Evidence map›Paper›PMID 21522130›Full record

ArticleThe EMBO journal2011

The CW domain, a new histone recognition module in chromatin proteins.

Verena Hoppmann, Tage Thorstensen, Per Eugen Kristiansen, Silje Veie Veiseth, Mohummad Aminur Rahman, Kenneth Finne, Reidunn B Aalen, Rein Aasland

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

52 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. NovelFrontiers in medicine · 2026
    Article
  7. Article
  8. Discovery and structural studies of histone demethylases.Frontiers in epigenetics and epigenomics · 2025
    Review
  9. Article
  10. Article
  11. DNA polymerase epsilon binds histone H3.1-H4 and recruits MORC1 to mediate meiotic heterochromatin condensation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Review
  13. Article
  14. The 3' processing of antisense RNAs physically links to chromatin-based transcriptional control.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Genome-Wide Identification of Epigenetic Regulators inInternational journal of molecular sciences · 2020
    Article
  16. Article
  17. The function of histone lysine methylation related SET domain group proteins in plants.Protein science : a publication of the Protein Society · 2020
    Review
  18. Article
  19. Frontiers in plant science · 2020
    Article
  20. Article
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

8 authors at 2 institutions in 1 country.

Verena HoppmannDepartment of Molecular Biology, University of Bergen, Bergen, Norway.
Tage Thorstensen
Per Eugen Kristiansen
Silje Veie Veiseth
Mohummad Aminur Rahman
Kenneth Finne
Reidunn B Aalen
Rein Aasland
University of Oslo · NOUniversity of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications of the N-terminal histone tails, including lysine methylation, have key roles in regulation of chromatin and gene expression. A number of protein modules have been identified that recognize differentially modified histone tails and provide their proteins with the capacity to sense such modifications. Here, we identify the CW domain of plant and animal chromatin-related proteins as a novel module that recognizes different methylated states of lysine 4 on histone H3 (H3K4me). The solution structure of the CW domain of the Arabidopsis ASH1 HOMOLOG2 (ASHH2) histone methyltransferase provides insight into how different CW domains can distinguish different methylated histone tails. We provide evidence that ASHH2 is acting on H3K4me-marked genes, allowing for ASHH2-dependent H3K36 tri-methylation, which contributes to sustained expression of tissue-specific and developmentally regulated genes. This suggests that ASHH2 is a combined 'reader' and 'writer' of the histone code. We propose that different CW domains, dependent on their specificity for different H3K4 methylations, are important for epigenetic memory or participate in switching between permissive and repressive chromatin states.

Indexed as

Protein Interaction Domains and MotifsArabidopsisGene Expression ProfilingGene Expression RegulationHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesMethylationModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction MappingProtein Structure, TertiarySurface Plasmon ResonanceHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistones

Identifiers

PMID21522130
PMCPMC3098480
OpenAlexW2109844363

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.