ReviewInternational journal of molecular sciences2015
Aminoacyl-tRNA synthetase complexes in evolution.
Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
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Who cites it
32 citing papers in PubMed.
- The genotypic and phenotypic spectrum of PARS2-related infantile-onset encephalopathy.Journal of human genetics · 2018Trial
- Cryo-EM structure of the LARS1:IARS1 complex reveals a nutrient-responsive switch controlling mTORC1 signaling.Nature communications · 2026Article
- Variant-specific interaction of kinectin 1 with the multi-tRNA synthetase complex regulates ER sheet organization.iScience · 2026Article
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- Protein-Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease.Life (Basel, Switzerland) · 2024Review
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- Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.Protein science : a publication of the Protein Society · 2023Article
- Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.The Journal of biological chemistry · 2022Article
- Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.Cellular and molecular life sciences : CMLS · 2022Article
- Aminoacyl-tRNA synthetases in human health and disease.Frontiers in physiology · 2022Review
- Aminoacyl-tRNA Synthetases: On Anti-Synthetase Syndrome and Beyond.Frontiers in immunology · 2022Review
- Structural basis for the dynamics of human methionyl-tRNA synthetase in multi-tRNA synthetase complexes.Nucleic acids research · 2021Article
- Regulation of ex-translational activities is the primary function of the multi-tRNA synthetase complex.Nucleic acids research · 2021Article
- The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability.iScience · 2021Article
- SUMOylation of Arginyl tRNA Synthetase Modulates theFrontiers in cell and developmental biology · 2021Article
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- Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.The Journal of biological chemistry · 2019Article
- Metabolic origin of the fused aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases are essential enzymes for interpreting the genetic code. They are responsible for the proper pairing of codons on mRNA with amino acids. In addition to this canonical, translational function, they are also involved in the control of many cellular pathways essential for the maintenance of cellular homeostasis. Association of several of these enzymes within supramolecular assemblies is a key feature of organization of the translation apparatus in eukaryotes. It could be a means to control their oscillation between translational functions, when associated within a multi-aminoacyl-tRNA synthetase complex (MARS), and nontranslational functions, after dissociation from the MARS and association with other partners. In this review, we summarize the composition of the different MARS described from archaea to mammals, the mode of assembly of these complexes, and their roles in maintenance of cellular homeostasis.
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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.