Evidence map›Paper›PMID 12429021›Full record

ReviewThe Biochemical journal2003

Histone deacetylases (HDACs): characterization of the classical HDAC family.

Annemieke J M de Ruijter, Albert H van Gennip, Huib N Caron, Stephan Kemp, André B P van Kuilenburg

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,270 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
1,270citing papers in PubMed, 1 pooled it
38.3field-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

1,270 citing papers in PubMed, 1 synthesis or guideline pooled it, 3,077 citations in OpenAlex.

  1. Pooled it
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  6. Toxoplasma gondii SIR2A Promotes Tachyzoite Invasion via Lysine Deacetylase Activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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1,210 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 2 institutions in 1 country.

Annemieke J M de RuijterAcademic Medical Centre, University of Amsterdam, Amsterdam, The, Netherlands.
Albert H van Gennip
Huib N Caron
Stephan Kemp
André B P van Kuilenburg
University of Amsterdam · NLEmma Kinderziekenhuis · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptional regulation in eukaryotes occurs within a chromatin setting, and is strongly influenced by the post-translational modification of histones, the building blocks of chromatin, such as methylation, phosphorylation and acetylation. Acetylation is probably the best understood of these modifications: hyperacetylation leads to an increase in the expression of particular genes, and hypoacetylation has the opposite effect. Many studies have identified several large, multisubunit enzyme complexes that are responsible for the targeted deacetylation of histones. The aim of this review is to give a comprehensive overview of the structure, function and tissue distribution of members of the classical histone deacetylase (HDAC) family, in order to gain insight into the regulation of gene expression through HDAC activity. SAGE (serial analysis of gene expression) data show that HDACs are generally expressed in almost all tissues investigated. Surprisingly, no major differences were observed between the expression pattern in normal and malignant tissues. However, significant variation in HDAC expression was observed within tissue types. HDAC inhibitors have been shown to induce specific changes in gene expression and to influence a variety of other processes, including growth arrest, differentiation, cytotoxicity and induction of apoptosis. This challenging field has generated many fascinating results which will ultimately lead to a better understanding of the mechanism of gene transcription as a whole.

Indexed as

Transcription, GeneticAcetylationEvolution, MolecularGene Expression RegulationHistone DeacetylasesHistonesHumansIsoenzymesModels, GeneticMolecular StructureNeoplasmsRepressor ProteinsSignal TransductionTissue DistributionHistone DeacetylasesHistonesIsoenzymesRepressor Proteins

Identifiers

PMID12429021
PMCPMC1223209
OpenAlexW2107733280

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.