Evidence map›Paper›PMID 23553272›Full record

ReviewChromosoma2013

The variant histone H2A.V of Drosophila--three roles, two guises.

Sandro Baldi, Peter B Becker

Abstract readReview
PubMed Publisher
In one paragraph

Review in Chromosoma, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. In thebioRxiv : the preprint server for biology · 2026
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  9. Global γH2AX phosphorylation inmicroPublication biology · 2025
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  20. Review
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

2 authors at 2 institutions in 1 country.

Sandro BaldiCenter for Integrated Protein Science, Adolf-Butenandt-Institute, Ludwig-Maximilians-University, 80336 Munich, Germany.
Peter B Becker
Center for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone variants play important roles in eukaryotic genome organization, the control of gene expression, cell division and DNA repair. Unlike other organisms that employ several H2A variants for different functions, the parsimonious fruit fly Drosophila melanogaster gets along with just a single H2A variant, H2A.V. Remarkably, H2A.V unites within one molecule features and functions of two different mammalian H2A variants, H2A.Z and H2A.X. Accordingly, H2A.V is involved in diverse functions, as an element of a class of active promoter structure, as a foundation for heterochromatin assembly and as a DNA damage sensor. Here, we comprehensively review the current knowledge of this fascinating histone variant.

Indexed as

AnimalsChromatin Assembly and DisassemblyDrosophila melanogasterDrosophila ProteinsHistonesHumansDrosophila ProteinsHistones

Identifiers

PMID23553272
OpenAlexW2078294443

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.