine-based lactate metabolism and lactylation regulation for exploring new therapeutic strategies in cancer.Materials today. Bio · 2026Review
- Building a credibility-based framework for target discovery: Perspectives from tRNA synthetase-linked metabolic diseases.Briefings in bioinformatics · 2026Article
- Article
- Variant-specific interaction of kinectin 1 with the multi-tRNA synthetase complex regulates ER sheet organization.iScience · 2026Article
- Decreased expression of immune activator WARS1 and other pro-inflammatory mediators in type 1-like macrophages as an associated mode of action in response to fucoidan from marine brown algae.Frontiers in immunology · 2026Article
- Aminoacyl-tRNA synthetases in tumor immunity: canonical translation, source-resolved immune circuits and therapeutic opportunities.Frontiers in immunology · 2026Review
- Isoleucyl-tRNA synthetase depletion reveals vulnerabilities in Mycobacterium abscessus and Mycobacterium marinum.Communications biology · 2025Article
- Design and Development of Lysyl tRNA Synthetase Inhibitors, for the Treatment of Tuberculosis.Journal of medicinal chemistry · 2025Article
- Exploration of Phosphoproteins inPathogens (Basel, Switzerland) · 2025Article
105 more citing papers are in PubMed but not listed here.
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 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases (ARSs) are essential enzymes for protein synthesis with evolutionarily conserved enzymatic mechanisms. Despite their similarity across organisms, scientists have been able to generate effective anti-infective agents based on the structural differences in the catalytic clefts of ARSs from pathogens and humans. However, recent genomic, proteomic and functionomic advances have unveiled unexpected disease-associated mutations and altered expression, secretion and interactions in human ARSs, revealing hidden biological functions beyond their catalytic roles in protein synthesis. These studies have also brought to light their potential as a rich and unexplored source for new therapeutic targets and agents through multiple avenues, including direct targeting of the catalytic sites, controlling disease-associated protein-protein interactions and developing novel biologics from the secreted ARS proteins or their parts. This Review addresses the emerging biology and therapeutic applications of human ARSs in diseases including autoimmune and rare diseases, and cancer.
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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.