Evidence map›Paper›PMID 39165563›Full record

ReviewMolecular therapy. Nucleic acids2024

Structural perspectives on adenosine to inosine RNA editing by ADARs.

Andrew J Fisher, Peter A Beal

Abstract readReview
In one paragraph

Review in Molecular therapy. Nucleic acids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. RNA modifications in cancer and their detection: a review.Japanese journal of clinical oncology · 2026
    Review
  7. Review
  8. Clickable RNA via 4'-Bioconjugate chemistry · 2025
    Article
  9. Article
  10. ZYS-1 is not an ADAR1 inhibitor.RNA (New York, N.Y.) · 2025
    Article
  11. Article
  12. Article
  13. Phylogenetic and structural analysis of Hydra ADAR.Archives of biochemistry and biophysics · 2025
    Article
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Andrew J FisherDepartment of Chemistry, University of California, Davis, One Shields Ave, Davis, CA 95616, USA.
Peter A BealDepartment of Chemistry, University of California, Davis, One Shields Ave, Davis, CA 95616, USA.

Funding

Supplement: Defining and Controlling Protein-RNA interactions in editing and interference pathwaysR35GM141907 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI PETER A. BEAL · 2021 to 2026
$3.2M
Supplement:High-throughput screening and structure-guided optimization of oligonucleotides for site-directed RNA editing by ADARsR01GM149799 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ANDREW J FISHER · 2023 to 2026
$1.4M
NIGMS NIH HHS R01 GM149799NIGMS NIH HHS R35 GM141907
6 · The paper itself

Abstract

Adenosine deaminases acting on RNA (ADARs) are enzymes that catalyze the hydrolytic deamination of adenosine to inosine. The editing feature of ADARs has garnered much attention as a therapeutic tool to repurpose ADARs to correct disease-causing mutations at the mRNA level in a technique called site-directed RNA editing (SDRE). Administering a short guide RNA oligonucleotide that hybridizes to a mutant sequence forms the requisite dsRNA substrate, directing ADARs to edit the desired adenosine. However, much is still unknown about ADARs' selectivity and sequence-specific effects on editing. Atomic-resolution structures can help provide additional insight to ADARs' selectivity and lead to novel guide RNA designs. Indeed, recent structures of ADAR domains have expanded our understanding on RNA binding and the base-flipping catalytic mechanism. These efforts have enabled the rational design of improved ADAR guide strands and advanced the therapeutic potential of the SDRE approach. While no full-length structure of any ADAR is known, this review presents an exposition of the structural basis for function of the different ADAR domains, focusing on human ADAR2. Key insights are extrapolated to human ADAR1, which is of substantial interest because of its widespread expression in most human tissues.

Indexed as

ADARadenosineadenosine deaminase acting on RNAinosineMT: RNA and epigenetic editing Special Issuenucleic acid therapeuticsSDREsite-directed RNA editing

Identifiers

PMID39165563
PMCPMC11334849

What OpenQuestion holds

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Registered trials

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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.