Evidence map›Paper›PMID 24753410›Full record

ArticleNucleic acids research2014

The histone variant H2A.Bbd is enriched at sites of DNA synthesis.

Viola Sansoni, Corella S Casas-Delucchi, Malini Rajan, Andreas Schmidt, Clemens Bönisch, Andreas W Thomae, Martin S Staege, Sandra B Hake, M Cristina Cardoso, Axel Imhof

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 66 citations in OpenAlex.

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  8. Histone H2A variants: Diversifying chromatin to ensure genome integrity.Seminars in cell & developmental biology · 2023
    Review
  9. Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023
    Review
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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

10 authors at 4 institutions in 1 country.

Viola SansoniMunich Center of Integrated Protein Science, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
Corella S Casas-DelucchiTechnische Universität Darmstadt Schnittspahnstr. 10, 64287 Darmstadt, Germany.
Malini RajanTechnische Universität Darmstadt Schnittspahnstr. 10, 64287 Darmstadt, Germany.
Andreas SchmidtMunich Center of Integrated Protein Science, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
Clemens BönischAdolf-Butenandt Institute, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
Andreas W ThomaeMunich Center of Integrated Protein Science, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
Martin S StaegeDepartment of Pediatrics, Martin Luther University Halle-Wittenberg, Ernst-Grube-Str. 40, 06097 Halle, Germany.
Sandra B HakeMunich Center of Integrated Protein Science, Ludwig Maximilians University of Munich, 80336 Munich, Germany Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
M Cristina CardosoTechnische Universität Darmstadt Schnittspahnstr. 10, 64287 Darmstadt, Germany.
Axel ImhofMunich Center of Integrated Protein Science, Ludwig Maximilians University of Munich, 80336 Munich, Germany Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, 80336 Munich, Germany Imhof@lmu.de.
Ludwig-Maximilians-Universität München · DETechnical University of Darmstadt · DECenter for Integrated Protein Science Munich · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone variants play an important role in shaping the mammalian epigenome and their aberrant expression is frequently observed in several types of cancer. However, the mechanisms that mediate their function and the composition of the variant-containing chromatin are still largely unknown. A proteomic interrogation of chromatin containing the different H2A variants macroH2A.1.2, H2A.Bbd and H2A revealed a strikingly different protein composition. Gene ontology analysis reveals a strong enrichment of splicing factors as well as components of the mammalian replisome in H2A.Bbd-containing chromatin. We find H2A.Bbd localizing transiently to sites of DNA synthesis during S-phase and during DNA repair. Cells that express H2A.Bbd have a shortened S-phase and are more susceptible to DNA damage, two phenotypes that are also observed in human Hodgkin's lymphoma cells that aberrantly express this variant. Based on our experiments we conclude that H2A.Bbd is targeted to newly synthesized DNA during replication and DNA repair. The transient incorporation of H2A.Bbd may be due to the intrinsic instability of nucleosomes carrying this variant or a faster chromatin loading. This potentially leads to a disturbance of the existing chromatin structure, which may have effects on cell cycle regulation and DNA damage sensitivity.

Indexed as

AnimalsCell Line, TumorCells, CulturedChromatinDNADNA DamageDNA RepairDNA ReplicationFemaleGenetic VariationHistonesHumansMiceChromatinDNAHistones

Identifiers

PMID24753410
PMCPMC4041467
OpenAlexW2120971578

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.