Evidence map›Paper›PMID 11604520›Full record

ArticleMolecular and cellular biology2001

CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain.

H Poulsen, J Nilsson, C K Damgaard, J Egebjerg, J Kjems

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

110 citing papers in PubMed, 175 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026
    Review
  9. Evolution of Engineered ADAR-Based RNA Editing Systems.International journal of molecular sciences · 2026
    Review
  10. Article
  11. Review
  12. ncRNA Editing: Functional Characterization and Computational Resources.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024
    Review
  19. Article
  20. Article

50 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

5 authors at 1 institution in 1 country.

H PoulsenDepartment of Molecular and Structural Biology, University of Aarhus, Denmark.
J Nilsson
C K Damgaard
J Egebjerg
J Kjems
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA editing of specific residues by adenosine deamination is a nuclear process catalyzed by adenosine deaminases acting on RNA (ADAR). Different promoters in the ADAR1 gene give rise to two forms of the protein: a constitutive promoter expresses a transcript encoding (c)ADAR1, and an interferon-induced promoter expresses a transcript encoding an N-terminally extended form, (i)ADAR1. Here we show that (c)ADAR1 is primarily nuclear whereas (i)ADAR1 encompasses a functional nuclear export signal in the N-terminal part and is a nucleocytoplasmic shuttle protein. Mutation of the nuclear export signal or treatment with the CRM1-specific drug leptomycin B induces nuclear accumulation of (i)ADAR1 fused to the green fluorescent protein and increases the nuclear editing activity. In concurrence, CRM1 and RanGTP interact specifically with the (i)ADAR1 nuclear export signal to form a tripartite export complex in vitro. Furthermore, our data imply that nuclear import of (i)ADAR1 is mediated by at least two nuclear localization sequences. These results suggest that the nuclear editing activity of (i)ADAR1 is modulated by nuclear export.

Indexed as

Receptors, Cytoplasmic and NuclearActive Transport, Cell NucleusAdenosine DeaminaseAnimalsBinding SitesCell NucleusConserved SequenceCytoplasmDNADNA-Binding ProteinsExportin 1 ProteinFatty Acids, UnsaturatedHumansKaryopherinsMiceNuclear Localization SignalsADARB1 protein, humanAdenosine DeaminaseDNADNA-Binding ProteinsExportin 1 ProteinFatty Acids, UnsaturatedKaryopherinsleptomycin BNuclear Localization Signalsran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRNA-Binding Proteins

Identifiers

PMID11604520
PMCPMC99958
OpenAlexW2132002570

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.