ReviewThe Journal of biological chemistry2019
Evolution of the multi-tRNA synthetase complex and its role in cancer.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed, 98 citations in OpenAlex.
- Nuclear localization of the glutaminyl-tRNA synthetase QARS reveals its role in DNA damage response in ovarian cancer.Nature communications · 2026Article
- LARS regulates cellular senescence and autophagy in liver cancer cells.Cell death & disease · 2026Article
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Proteasome dysfunction underlies HERC2-linked neurodevelopmental disorder with Angelman-like clinical features.Cell death discovery · 2026Article
- The redundant protein synthesis gene Aimp1 challenges the canonical inverse relationship between translation and autophagy.Communications biology · 2026Article
- LARS promotes osteosarcoma proliferation through leucine-dependent PRIM2 translation and DNA replication activation.Journal of experimental & clinical cancer research : CR · 2026Article
- Variant-specific interaction of kinectin 1 with the multi-tRNA synthetase complex regulates ER sheet organization.iScience · 2026Article
- Mycoplasma penetrans methionyl-tRNA synthetase dimerizes via tandem N-terminal ancillary domains.PloS one · 2026Article
- Nanopore sequencing of intact aminoacylated tRNAs.Nature communications · 2025Article
- AIMP3 maintains cardiac homeostasis by regulating the editing activity of methionyl-tRNA synthetase.Nature cardiovascular research · 2025Article
- Overview of genetic variants in a cohort of Iranian patients with leukodystrophy.Scientific reports · 2025Article
- Transfer RNA and small molecule therapeutics for aminoacyl-tRNA synthetase diseases.The FEBS journal · 2025Review
- Causal effect of gut microbiota metabolic pathways on CSAG1 expression in chondrosarcoma: a mendelian randomization analysis.BMC cancer · 2025Article
- Serine mistranslation induces the integrated stress response through the P stalk.The Journal of biological chemistry · 2025Article
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- A methyltransferase-independent role for METTL1 in tRNA aminoacylation and oncogenic transformation.Molecular cell · 2025Article
- Setting the Stage for Treatment of Aminoacyl-tRNA Synthetase (ARS)1-Deficiencies: Phenotypic Characterization and a Review of Treatment Effects.Journal of inherited metabolic disease · 2025Review
- Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase.Nucleic acids research · 2025Article
- Structural basis for aminoacylation of cellular modified tRNAbioRxiv : the preprint server for biology · 2024Article
- MTCH2 promotes the malignant progression of ovarian cancer through the upregulation of AIMP2 expression levels, mitochondrial dysfunction and by mediating energy metabolism.Oncology letters · 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
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases (ARSs) are enzymes that ligate their cognate amino acids to tRNAs for protein synthesis. However, recent studies have shown that their functions are expanded beyond protein synthesis through the interactions with diverse cellular factors. In this review, we discuss how ARSs have evolved to expand and control their functions by forming protein assemblies. We particularly focus on a macromolecular ARS complex in eukaryotes, named multi-tRNA synthetase complex (MSC), which is proposed to provide a channel through which tRNAs reach bound ARSs to receive their cognate amino acid and transit further to the translation machinery. Approximately half of the ARSs assemble into the MSC through
Indexed as
Identifiers
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.