Evidence map›Paper›PMID 33456978›Full record

ArticleActa naturae

The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation.

N V Soshnikova, A A Sheynov, Eu V Tatarskiy, S G Georgieva

Abstract read
In one paragraph

Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Review
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  4. Article
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  6. Article
  7. Histone acylation at a glance.Journal of cell science · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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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

4 authors.

N V SoshnikovaInstitute of Gene Biology Russian Academy of Sciences, Moscow, 119334 Russia.
A A SheynovInstitute of Gene Biology Russian Academy of Sciences, Moscow, 119334 Russia.
Eu V TatarskiyInstitute of Gene Biology Russian Academy of Sciences, Moscow, 119334 Russia.
S G GeorgievaInstitute of Gene Biology Russian Academy of Sciences, Moscow, 119334 Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DPF (double PHD finger) domain consists of two PHD fingers organized in tandem. The two PHD-finger domains within a DPF form a single structure that interacts with the modification of the N-terminal histone fragment in a way different from that for single PHD fingers. Several histone modifications interacting with the DPF domain have already been identified. They include acetylation of H3K14 and H3K9, as well as crotonylation of H3K14. These modifications are found predominantly in transcriptionally active chromatin. Proteins containing DPF belong to two classes of protein complexes, which are the transcriptional coactivators involved in the regulation of the chromatin structure. These are the histone acetyltransferase complex belonging to the MYST family and the SWI/SNF chromatin-remodeling complex. The DPF domain is responsible for the specificity of the interactions between these complexes and chromatin. Proteins containing DPF play a crucial role in the activation of the transcription of a number of genes expressed during the development of an organism. These genes are important in the differentiation and malignant transformation of mammalian cells.

Indexed as

BAFDPF1DPF2DPF3DPF domainsMOZ and MORF histone acetyltransferasesPBAFPHF10tandem PHD

Identifiers

PMID33456978
PMCPMC7800603

What OpenQuestion holds

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Registered trials

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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.