Evidence map›Paper›PMID 41476260›Full record

ArticleCommunications biology2025

The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.

Tim Rasmussen, Jannik Küspert, Lars Schönemann, Dietmar Geiger, Bettina Böttcher

Abstract read
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026
    Article
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.

Tim RasmussenUniversity of Würzburg, Rudolf Virchow Centre, Würzburg, Germany.ORCID http://orcid.org/0000-0003-1126-846X
Jannik KüspertUniversity of Würzburg, Julius-von-Sachs-Institute for Biosciences, Department of Molecular Plant Physiology and Biophysics, Würzburg, Germany.
Lars SchönemannUniversity of Würzburg, Rudolf Virchow Centre, Würzburg, Germany.
Dietmar GeigerUniversity of Würzburg, Julius-von-Sachs-Institute for Biosciences, Department of Molecular Plant Physiology and Biophysics, Würzburg, Germany. dietmar.geiger@uni-wuerzburg.de.
Bettina BöttcherUniversity of Würzburg, Rudolf Virchow Centre, Würzburg, Germany. Bettina.boettcher@uni-wuerzburg.de.ORCID http://orcid.org/0000-0002-7962-4849

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 359471283Deutsche Forschungsgemeinschaft (German Research Foundation) 456578072Deutsche Forschungsgemeinschaft (German Research Foundation) 525040890
6 · The paper itself

Abstract

Proteins of the Drosophila behaviour/human splicing (DBHS) family are involved in many aspects of gene regulation and maintenance like transcription, splicing and DNA repair. DBHS proteins form obligate homo- and heterodimers through interactions within a globular domain and can further dynamically oligomerise through α-helical coiled-coils, which is crucial for many functions. While the atomic structures of the dimers are established, the arrangement in higher oligomers is unknown. Here we present the structure of a filamentous NONO/SFPQ heterooligomer resolved by cryo-EM. The filaments form a double helix which is stabilized by an interdigitating network of coiled-coil interactions.

Indexed as

DNA-Binding ProteinsDrosophila ProteinsRNA-Binding ProteinsAnimalsCryoelectron MicroscopyDrosophila melanogasterHumansModels, MolecularProtein MultimerizationDNA-Binding ProteinsDrosophila ProteinsNONO protein, humanRNA-Binding Proteins

Identifiers

PMID41476260
PMCPMC12848012

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.