ArticleNature structural & molecular biology2016
Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 162 papers.
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Who cites it
162 citing papers in PubMed, 229 citations in OpenAlex.
- Targeting ADAR1 in Cancer: Biology, Therapeutic Strategies, Challenges, and Limitations.Pharmaceuticals (Basel, Switzerland) · 2026Review
- ADAR-mediated RNA editing in CNS disorders: from pathogenic mechanisms to therapeutic opportunities.Cellular & molecular biology letters · 2026Review
- Sensing and perturbing mammalian cell states with reprogrammable ADAR sensors (RADARS).Nature protocols · 2026Review
- Base Editors for Engineering Industrial Microorganisms: Types, Applications, and Future Perspectives.Biotechnology journal · 2026Review
- Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins.Nature communications · 2026Article
- Review
- Inducible, split base editors for in vivo cancer functional genomics.Nature biotechnology · 2026Article
- Structural and mechanistic basis of ADAR1-mediated RNA editing and immune regulation.Cell insight · 2026Review
- Improved RNA base editing with guide RNAs mimicking highly edited endogenous ADAR substrates.Nature biotechnology · 2026Article
- Target-stabilized base editors enable robust high-fidelity RNA editing.Nature communications · 2026Article
- Identification of ADAR1i-124: The first effective A-to-I RNA editing inhibitor with promising cancer therapeutic potential.iScience · 2026Article
- Evolution of Engineered ADAR-Based RNA Editing Systems.International journal of molecular sciences · 2026Review
- Specific and efficient RNA A-to-I editing through cleavage of an ADAR inhibitor.Nature biotechnology · 2026Article
- Engineered Allosteric RNA Editors Enable Compact, Stimulus-Responsive Post-Transcriptional Circuits.bioRxiv : the preprint server for biology · 2026Article
- ADAR-GPT: A continually fine-tuned language model for predicting A-to-I RNA editing sites.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Single-strand deaminase-assisted editing for functional RNA manipulation.Nature biotechnology · 2026Article
- Synthesis of 2'-O,4'-Cα-Dimethyl Ribonucleoside Analogs and Their Effects on RNA and Modulation of ADAR Editing.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Clickable RNA via 4'-Bioconjugate chemistry · 2025Article
- Discovery and Tuning of RNA Editing Guides via High-Throughput Screening and Chemical Modification.Chembiochem : a European journal of chemical biology · 2025Article
- Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.Current issues in molecular biology · 2025Review
102 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Adenosine deaminases acting on RNA (ADARs) are editing enzymes that convert adenosine to inosine in duplex RNA, a modification reaction with wide-ranging consequences in RNA function. Understanding of the ADAR reaction mechanism, the origin of editing-site selectivity, and the effect of mutations is limited by the lack of high-resolution structural data for complexes of ADARs bound to substrate RNAs. Here we describe four crystal structures of the human ADAR2 deaminase domain bound to RNA duplexes bearing a mimic of the deamination reaction intermediate. These structures, together with structure-guided mutagenesis and RNA-modification experiments, explain the basis of the ADAR deaminase domain's dsRNA specificity, its base-flipping mechanism, and its nearest-neighbor preferences. In addition, we identified an ADAR2-specific RNA-binding loop near the enzyme active site, thus rationalizing differences in selectivity observed between different ADARs. Finally, our results provide a structural framework for understanding the effects of ADAR mutations associated with human disease.
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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.