ArticleCell2010
The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove.
Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.
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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
148 citing papers in PubMed.
- Structural basis for recognition of diverse localizing mRNAs by Egl-BicD.Nature structural & molecular biology · 2026Article
- Structural and mechanistic basis of ADAR1-mediated RNA editing and immune regulation.Cell insight · 2026Review
- Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026Review
- Structural basis of double-stranded RNA recognition by the J2 monoclonal antibody.Nature communications · 2025Article
- Systematic characterization of the composition and dynamics of processing body-associated mRNAs.Nature communications · 2025Article
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- Stereo-random oligonucleotides enable efficient recruitment of ADAR in vitro and in vivo.Nature communications · 2025Article
- ADARs: pleiotropy in function, versatility in application.Nucleic acids research · 2025Review
- Computer-Aided Discovery of Natural Compounds Targeting the ADAR2 dsRBD2-RNA Interface and Computational Modeling of Full-Length ADAR2 Protein Structure.International journal of molecular sciences · 2025Article
- Biochemical profiling and structural basis of ADAR1-mediated RNA editing.Molecular cell · 2025Article
- Precise in vivo RNA base editing with a wobble-enhanced circular CLUSTER guide RNA.Nature biotechnology · 2025Article
- RNA editing in disease: mechanisms and therapeutic potential.RNA (New York, N.Y.) · 2025Review
- RNAproDB: A Webserver and Interactive Database for Analyzing Protein-RNA Interactions.Journal of molecular biology · 2025Article
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
- Structural perspectives on adenosine to inosine RNA editing by ADARs.Molecular therapy. Nucleic acids · 2024Review
- Article
- 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
- Dissecting the basis for differential substrate specificity of ADAR1 and ADAR2.Nature communications · 2023Article
- Precision RNA base editing with engineered and endogenous effectors.Nature biotechnology · 2023Review
88 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Sequence-dependent recognition of dsDNA-binding proteins is well understood, yet sequence-specific recognition of dsRNA by proteins remains largely unknown, despite their importance in RNA maturation pathways. Adenosine deaminases that act on RNA (ADARs) recode genomic information by the site-selective deamination of adenosine. Here, we report the solution structure of the ADAR2 double-stranded RNA-binding motifs (dsRBMs) bound to a stem-loop pre-mRNA encoding the R/G editing site of GluR-2. The structure provides a molecular basis for how dsRBMs recognize the shape, and also more surprisingly, the sequence of the dsRNA. The unexpected direct readout of the RNA primary sequence by dsRBMs is achieved via the minor groove of the dsRNA and this recognition is critical for both editing and binding affinity at the R/G site of GluR-2. More generally, our findings suggest a solution to the sequence-specific paradox faced by many dsRBM-containing proteins that are involved in post-transcriptional regulation of gene expression.
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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.