ArticleRNA (New York, N.Y.)2019
tRNA deamination by ADAT requires substrate-specific recognition mechanisms and can be inhibited by tRFs.
Article in RNA (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed, 21 citations in OpenAlex.
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- RNA modifications, alternative splicing and circular RNA landscape in the mouse brain: inosine and beyond.Scientific reports · 2025Article
- ADAT3 variants disrupt the activity of the ADAT tRNA deaminase complex and impair neuronal migration.Brain : a journal of neurology · 2025Article
- Unveiling the A-to-I mRNA editing machinery and its regulation and evolution in fungi.Nature communications · 2024Article
- Codon decoding by orthogonal tRNAs interrogates theFrontiers in genetics · 2024Article
- Article
- The occurrence, characteristics, and adaptation of A-to-I RNA editing in bacteria: A review.Frontiers in microbiology · 2023Review
- The structure of the mouse ADAT2/ADAT3 complex reveals the molecular basis for mammalian tRNA wobble adenosine-to-inosine deamination.Nucleic acids research · 2021Article
- tRNA-derived fragments (tRFs): establishing their turf in post-transcriptional gene regulation.Cellular and molecular life sciences : CMLS · 2021Review
- tRNA-Derived Fragment tRF-Glu-TTC-027 Regulates the Progression of Gastric CarcinomaFrontiers in oncology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenosine deaminase acting on transfer RNA (ADAT) is an essential eukaryotic enzyme that catalyzes the deamination of adenosine to inosine at the first position of tRNA anticodons. Mammalian ADATs modify eight different tRNAs, having increased their substrate range from a bacterial ancestor that likely deaminated exclusively tRNA
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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.