Evidence map›Paper›PMID 24691964›Full record

ReviewCold Spring Harbor perspectives in biology2014

Erasers of histone acetylation: the histone deacetylase enzymes.

Edward Seto, Minoru Yoshida

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,138 papers.

0numbers the graph read from it
0cells of the map it votes in
1,138citing papers in PubMed
–field-weighted citation impact
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

1,138 citing papers in PubMed.

  1. Article
  2. Review
  3. Advances in sirtuin research in lung diseases (Review).International journal of molecular medicine · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Aspirin-Derived Salicyl-CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  11. Article
  12. The histone deacetylase family in health and disease.Signal transduction and targeted therapy · 2026
    Review
  13. Research Progress of Histone Deacetylase and Its Inhibitors in Endometriosis.Reproductive sciences (Thousand Oaks, Calif.) · 2026
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

1,078 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

2 authors.

Edward SetoDepartment of Molecular Oncology, Moffitt Cancer Center and Research Institute, Tampa, Florida 33612.
Minoru Yoshida

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.

Indexed as

ArginaseGene Expression RegulationHistone Deacetylase InhibitorsHistone DeacetylasesHistonesHumansModels, BiologicalProtein Processing, Post-TranslationalProtein Structure, TertiarySaccharomyces cerevisiaeSirtuinsSubstrate SpecificityArginaseHistone Deacetylase InhibitorsHistone DeacetylasesHistonesSirtuins

Identifiers

PMID24691964
PMCPMC3970420

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.