Evidence map›Paper›PMID 27417714›Full record

ArticleDoklady. Biochemistry and biophysics2016

CTCF and Sgfl1 proteins form alternative complexes with ENY2 proteins.

A N Bonchuk, P G Georgiev, O G Maksimenko

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Article in Doklady. Biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

A N BonchukInstitute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, Moscow, 119334, Russia. errinaceus@rambler.ru.
P G GeorgievInstitute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, Moscow, 119334, Russia.
O G MaksimenkoInstitute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, Moscow, 119334, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ENY2 is a multifunctional protein, a component of the SAGA complex (protein complex involved in the regulation of transcription, possessing histone-acetyltransferase and H2B-histone-deubiquitinylating activities [1]) and TREX-2 (complex involved in the mRNA nuclear export [2]). Besides this, the interactions of ENY2 with DNA-binding insulator proteins Su(Hw) and dCTCF have been described as essential for the barrier activity of corresponding insulators [3, 4]. In this study, we described the formation of mutually exclusive complexes of ENY2 with insulator proteins and Sgfl1-a component of the SAGA complex, direct binding partner for ENY2.

Indexed as

AnimalsCCCTC-Binding FactorDrosophilaDrosophila ProteinsEscherichia coliEscherichia coli ProteinsHumansMolecular Docking SimulationNuclear Magnetic Resonance, BiomolecularRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsCCCTC-Binding FactorCTCF protein, humanDrosophila ProteinsEscherichia coli ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSgf11 protein, DrosophilaSGF11 protein, S cerevisiaeTranscription Factors

Identifiers

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.