Evidence map›Paper›PMID 24583555›Full record

ReviewBiochimica et biophysica acta2014

Chromatin dynamics: interplay between remodeling enzymes and histone modifications.

Sarah G Swygert, Craig L Peterson

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 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing 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

133 citing papers in PubMed, 241 citations in OpenAlex.

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  11. The PBAP chromatin remodeling complex mediates summer diapause via H3K4me3-driven juvenile hormone regulation inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
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  20. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review

73 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.

Sarah G SwygertProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Craig L PetersonProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: craig.peterson@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

YEAST CHROMATIN STRUCTURE/FUNCTIONR01GM054096 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 1997 to 2017
$5.7M
Analysis of the yeast SWI1, SWI2, and SWI3 proteinsR37GM049650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 2006 to 2015
$4.9M
NIGMS NIH HHS R01 GM054096NIGMS NIH HHS R37 GM049650
6 · The paper itself

Abstract

Chromatin dynamics play an essential role in regulating the accessibility of genomic DNA for a variety of nuclear processes, including gene transcription and DNA repair. The posttranslational modification of the core histones and the action of ATP-dependent chromatin remodeling enzymes represent two primary mechanisms by which chromatin dynamics are controlled and linked to nuclear events. Although there are examples in which a histone modification or a remodeling enzyme may be sufficient to drive a chromatin transition, these mechanisms typically work in concert to integrate regulatory inputs, leading to a coordinated alteration in chromatin structure and function. Indeed, site-specific histone modifications can facilitate the recruitment of chromatin remodeling enzymes to particular genomic regions, or they can regulate the efficiency or the outcome of a chromatin remodeling reaction. Conversely, chromatin remodeling enzymes can also influence, and sometimes directly modulate, the modification state of histones. These functional interactions are generally complex, frequently transient, and often require the association of myriad additional factors. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylationAnimalsChromatinChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneDNA RepairEukaryotic CellsHistonesHumansLysineMethylationProtein BindingTranscription FactorsTranscription, GeneticChromatinChromosomal Proteins, Non-HistoneHistonesLysineTranscription FactorsChromatin dynamicsChromatin remodelingHistone modifications

Identifiers

PMID24583555
PMCPMC4099280
OpenAlexW2061434854

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.