ReviewFEBS letters2010
The balance between pre- and post-transfer editing in tRNA synthetases.
Review in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed.
- Different chemical scaffolds bind to L-phe site in Mycobacterium tuberculosis Phe-tRNA synthetase.European journal of medicinal chemistry · 2025Article
- New antibacterial candidates against Acinetobacter baumannii discovered by in silico-driven chemogenomics repurposing.PloS one · 2024Article
- Genome-wide screening reveals metabolic regulation of stop-codon readthrough by cyclic AMP.Nucleic acids research · 2023Article
- System-wide optimization of an orthogonal translation system with enhanced biological tolerance.Molecular systems biology · 2023Article
- A standalone editing protein deacylates mischarged canavanyl-tRNAArg to prevent canavanine incorporation into proteins.Nucleic acids research · 2023Article
- Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy.Nucleic acids research · 2021Article
- The uniqueness of AlaRS and its human disease connections.RNA biology · 2021Review
- Impact of alanyl-tRNA synthetase editing deficiency in yeast.Nucleic acids research · 2021Article
- Reciprocally-Coupled Gating: Strange Loops in Bioenergetics, Genetics, and Catalysis.Biomolecules · 2021Review
- The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases.Scientific reports · 2020Article
- Cross-editing by a tRNA synthetase allows vertebrates to abundantly express mischargeable tRNA without causing mistranslation.Nucleic acids research · 2020Article
- Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions.The Journal of biological chemistry · 2020Article
- Glutaminyl-tRNA Synthetase from Pseudomonas aeruginosa: Characterization, structure, and development as a screening platform.Protein science : a publication of the Protein Society · 2020Article
- MRNA Transcription, Translation, and Defects in Developmental Cognitive and Behavioral Disorders.Frontiers in molecular biosciences · 2020Review
- Deciphering the interaction of benzoxaborole inhibitor AN2690 with connective polypeptide 1 (CP1) editing domain ofJournal of biosciences · 2020Article
- Oxidation of phenylalanyl-tRNA synthetase positively regulates translational quality control.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Backbone Brackets and Arginine Tweezers delineate Class I and Class II aminoacyl tRNA synthetases.PLoS computational biology · 2018Article
- A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.Nature communications · 2018Article
- Kinetic analysis of the isoleucyl-tRNA synthetase mechanism: the next reaction cycle can start before the previous one ends.FEBS open bio · 2018Article
- Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid.Nature communications · 2017Article
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.
Funding
Abstract
The fidelity of tRNA aminoacylation is dependent in part on amino acid editing mechanisms. A hydrolytic activity that clears mischarged tRNAs typically resides in an active site on the tRNA synthetase that is distinct from its synthetic aminoacylation active site. A second pre-transfer editing pathway that hydrolyzes the tRNA synthetase aminoacyl adenylate intermediate can also be activated. Pre- and post-transfer editing activities can co-exist within a single tRNA synthetase resulting in a redundancy of fidelity mechanisms. However, in most cases one pathway appears to dominate, but when compromised, the secondary pathway can be activated to suppress tRNA synthetase infidelities.
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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.