Evidence map›Paper›PMID 30940741›Full record

ReviewEssays in biochemistry2019

Acetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription.

Claire E Barnes, David M English, Shaun M Cowley

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
12.7field-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

137 citing papers in PubMed, 234 citations in OpenAlex.

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  4. Proceedings of the National Academy of Sciences of the United States of America · 2026
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77 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.

Claire E BarnesDepartment of Molecular and Cell Biology, University of Leicester, Leicester, U.K.
David M EnglishDepartment of Molecular and Cell Biology, University of Leicester, Leicester, U.K.
Shaun M CowleyDepartment of Molecular and Cell Biology, University of Leicester, Leicester, U.K. smc57@le.ac.uk.ORCID 0000-0002-2510-1305
University of Leicester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N002954/1Biotechnology and Biological Sciences Research Council BB/P021689/1Medical Research Council MR/J009202/1
6 · The paper itself

Abstract

Packaging the long and fragile genomes of eukaryotic species into nucleosomes is all well and good, but how do cells gain access to the DNA again after it has been bundled away? The solution, in every species from yeast to man, is to post-translationally modify histones, altering their chemical properties to either relax the chromatin, label it for remodelling or make it more compact still. Histones are subject to a myriad of modifications: acetylation, methylation, phosphorylation, ubiquitination etc. This review focuses on histone acylations, a diverse group of modifications which occur on the ε-amino group of Lysine residues and includes the well-characterised Lysine acetylation. Over the last 50 years, histone acetylation has been extensively characterised, with the discovery of histone acetyltransferases (HATs) and histone deacetylases (HDACs), and global mapping experiments, revealing an association of hyperacetylated histones with accessible, transcriptionally active chromatin. More recently, there has been an explosion in the number of unique short chain 'acylations' identified by MS, including: propionylation, butyrylation, crotonylation, succinylation, malonylation and 2-hydroxyisobutyrylation. These novel modifications add a range of chemical environments to histones, and similar to acetylation, appear to accumulate at transcriptional start sites and correlate with gene activity.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsDNAGene Expression RegulationHistonesHumansLysineNucleosomesDNAHistonesLysineNucleosomesAcetylationChromatinHistoneTranscription

Identifiers

PMID30940741
PMCPMC6484784
OpenAlexW2928427498

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.