Evidence map›Paper›PMID 27084935›Full record

ArticleNucleic acids research2016

The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.

Gavin J Knott, Charles S Bond, Archa H Fox

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed, 2 pooled it
–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

198 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026
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  15. Development of PolyHis-Targeting PROTAC Degraders.Angewandte Chemie (International ed. in English) · 2026
    Article
  16. Review
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138 more citing papers are in PubMed but not listed here.

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.

Gavin J KnottSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, WA 6009, Australia.
Charles S BondSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, WA 6009, Australia.
Archa H FoxSchool of Anatomy, Physiology and Human Biology, The University of Western Australia, Crawley, Western Australia, WA 6009, Australia Harry Perkins Institute of Medical Research, QEII Medical Centre, Nedlands, WA 6009, Australia archa.fox@uwa.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear proteins are often given a concise title that captures their function, such as 'transcription factor,' 'polymerase' or 'nuclear-receptor.' However, for members of the Drosophila behavior/human splicing (DBHS) protein family, no such clean-cut title exists. DBHS proteins are frequently identified engaging in almost every step of gene regulation, including but not limited to, transcriptional regulation, RNA processing and transport, and DNA repair. Herein, we present a coherent picture of DBHS proteins, integrating recent structural insights on dimerization, nucleic acid binding modalities and oligomerization propensity with biological function. The emerging paradigm describes a family of dynamic proteins mediating a wide range of protein-protein and protein-nucleic acid interactions, on the whole acting as a multipurpose molecular scaffold. Overall, significant steps toward appreciating the role of DBHS proteins have been made, but we are only beginning to understand the complexity and broader importance of this family in cellular biology.

Indexed as

Amino Acid SequenceAnimalsCaenorhabditis elegansDNA-Binding ProteinsDNA RepairDrosophila melanogasterGene Expression RegulationHumansNuclear Matrix-Associated ProteinsNuclear ProteinsOctamer Transcription FactorsProtein Interaction MapsProtein Structure, SecondaryPTB-Associated Splicing FactorRNA-Binding ProteinsRNA Processing, Post-TranscriptionalDNA-Binding ProteinsNONO protein, humanNuclear Matrix-Associated ProteinsNuclear ProteinsOctamer Transcription FactorsPSPC1 protein, humanPTB-Associated Splicing FactorRNA-Binding ProteinsRNA Splicing Factors

Identifiers

PMID27084935
PMCPMC4872119

What OpenQuestion holds

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LicenceCC BY-NC
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.