Evidence map›Paper›PMID 26783963›Full record

ArticleOncotarget2016

Histone H3 lysine 4 acetylation and methylation dynamics define breast cancer subtypes.

Terri L Messier, Jonathan A R Gordon, Joseph R Boyd, Coralee E Tye, Gillian Browne, Janet L Stein, Jane B Lian, Gary S Stein

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 114 citations in OpenAlex.

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  17. Review
  18. Acetylation of Histone H3 in Cancer Progression and Prognosis.International journal of molecular sciences · 2024
    Review
  19. Article
  20. Article

15 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

8 authors at 1 institution in 1 country.

Terri L MessierDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Jonathan A R GordonDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Joseph R BoydDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Coralee E TyeDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Gillian BrowneDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Janet L SteinDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Jane B LianDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
Gary S SteinDepartment of Biochemistry and University of Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT, USA.
University of Vermont · US

Funding

SUBNUCLEAR TARGETING OF TRANSCRIPTION FACTORSP01CA082834 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, GARY S. · 2001 to 2015
$18.4M
Synthesis of Osteocalcin in BoneR37DE012528 · NIDCR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LIAN, JANE B. · 2008 to 2017
$5.0M
NCI NIH HHS P01 CA082834NIDCR NIH HHS R37 DE012528
6 · The paper itself

Abstract

The onset and progression of breast cancer are linked to genetic and epigenetic changes that alter the normal programming of cells. Epigenetic modifications of DNA and histones contribute to chromatin structure that result in the activation or repression of gene expression. Several epigenetic pathways have been shown to be highly deregulated in cancer cells. Targeting specific histone modifications represents a viable strategy to prevent oncogenic transformation, tumor growth or metastasis. Methylation of histone H3 lysine 4 has been extensively studied and shown to mark genes for expression; however this residue can also be acetylated and the specific function of this alteration is less well known. To define the relative roles of histone H3 methylation (H3K4me3) and acetylation (H3K4ac) in breast cancer, we determined genomic regions enriched for both marks in normal-like (MCF10A), transformed (MCF7) and metastatic (MDA-MB-231) cells using a genome-wide ChIP-Seq approach. Our data revealed a genome-wide gain of H3K4ac associated with both early and late breast cancer cell phenotypes, while gain of H3K4me3 was predominantly associated with late stage cancer cells. Enrichment of H3K4ac was over-represented at promoters of genes associated with cancer-related phenotypic traits, such as estrogen response and epithelial-to-mesenchymal transition pathways. Our findings highlight an important role for H3K4ac in predicting epigenetic changes associated with early stages of transformation. In addition, our data provide a valuable resource for understanding epigenetic signatures that correlate with known breast cancer-associated oncogenic pathways.

Indexed as

AcetylationBreast NeoplasmsDNA MethylationEpigenesis, GeneticFemaleHistonesHumansLysineHistonesLysinebreast cancerEMT pathwayepigeneticsestrogen receptor pathwayhistone H3K4 modifications

Identifiers

PMID26783963
PMCPMC4868673
OpenAlexW2258775018

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.