ReviewFEMS microbiology reviews2008
Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed.
Review in FEMS microbiology reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 91 citations in OpenAlex.
- A metabolite-bridged complex between SerRS and SIRT2 couples NAD⁺ metabolism to translation control.Nature communications · 2026Article
- Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026Review
- Interactions ofFoods (Basel, Switzerland) · 2024Article
- Deciphering the Intracellular Action of the Antimicrobial Peptide A11 via an In-Depth Analysis of Its Effect on the Global Proteome ofACS infectious diseases · 2024Article
- Protein Thermal Stability Changes Induced by the Global Methylation Inhibitor 3-Deazaneplanocin A (DZNep).Biomolecules · 2024Article
- Early-onset dysphagia and severe neurodevelopmental disorder as early signs in a patient with two novel variants in NARS1: a case report and brief review of the literature.Neurogenetics · 2024Review
- Protein-Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease.Life (Basel, Switzerland) · 2024Review
- RNA granule-clustered mitochondrial aminoacyl-tRNA synthetases form multiple complexes with the potential to fine-tune tRNA aminoacylation.Nucleic acids research · 2022Article
- Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures.Nucleic acids research · 2022Article
- Circadian clock control of tRNA synthetases inF1000Research · 2022Article
- Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator.Molecular oral microbiology · 2021Article
- Rice TSV2 encoding threonyl-tRNA synthetase is needed for early chloroplast development and seedling growth under cold stress.G3 (Bethesda, Md.) · 2021Article
- Article
- Generation and validation of recombinant antibodies to study human aminoacyl-tRNA synthetases.The Journal of biological chemistry · 2020Article
- MHC class I and II peptide homology regulates the cellular immune response.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Mitochondrial aminoacyl-tRNA synthetase disorders: an emerging group of developmental disorders of myelination.Journal of neurodevelopmental disorders · 2019Review
- Pneumonia: host susceptibility and shared genetics with pulmonary function and other traits.Clinical and experimental immunology · 2019Article
- The Tyrosine-Autokinase UbK Is Required for Proper Cell Growth and Cell Morphology ofFrontiers in microbiology · 2019Article
- Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The accurate synthesis of proteins, dictated by the corresponding nucleotide sequence encoded in mRNA, is essential for cell growth and survival. Central to this process are the aminoacyl-tRNA synthetases (aaRSs), which provide amino acid substrates for the growing polypeptide chain in the form of aminoacyl-tRNAs. The aaRSs are essential for coupling the correct amino acid and tRNA molecules, but are also known to associate in higher order complexes with proteins involved in processes beyond translation. Multiprotein complexes containing aaRSs are found in all three domains of life playing roles in splicing, apoptosis, viral assembly, and regulation of transcription and translation. An overview of the complexes aaRSs form in all domains of life is presented, demonstrating the extensive network of connections between the translational machinery and cellular components involved in a myriad of essential processes beyond protein synthesis.
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.