Evidence map›Paper›PMID 20003410›Full record

ArticleBMC biology2009

Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates.

Deanna Dryhurst, Toyotaka Ishibashi, Kristie L Rose, José M Eirín-López, Darin McDonald, Begonia Silva-Moreno, Nik Veldhoen, Caren C Helbing, Michael J Hendzel, Jeffrey Shabanowitz and 2 more

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

75 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Article
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  6. Review
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  9. Article
  10. Role of the histone variant H2A.Z.1 in memory, transcription, and alternative splicing is mediated by lysine modification.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2024
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023
    Review
  17. Article
  18. Review
  19. Review
  20. Article

15 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

12 authors at 6 institutions in 3 countries.

Deanna DryhurstDepartment of Biochemistry and Microbiology and The Center for Biomedical Research, University of Victoria, Petch Building, Victoria, BC, V8W 3P6, Canada. deannad@uvic.ca
Toyotaka Ishibashi
Kristie L Rose
José M Eirín-López
Darin McDonald
Begonia Silva-Moreno
Nik Veldhoen
Caren C Helbing
Michael J Hendzel
Jeffrey Shabanowitz
Donald F Hunt
Juan Ausió
University of Victoria · CAUniversity of Alberta · CAUniversity of Virginia · USScripps Research Institute · USUniversidade da Coruña · ESUniversity of California, Berkeley · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
CIHR MOP-97878NIGMS NIH HHS GM 37537NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

backgroundWithin chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues.

resultsWe report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution.

conclusionsOur biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence.

Indexed as

AcetylationAnimalsAvian ProteinsBiological EvolutionCells, CulturedChickensEuchromatinHeLa CellsHistonesHumansMacaca mulattaMethylationMicePromoter Regions, GeneticProtein IsoformsRNA, MessengerAvian ProteinsEuchromatinhistone H2A.F-ZHistonesProtein IsoformsRNA, Messenger

Identifiers

PMID20003410
PMCPMC2805615
OpenAlexW2070835225

What OpenQuestion holds

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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.