Evidence map›Paper›PMID 32500630›Full record

ArticleGenes to cells : devoted to molecular & cellular mechanisms2020

The N-terminal and C-terminal halves of histone H2A.Z independently function in nucleosome positioning and stability.

Shoko Sato, Naoki Tanaka, Yasuhiro Arimura, Tomoya Kujirai, Hitoshi Kurumizaka

Open access · hybridAbstract read
In one paragraph

Article in Genes to cells : devoted to molecular & cellular mechanisms, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
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    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

5 authors at 2 institutions in 2 countries.

Shoko SatoLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.
Naoki TanakaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Yasuhiro ArimuraLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.
Tomoya KujiraiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.
Hitoshi KurumizakaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.ORCID https://orcid.org/0000-0001-7412-3722
Quantitative BioSciences · USWaseda University · JP

Funding

Core Research for Evolutional Science and Technology JPMJCR16G1Exploratory Research for Advanced Technology JPMJER1901Japan Agency for Medical Research and Development JP20am0101076Japan Society for the Promotion of Science JP17H01408Japan Society for the Promotion of Science JP18H05534Japan Society for the Promotion of Science JP19K06609Japan Society for the Promotion of Science JP19K21177
6 · The paper itself

Abstract

Nucleosome positioning and stability affect gene regulation in eukaryotic chromatin. Histone H2A.Z is an evolutionally conserved histone variant that forms mobile and unstable nucleosomes in vivo and in vitro. In the present study, we reconstituted nucleosomes containing human H2A.Z.1 mutants, in which the N-terminal or C-terminal half of H2A.Z.1 was replaced by the corresponding canonical H2A region. We found that the N-terminal portion of H2A.Z.1 is involved in flexible nucleosome positioning, whereas the C-terminal portion leads to weak H2A.Z.1-H2B association in the nucleosome. These results indicate that the N-terminal and C-terminal portions are independently responsible for the H2A.Z.1 nucleosome characteristics.

Indexed as

ChromatinChromatin Assembly and DisassemblyHistonesHumansModels, MolecularNucleosomesProtein BindingProtein ConformationChromatinhistone H2A.F-ZHistonesNucleosomesepigeneticsH2A.Zhistone variantnucleosome positioningnucleosome stability

Identifiers

PMID32500630
PMCPMC7496805
OpenAlexW3033211951

What OpenQuestion holds

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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.