Evidence map›Paper›PMID 31552420›Full record

ArticleNucleic acids research2019

RNA binding candidates for human ADAR3 from substrates of a gain of function mutant expressed in neuronal cells.

Yuru Wang, Dong Hee Chung, Leanna R Monteleone, Jie Li, Yao Chiang, Michael D Toney, Peter A Beal

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024
    Review
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 1 institution in 1 country.

Yuru WangDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Dong Hee ChungDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Leanna R MonteleoneDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Jie LiDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Yao ChiangDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Michael D ToneyDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, USA.
Peter A BealDepartment of Chemistry, University of California, One Shields Ave, Davis, CA 95616, 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 GM061115
6 · The paper itself

Abstract

Human ADAR3 is a catalytically inactive member of the Adenosine Deaminase Acting on RNA (ADAR) protein family, whose active members catalyze A-to-I RNA editing in metazoans. Until now, the reasons for the catalytic incapability of ADAR3 has not been defined and its biological function rarely explored. Yet, its exclusive expression in the brain and involvement in learning and memory suggest a central role in the nervous system. Here we describe the engineering of a catalytically active ADAR3 enzyme using a combination of computational design and functional screening. Five mutations (A389V, V485I, E527Q, Q549R and Q733D) engender RNA deaminase in human ADAR3. By way of its catalytic activity, the ADAR3 pentamutant was used to identify potential binding targets for wild type ADAR3 in a human glioblastoma cell line. Novel ADAR3 binding sites discovered in this manner include the 3'-UTRs of the mRNAs encoding early growth response 1 (EGR1) and dual specificity phosphatase 1 (DUSP1); both known to be activity-dependent immediate early genes that respond to stimuli in the brain. Further studies reveal that the wild type ADAR3 protein can regulate transcript levels for DUSP1 and EGR1, suggesting a novel role ADAR3 may play in brain function.

Indexed as

Adenosine DeaminaseBase SequenceCell Line, TumorDual Specificity Phosphatase 1Early Growth Response Protein 1Gain of Function MutationGene Expression RegulationHumansNeuronsProtein BindingProtein DomainsRNARNA-Binding ProteinsRNA, MessengerSubstrate SpecificityADARB1 protein, humanADARB2 protein, humanAdenosine DeaminaseDual Specificity Phosphatase 1DUSP1 protein, humanEarly Growth Response Protein 1EGR1 protein, humanRNARNA-Binding ProteinsRNA, Messenger

Identifiers

PMID31552420
PMCPMC6846710
OpenAlexW2975902559

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.