Evidence map›Paper›PMID 19250903›Full record

ArticleMolecular cell2009

Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells.

Wei Xie, Chunying Song, Nicolas L Young, Adam S Sperling, Feng Xu, Rupa Sridharan, Anne E Conway, Benjamin A Garcia, Kathrin Plath, Amander T Clark and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
10.6field-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

124 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
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  19. Emerging Therapeutic Potential of SIRT6 Modulators.Journal of medicinal chemistry · 2021
    Review
  20. Article

64 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

11 authors at 2 institutions in 1 country.

Wei XieMolecular Biology Institute, Geffen School of Medicine at the University of California, Los Angeles, Los Angeles, CA 90095, USA.
Chunying Song
Nicolas L Young
Adam S Sperling
Feng Xu
Rupa Sridharan
Anne E Conway
Benjamin A Garcia
Kathrin Plath
Amander T Clark
Michael Grunstein
University of California, Los Angeles · USPrinceton University · 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 R01 GM023674NIGMS NIH HHS R37 GM023674
6 · The paper itself

Abstract

Lysine 56 acetylation in the helical core of histone H3 opens yeast chromatin and enables histone gene transcription, DNA replication, and DNA repair and prevents epigenetic silencing. While K56Ac is globally abundant in yeast and flies, its presence has been uncertain in mammals. We show here using mass spectrometry and genome-wide analyses that K56Ac is present in human embryonic stem cells (hESCs), overlapping strongly at active and inactive promoters with the binding of the key regulators of pluripotency, NANOG, SOX2, and OCT4. This includes also the canonical histone gene promoters and those for the hESC-specific microRNAs. K56Ac then relocates to developmental genes upon cellular differentiation. Thus the K56Ac state more accurately reflects the epigenetic differences between hESCs and somatic cells than other active histone marks such as H3 K4 trimethylation and K9 acetylation. These results suggest that K56Ac is involved in the human core transcriptional network of pluripotency.

Indexed as

Gene Regulatory NetworksAcetylationAnimalsChromatin ImmunoprecipitationEmbryonic Stem CellsGenome, HumanHistonesHomeodomain ProteinsHumansLysineMiceNanog Homeobox ProteinOctamer Transcription Factor-3Protein Processing, Post-TranslationalSOXB1 Transcription FactorsHistonesHomeodomain ProteinsLysineNanog Homeobox ProteinNANOG protein, humanOctamer Transcription Factor-3POU5F1 protein, humanSOX2 protein, humanSOXB1 Transcription Factors

Identifiers

PMID19250903
PMCPMC2671231
OpenAlexW1992111383

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.