Evidence map›Paper›PMID 32203492›Full record

ArticleNature structural & molecular biology2020

irCLASH reveals RNA substrates recognized by human ADARs.

Yulong Song, Wenbing Yang, Qiang Fu, Liang Wu, Xueni Zhao, Yusen Zhang, Rui Zhang

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  8. Review
  9. Article
  10. ADAR-GPT: A continually fine-tuned language model for predicting A-to-I RNA editing sites.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. An ADAR2-mimic base editor for efficient C-to-U RNA editing in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Article
  15. ADAR1: from basic mechanisms to inhibitors.Trends in cell biology · 2025
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  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 2 institutions in 2 countries.

Yulong Song *MOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China.
Wenbing Yang *MOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China.
Qiang FuMOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China.
Liang WuDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN, USA.
Xueni ZhaoMOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China.
Yusen ZhangMOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China.
Rui ZhangMOE Key Laboratory of Gene Function and Regulation, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, P. R. China. zhangrui3@mail.sysu.edu.cn.ORCID http://orcid.org/0000-0001-9000-5021
Sun Yat-sen University · CNMayo Clinic in Arizona · US

Funding

NCI NIH HHS HHSN261200800001ENHLBI NIH HHS HHSN268201000029C
6 · The paper itself

Abstract

Adenosine deaminases acting on RNA (ADARs) convert adenosines to inosines in double-stranded RNA (dsRNA) in animals. Despite their importance, ADAR RNA substrates have not been mapped extensively in vivo. Here we develop irCLASH to map RNA substrates recognized by human ADARs and uncover features that determine their binding affinity and editing efficiency. We also observe a dominance of long-range interactions within ADAR substrates and analyze differences between ADAR1 and ADAR2 editing substrates. Moreover, we unexpectedly discovered that ADAR proteins bind dsRNA substrates tandemly in vivo, each with a 50-bp footprint. Using RNA duplexes recognized by ADARs as readout of pre-messenger RNA structures, we reveal distinct higher-order architectures between pre-messenger RNAs and mRNAs. Our transcriptome-wide atlas of ADAR substrates and the features governing RNA editing observed in our study will assist in the rational design of guide RNAs for ADAR-mediated RNA base editing.

Indexed as

AdenosineAdenosine DeaminaseAnimalsHumansInosineNucleic Acid ConformationRNA-Binding ProteinsRNA, Double-StrandedRNA EditingRNA, MessengerTranscriptomeADARB1 protein, humanADAR protein, humanAdenosineAdenosine DeaminaseInosineRNA-Binding ProteinsRNA, Double-StrandedRNA, Messenger

Identifiers

PMID32203492
OpenAlexW3012857753

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.