Evidence map›Paper›PMID 32597966›Full record

ArticleNucleic acids research2020

Asymmetric dimerization of adenosine deaminase acting on RNA facilitates substrate recognition.

Alexander S Thuy-Boun, Justin M Thomas, Herra L Grajo, Cody M Palumbo, SeHee Park, Luan T Nguyen, Andrew J Fisher, Peter A Beal

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
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

53 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Review
  3. Evolution of Engineered ADAR-Based RNA Editing Systems.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Phylogenetic and structural analysis of Hydra ADAR.Archives of biochemistry and biophysics · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors at 1 institution in 1 country.

Alexander S Thuy-BounDepartment of Chemistry, University of California, Davis, CA, USA.
Justin M ThomasDepartment of Chemistry, University of California, Davis, CA, USA.
Herra L GrajoDepartment of Chemistry, University of California, Davis, CA, USA.
Cody M PalumboDepartment of Chemistry, University of California, Davis, CA, USA.
SeHee ParkDepartment of Chemistry, University of California, Davis, CA, USA.
Luan T NguyenDepartment of Chemistry, University of California, Davis, CA, USA.
Andrew J FisherDepartment of Chemistry, University of California, Davis, CA, USA.
Peter A BealDepartment of Chemistry, University of California, Davis, CA, USA.
University of California, Davis · US

Funding

The Bioorganic Chemistry Of RNA Editing By ADARSR01GM061115 · NIGMS · UNIVERSITY OF UTAH · PI BEAL, PETER A. · 2001 to 2020
$4.5M
NIGMS NIH HHS R01 GM061115US Department of Energy DE-AC02–76SF00515
6 · The paper itself

Abstract

Adenosine deaminases acting on RNA (ADARs) are enzymes that convert adenosine to inosine in duplex RNA, a modification that exhibits a multitude of effects on RNA structure and function. Recent studies have identified ADAR1 as a potential cancer therapeutic target. ADARs are also important in the development of directed RNA editing therapeutics. A comprehensive understanding of the molecular mechanism of the ADAR reaction will advance efforts to develop ADAR inhibitors and new tools for directed RNA editing. Here we report the X-ray crystal structure of a fragment of human ADAR2 comprising its deaminase domain and double stranded RNA binding domain 2 (dsRBD2) bound to an RNA duplex as an asymmetric homodimer. We identified a highly conserved ADAR dimerization interface and validated the importance of these sequence elements on dimer formation via gel mobility shift assays and size exclusion chromatography. We also show that mutation in the dimerization interface inhibits editing in an RNA substrate-dependent manner for both ADAR1 and ADAR2.

Indexed as

RNA EditingAdenosine DeaminaseCrystallography, X-RayHumansModels, MolecularMutationProtein BindingProtein DomainsProtein MultimerizationRNA-Binding ProteinsRNA, Double-StrandedADARB1 protein, humanAdenosine DeaminaseRNA-Binding ProteinsRNA, Double-Stranded

Identifiers

PMID32597966
PMCPMC7641318
OpenAlexW3037151668

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.