Evidence map›Paper›PMID 29457714›Full record

ArticleBiochemistry2018

Selective Recognition of RNA Substrates by ADAR Deaminase Domains.

Yuru Wang, SeHee Park, Peter A Beal

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

44 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Evolution of Engineered ADAR-Based RNA Editing Systems.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Phylogenetic and structural analysis of Hydra ADAR.Archives of biochemistry and biophysics · 2025
    Article
  10. Article
  11. Article
  12. ncRNA Editing: Functional Characterization and Computational Resources.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Article
  14. Review
  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

3 authors at 1 institution in 1 country.

Yuru WangDepartment of Chemistry , University of California , One Shields Ave , Davis , California 95616 , United States.
SeHee ParkDepartment of Chemistry , University of California , One Shields Ave , Davis , California 95616 , United States.
Peter A BealDepartment of Chemistry , University of California , One Shields Ave , Davis , California 95616 , United States.ORCID 0000-0003-4855-7185
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
The Bioorganic Chemistry Of RNA Editing By ADARSR01GM061115 · NIGMS · UNIVERSITY OF UTAH · PI BEAL, PETER A. · 2001 to 2020
$4.5M
UC Davis Shared Astrios Cell SorterS10OD018223 · OD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SHACKLETT, BARBARA L. · 2015 to 2015
$555k
NCI NIH HHS P30 CA093373NIGMS NIH HHS R01 GM061115NIH HHS S10 OD018223
6 · The paper itself

Abstract

Adenosine deamination is one of the most prevalent post-transcriptional modifications in mRNA and is catalyzed by ADAR1 and ADAR2 in humans. ADAR1 and ADAR2 have different substrate selectivity, which is believed to mainly originate from the proteins' deaminase domains (hADAR1d and hADAR2d, respectively). RNA-seq of the Saccharomyces cerevisiae transcriptome subjected to ADAR-catalyzed RNA editing identified substrates with common secondary structure features preferentially edited by hADAR1d over hADAR2d. The relatively small size and efficient reaction of one of these substrates suggested it could be useful for further study of the hADAR1d reaction. Indeed, a short hairpin stem from the S. cerevisiae HER1 mRNA was efficiently deaminated by hADAR1d and used to generate an hADAR1d-specific fluorescent reporter of editing activity. Using substrates preferred by either hADAR1d or hADAR2d in vitro, we found that a chimeric protein bearing an RNA-binding loop from hADAR2d grafted onto hADAR1d showed ADAR2-like selectivity. Finally, a high-throughput mutagenesis analysis (Sat-FACS-Seq) of conserved residues in an RNA-binding loop of hADAR1d revealed essential amino acids for function, advancing our understanding of RNA recognition by this domain.

Indexed as

Protein DomainsAdenosine DeaminaseBase SequenceGenes, ReporterGreen Fluorescent ProteinsHigh-Throughput Screening AssaysHumansProtein Processing, Post-TranslationalRNARNA-Binding ProteinsSequence Analysis, RNASubstrate SpecificityADARB1 protein, humanADAR protein, humanAdenosine Deaminaseenhanced green fluorescent proteinGreen Fluorescent ProteinsRNARNA-Binding Proteins

Identifiers

PMID29457714
PMCPMC5898644
OpenAlexW2788015265

What OpenQuestion holds

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LicenceTDM
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.