Evidence map›Paper›PMID 32702132›Full record

ArticleJournal of biochemistry2020

Linker DNA and histone contributions in nucleosome binding by p53.

Masahiro Nishimura, Yasuhiro Arimura, Kayo Nozawa, Hitoshi Kurumizaka

Open access · hybridAbstract read
In one paragraph

Article in Journal of biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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  12. Pioneer factors: nature or nurture?Critical reviews in biochemistry and molecular biology
    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

4 authors at 1 institution in 2 countries.

Masahiro NishimuraLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences.
Yasuhiro ArimuraLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences.
Kayo NozawaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences.
Hitoshi KurumizakaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences.
Quantitative BioSciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumour suppressor protein p53 regulates various genes involved in cell-cycle arrest, apoptosis and DNA repair in response to cellular stress, and apparently functions as a pioneer transcription factor. The pioneer transcription factors can bind nucleosomal DNA, where many transcription factors are largely restricted. However, the mechanisms by which p53 recognizes the nucleosomal DNA are poorly understood. In the present study, we found that p53 requires linker DNAs for the efficient formation of p53-nucleosome complexes. p53 forms an additional specific complex with the nucleosome, when the p53 binding sequence is located around the entry/exit region of the nucleosomal DNA. We also showed that p53 directly binds to the histone H3-H4 complex via its N-terminal 1-93 amino acid region. These results shed light on the mechanism of nucleosome recognition by p53.

Indexed as

Binding SitesDNAHistonesHumansNucleosomesProtein BindingProtein ConformationTumor Suppressor Protein p53DNAHistonesNucleosomesTP53 protein, humanTumor Suppressor Protein p53chromatinhistonenucleosomep53pioneer transcription factor

Identifiers

PMID32702132
PMCPMC7763433
OpenAlexW3044816502

What OpenQuestion holds

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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.