ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2017
How do ADARs bind RNA? New protein-RNA structures illuminate substrate recognition by the RNA editing ADARs.
Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 65 citations in OpenAlex.
- Structural and mechanistic basis of ADAR1-mediated RNA editing and immune regulation.Cell insight · 2026Review
- Target-stabilized base editors enable robust high-fidelity RNA editing.Nature communications · 2026Article
- Evaluation of novel computational methods to identify RNA-binding protein footprints from structural data.RNA (New York, N.Y.) · 2025Article
- An engineered U7 small nuclear RNA scaffold greatly increases ADAR-mediated programmable RNA base editing.Nature communications · 2025Article
- Programming ADAR-recruiting hairpin RNA sensor to detect endogenous molecules.Nucleic acids research · 2025Article
- Article
- Exploring functional conservation in silico: a new machine learning approach to RNA-editing.Briefings in bioinformatics · 2024Article
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- Adenosine deaminases that act on RNA, then and now.RNA (New York, N.Y.) · 2024Article
- RNA sequences that direct selective ADAR editing from a SELEX library bearing 8-azanebularine.Bioorganic & medicinal chemistry · 2024Article
- RNA editing enzymes: structure, biological functions and applications.Cell & bioscience · 2024Review
- Recommendations for detection, validation, and evaluation of RNA editing events in cardiovascular and neurological/neurodegenerative diseases.Molecular therapy. Nucleic acids · 2024Review
- RNA molecular recording with an engineered RNA deaminase.Nature methods · 2023Article
- A-to-I RNA editing by ADAR and its therapeutic applications: From viral infections to cancer immunotherapy.Wiley interdisciplinary reviews. RNA · 2023Review
- The RNA-binding protein Adad1 is necessary for germ cell maintenance and meiosis in zebrafish.PLoS genetics · 2023Article
- Epigenetic regulation in the tumor microenvironment: molecular mechanisms and therapeutic targets.Signal transduction and targeted therapy · 2023Review
- Selective Inhibition of ADAR1 Using 8-Azanebularine-Modified RNA Duplexes.Biochemistry · 2023Article
- Flipped over U: structural basis for dsRNA cleavage by the SARS-CoV-2 endoribonuclease.Nucleic acids research · 2022Article
- Flipped Over U: Structural Basis for dsRNA Cleavage by the SARS-CoV-2 Endoribonuclease.bioRxiv : the preprint server for biology · 2022Article
- ADAR1-Mediated RNA Editing and Its Role in Cancer.Frontiers in cell and developmental biology · 2022Review
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
Deamination of adenosine in RNA to form inosine has wide ranging consequences on RNA function including amino acid substitution to give proteins not encoded in the genome. What determines which adenosines in an mRNA are subject to this modification reaction? The answer lies in an understanding of the mechanism and substrate recognition properties of adenosine deaminases that act on RNA (ADARs). Our recent publication of X-ray crystal structures of the human ADAR2 deaminase domain bound to RNA editing substrates shed considerable light on how the catalytic domains of these enzymes bind RNA and promote adenosine deamination. Here we review in detail the deaminase domain-RNA contact surfaces and present models of how full length ADARs, bearing double stranded RNA-binding domains (dsRBDs) and deaminase domains, could process naturally occurring substrate RNAs.
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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.