Evidence map›Paper›PMID 14612560›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Modulation of RNA editing by functional nucleolar sequestration of ADAR2.

Christopher L Sansam, K Sam Wells, Ronald B Emeson

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
3.6field-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

109 citing papers in PubMed, 189 citations in OpenAlex.

  1. Article
  2. Evolution of Engineered ADAR-Based RNA Editing Systems.International journal of molecular sciences · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. ncRNA Editing: Functional Characterization and Computational Resources.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Review
  8. Article
  9. ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. ADAR1 Isoforms RegulateInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Review
  18. Deciphering the Biological Significance of ADAR1-Z-RNA Interactions.International journal of molecular sciences · 2021
    Review
  19. Article
  20. Biallelic variants inJournal of medical genetics · 2021
    Article

49 more citing papers are in PubMed but not listed here.

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.

Christopher L SansamDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
K Sam Wells
Ronald B Emeson
Vanderbilt University · US

Funding

REGULATION OF RNA EDITING IN THE CNSR01NS033323 · NINDS · VANDERBILT UNIVERSITY · PI EMESON, RONALD B. · 1995 to 2010
$2.5M
NINDS NIH HHS NS33323NINDS NIH HHS R01 NS033323
6 · The paper itself

Abstract

The adenosine deaminases that act on RNA (ADARs) catalyze the site-specific conversion of adenosine to inosine (A to I) in primary mRNA transcripts, thereby affecting the splicing pattern or coding potential of mature mRNAs. Although the subnuclear localization of A-to-I editing has not been precisely defined, ADARs have been shown to act before splicing, suggesting that they function near nucleoplasmic sites of transcription. Here we demonstrate that ADAR2, a member of the vertebrate ADAR family, is concentrated in the nucleolus, a subnuclear domain disparate from the sites of mRNA transcription. Selective inhibition of ribosomal RNA synthesis or the introduction of mutations in the double-stranded RNA-binding domains within ADAR2 results in translocation of the protein to the nucleoplasm, suggesting that nucleolar association of ADAR2 depends on its ability to bind to ribosomal RNA. Fluorescence recovery after photobleaching reveals that ADAR2 can shuttle rapidly between subnuclear compartments. Enhanced translocation of endogenous ADAR2 from the nucleolus to the nucleoplasm results in increased editing of endogenous ADAR2 substrates. These observations indicate that the nucleolar localization of ADAR2 represents an important mechanism by which RNA editing can be modulated by the sequestration of enzymatic activity from potential RNA substrates in the nucleoplasm.

Indexed as

RNA EditingAdenosine DeaminaseAmino Acid SequenceAnimalsBase SequenceCell LineCell NucleolusIn Vitro TechniquesMiceMolecular Sequence DataNIH 3T3 CellsRatsRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, Double-StrandedRNA PrecursorsADARB1 protein, humanAdenosine DeaminaseRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, Double-StrandedRNA PrecursorsRNA, Ribosomal

Identifiers

PMID14612560
PMCPMC283538
OpenAlexW2043724929

What OpenQuestion holds

Textmetadata
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.