Evidence map›Paper›PMID 23798425›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Acetylated histone H3K56 interacts with Oct4 to promote mouse embryonic stem cell pluripotency.

Yuliang Tan, Yong Xue, Chunying Song, Michael Grunstein

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 85 citations in OpenAlex.

  1. H3K27ac Is Essential for Human Naive Pluripotency Modulated by m6A-Driven EP300 Expression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  17. Emerging Therapeutic Potential of SIRT6 Modulators.Journal of medicinal chemistry · 2021
    Review
  18. Article
  19. Review
  20. Organization of the Pluripotent Genome.Cold Spring Harbor perspectives in biology · 2021
    Review

1 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

4 authors at 1 institution in 1 country.

Yuliang TanDepartment of Biological Chemistry and the Molecular Biology Institute, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
Yong Xue
Chunying Song
Michael Grunstein
University of California, Los Angeles · US

Funding

CONTROL OF HISTONE FUNCTION IN YEASTR37GM023674 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GRUNSTEIN, MICHAEL · 1998 to 2007
$4.7M
GENETIC AND BIOCHEMICAL APPROACH TO HISTONE FUNCTIONR01GM023674 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GRUNSTEIN, MICHAEL · 1985 to 2011
$2.6M
NIGMS NIH HHS GM23674NIGMS NIH HHS R01 GM023674NIGMS NIH HHS R37 GM023674
6 · The paper itself

Abstract

The presence of acetylated histone H3K56 (H3K56ac) in human ES cells (ESCs) correlates positively with the binding of Nanog, Sox2, and Oct4 (NSO) transcription factors at their target gene promoters. However, the function of H3K56ac there has been unclear. We now report that Oct4 interacts with H3K56ac in mouse ESC nuclear extracts and that perturbing H3K56 acetylation decreases Oct4-H3 binding. This interaction is likely to be direct because it can be recapitulated in vitro in an H3K56ac-dependent manner and is functionally important because H3K56ac combines with NSO factors in chromatin immunoprecipitation sequencing to mark the regions associated with pluripotency better than NSO alone. Moreover, reducing H3K56ac by short hairpin Asf1a decreases expression of pluripotency-related markers and increases expression of differentiation-related ones. Therefore, our data suggest that H3K56ac plays a central role in binding to Oct4 to promote the pluripotency of ESCs.

Indexed as

AcetylationAnimalsCells, CulturedEmbryonic Stem CellsHistonesMiceOctamer Transcription Factor-3Protein BindingHistonesOctamer Transcription Factor-3Pou5f1 protein, mouse

Identifiers

PMID23798425
PMCPMC3710873
OpenAlexW2007662442

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.