Evidence map›Paper›PMID 24631868›Full record

ReviewBiochimica et biophysica acta2014

Interpreting the language of histone and DNA modifications.

Scott B Rothbart, Brian D Strahl

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 365 papers.

0numbers the graph read from it
0cells of the map it votes in
365citing papers in PubMed
34.5field-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

365 citing papers in PubMed, 721 citations in OpenAlex.

  1. Review
  2. Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  11. Regulatory B Cells in Tumor Microenvironment.Current issues in molecular biology · 2026
    Review
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305 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 at 1 institution in 1 country.

Scott B RothbartLineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Biochemistry & Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Brian D StrahlLineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Biochemistry & Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. Electronic address: brian_strahl@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Role of Set2 and H3 methylation in chromatin functionR01GM068088 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STRAHL, BRIAN D · 2003 to 2017
$3.4M
Engineering histone genes to interrogate the epigenetic code in space and timeR01DA036897 · NIDA · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DURONIO, ROBERT J, MATERA, A. GREGORY · 2013 to 2017
$2.2M
Spatiotemporal Control of the Epigenome via Photoactivatable Nuclear LocalizationR01DA036877 · NIDA · UNIV OF NORTH CAROLINA CHAPEL HILL · PI HAHN, KLAUS M., KUHLMAN, BRIAN A · 2013 to 2017
$2.1M
Mechanisms Regulating DNA Methylation Maintenance in ChromatinR00CA181343 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI ROTHBART, SCOTT · 2015 to 2017
$746k
Mechanisms Regulating DNA Methylation Maintenance in ChromatinK99CA181343 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROTHBART, SCOTT · 2014 to 2015
$211k
NCI NIH HHS K99 CA181343NCI NIH HHS K99CA181343NCI NIH HHS R00 CA181343NIDA NIH HHS R01 DA036877NIDA NIH HHS R01DA036877NIDA NIH HHS R01 DA036897NIDA NIH HHS R01DA036897NIGMS NIH HHS R01 GM068088
6 · The paper itself

Abstract

A major mechanism regulating the accessibility and function of eukaryotic genomes are the covalent modifications to DNA and histone proteins that dependably package our genetic information inside the nucleus of every cell. Formally postulated over a decade ago, it is becoming increasingly clear that post-translational modifications (PTMs) on histones act singly and in combination to form a language or 'code' that is read by specialized proteins to facilitate downstream functions in chromatin. Underappreciated at the time was the level of complexity harbored both within histone PTMs and their combinations, as well as within the proteins that read and interpret the language. In addition to histone PTMs, newly-identified DNA modifications that can recruit specific effector proteins have raised further awareness that histone PTMs operate within a broader language of epigenetic modifications to orchestrate the dynamic functions associated with chromatin. Here, we highlight key recent advances in our understanding of the epigenetic language encompassing histone and DNA modifications and foreshadow challenges that lie ahead as we continue our quest to decipher the fundamental mechanisms of chromatin regulation. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylationAnimalsChromatinDNADNA MethylationHistonesHumansSignal TransductionSumoylationTranscription, GeneticUbiquitinationChromatinDNAHistonesChromatinDNA methylationEpigeneticHistoneHistone codePost-translational modification

Identifiers

PMID24631868
PMCPMC4099259
OpenAlexW2063271327

What OpenQuestion holds

Textmetadata
LicenceTDM
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.