Evidence map›Paper›PMID 31200754›Full record

ReviewEpigenetics & chromatin2019

The histone variant H2A.Z in gene regulation.

Benedetto Daniele Giaimo, Francesca Ferrante, Andreas Herchenröther, Sandra B Hake, Tilman Borggrefe

Open access · goldAbstract readReview
In one paragraph

Review in Epigenetics & chromatin, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 196 papers.

0numbers the graph read from it
0cells of the map it votes in
196citing papers in PubMed
14.0field-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

196 citing papers in PubMed, 354 citations in OpenAlex.

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  6. Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. In thebioRxiv : the preprint server for biology · 2026
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  15. Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026
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136 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

5 authors at 1 institution in 1 country.

Benedetto Daniele GiaimoInstitute of Biochemistry, University of Giessen, Friedrichstrasse 24, 35392, Giessen, Germany. Benedetto.Giaimo@biochemie.med.uni-giessen.de.
Francesca FerranteInstitute of Biochemistry, University of Giessen, Friedrichstrasse 24, 35392, Giessen, Germany.
Andreas HerchenrötherInstitute for Genetics, University of Giessen, Heinrich-Buff-Ring 58-62, 35392, Giessen, Germany.
Sandra B HakeInstitute for Genetics, University of Giessen, Heinrich-Buff-Ring 58-62, 35392, Giessen, Germany.
Tilman BorggrefeInstitute of Biochemistry, University of Giessen, Friedrichstrasse 24, 35392, Giessen, Germany. Tilman.Borggrefe@biochemie.med.uni-giessen.de.ORCID 0000-0003-4325-5452
Justus-Liebig-Universität Gießen · DE

Funding

Deutsche Forschungsgemeinschaft BO1639/5-1Deutsche Forschungsgemeinschaft TRR81ECCPS SH1ECCPS TB1UKGM grant BDG-04Von-Behring-Röntgen-Stiftung BO04
6 · The paper itself

Abstract

The histone variant H2A.Z is involved in several processes such as transcriptional control, DNA repair, regulation of centromeric heterochromatin and, not surprisingly, is implicated in diseases such as cancer. Here, we review the recent developments on H2A.Z focusing on its role in transcriptional activation and repression. H2A.Z, as a replication-independent histone, has been studied in several model organisms and inducible mammalian model systems. Its loading machinery and several modifying enzymes have been recently identified, and some of the long-standing discrepancies in transcriptional activation and/or repression are about to be resolved. The buffering functions of H2A.Z, as supported by genome-wide localization and analyzed in several dynamic systems, are an excellent example of transcriptional control. Posttranslational modifications such as acetylation and ubiquitination of H2A.Z, as well as its specific binding partners, are in our view central players in the control of gene expression. Understanding the key-mechanisms in either turnover or stabilization of H2A.Z-containing nucleosomes as well as defining the H2A.Z interactome will pave the way for therapeutic applications in the future.

Indexed as

Gene Expression RegulationAcetylationAdenosine TriphosphatasesAnimalsDNA RepairHeterochromatinHistonesHumansNucleosomesPromoter Regions, GeneticProtein Processing, Post-TranslationalTranscriptional ActivationUbiquitinationAdenosine TriphosphatasesHeterochromatinhistone H2A.F-ZHistonesNucleosomesCRISPR/Cas9DominoH2AvH2A.ZHistone variantp400Tip60

Identifiers

PMID31200754
PMCPMC6570943
OpenAlexW2951529323

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.