Evidence map›Paper›PMID 26437436›Full record

ReviewBiomolecules2015

New Insights into the Biological Role of Mammalian ADARs; the RNA Editing Proteins.

Niamh Mannion, Fabiana Arieti, Angela Gallo, Liam P Keegan, Mary A O'Connell

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Assembling the RNA therapeutics toolbox.Medical review (2021) · 2024
    Review
  10. Review
  11. Global medical genetics · 2023
    Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The role of RNA editing enzyme ADAR1 in human disease.Wiley interdisciplinary reviews. RNA · 2022
    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

5 authors at 3 institutions in 3 countries.

Niamh MannionPaul O'Gorman Leukaemia Research Centre, Institute of Cancer Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, 21 Shelley Road, Glasgow G12 0ZD, UK. Niamh.Mannion@glasgow.ac.uk.
Fabiana ArietiCEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, Brno 625 00, Czech Republic. fabiana.arieti@ceitec.muni.cz.
Angela GalloOncohaematoogy Department, Ospedale Pediatrico Bambino Gesù (IRCCS) Viale di San Paolo, Roma 15-00146, Italy. pillipo44@yahoo.it.
Liam P KeeganCEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, Brno 625 00, Czech Republic. liam.keegan@ceitec.muni.cz.
Mary A O'ConnellCEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, Brno 625 00, Czech Republic. mary.oconnell@ceitec.muni.cz.
Central European Institute of Technology · CZIstituti di Ricovero e Cura a Carattere Scientifico · ITUniversity of Glasgow · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ADAR proteins deaminate adenosine to inosine in double-stranded RNA which is one of the most abundant modifications present in mammalian RNA. Inosine can have a profound effect on the RNAs that are edited, not only changing the base-pairing properties, but can also result in recoding, as inosine behaves as if it were guanosine. In mammals there are three ADAR proteins and two ADAR-related proteins (ADAD) expressed. All have a very similar modular structure; however, both their expression and biological function differ significantly. Only two of the ADAR proteins have enzymatic activity. However, both ADAR and ADAD proteins possess the ability to bind double-strand RNA. Mutations in ADARs have been associated with many diseases ranging from cancer, innate immunity to neurological disorders. Here, we will discuss in detail the domain structure of mammalian ADARs, the effects of RNA editing, and the role of ADARs in human diseases.

Indexed as

Adenosine DeaminaseAnimalsHumansMammalsRNA-Binding ProteinsRNA, Double-StrandedRNA EditingAdenosine DeaminaseRNA-Binding ProteinsRNA, Double-StrandedADARAlu elementscancerdeaminase domaindsRBDsRNA editing

Identifiers

PMID26437436
PMCPMC4693238
OpenAlexW1790230890

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.