ArticleNature communications2020
High-throughput mutagenesis reveals unique structural features of human ADAR1.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 24 citations in OpenAlex.
- Inducible, split base editors for in vivo cancer functional genomics.Nature biotechnology · 2026Article
- Target-stabilized base editors enable robust high-fidelity RNA editing.Nature communications · 2026Article
- In Silico Characterization of ADAR1: Structure, Dynamics, and Functional Implications.Current issues in molecular biology · 2025Article
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- High-speed atomic force microscopy and 3D modeling reveal the structural dynamics of ADAR1 complexes.Nature communications · 2025Article
- An engineered U7 small nuclear RNA scaffold greatly increases ADAR-mediated programmable RNA base editing.Nature communications · 2025Article
- Phylogenetic and structural analysis of Hydra ADAR.Archives of biochemistry and biophysics · 2025Article
- Biochemical profiling and structural basis of ADAR1-mediated RNA editing.Molecular cell · 2025Article
- Targeting ADAR1 with a small molecule for the treatment of prostate cancer.Nature cancer · 2025Article
- Databases of ligand-binding pockets and protein-ligand interactions.Computational and structural biotechnology journal · 2024Review
- Rational design of base, sugar and backbone modifications improves ADAR-mediated RNA editing.Nucleic acids research · 2024Article
- Structural perspectives on adenosine to inosine RNA editing by ADARs.Molecular therapy. Nucleic acids · 2024Review
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- Impact of Disease-Associated Mutations on the Deaminase Activity of ADAR1.Biochemistry · 2024Article
- Engineered deaminases as a key component of DNA and RNA editing tools.Molecular therapy. Nucleic acids · 2023Review
- Chemical Modifications in RNA: Elucidating the Chemistry of dsRNA-Specific Adenosine Deaminases (ADARs).Accounts of chemical research · 2023Article
- RNA editing: Expanding the potential of RNA therapeutics.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Review
- Selective Inhibition of ADAR1 Using 8-Azanebularine-Modified RNA Duplexes.Biochemistry · 2023Article
- Site-directed RNA editing by harnessing ADARs: advances and challenges.Functional & integrative genomics · 2022Review
- Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position.Journal of the American Chemical Society · 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
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Adenosine Deaminases that act on RNA (ADARs) are enzymes that catalyze adenosine to inosine conversion in dsRNA, a common form of RNA editing. Mutations in the human ADAR1 gene are known to cause disease and recent studies have identified ADAR1 as a potential therapeutic target for a subset of cancers. However, efforts to define the mechanistic effects for disease associated ADAR1 mutations and the rational design of ADAR1 inhibitors are limited by a lack of structural information. Here, we describe the combination of high throughput mutagenesis screening studies, biochemical characterization and Rosetta-based structure modeling to identify unique features of ADAR1. Importantly, these studies reveal a previously unknown zinc-binding site on the surface of the ADAR1 deaminase domain which is important for ADAR1 editing activity. Furthermore, we present structural models that explain known properties of this enzyme and make predictions about the role of specific residues in a surface loop unique to ADAR1.
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.