Evidence map›Paper›PMID 41971996›Full record

ArticleiScience2026

hnRNPUL1 has a dead polynucleotide kinase domain that regulates RNA and protein interactions.

Carmen V Apostol, Ang Li, Peter Daniels, Llywelyn Griffith, Johnathan Cooper-Knock, Elisa Aguilar-Martinez, Ivaylo D Yonchev, Ashleigh G R Whelan, Pamela J Shaw, Ian M Sudbery and 1 more

Abstract read
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In one paragraph

Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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

11 authors.

Carmen V ApostolSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Ang LiSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Peter DanielsSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Llywelyn GriffithSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Johnathan Cooper-KnockSheffield Institute for Translational Neuroscience, The University of Sheffield, Sheffield S10 2HQ, UK.
Elisa Aguilar-MartinezSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Ivaylo D YonchevSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Ashleigh G R WhelanSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Pamela J ShawSheffield Institute for Translational Neuroscience, The University of Sheffield, Sheffield S10 2HQ, UK.
Ian M SudberySheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Stuart A WilsonSheffield Institute for Nucleic Acids, School of Biosciences, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

hnRNPUL1 is a nuclear RNA-binding protein involved in both pre-mRNA splicing and DNA double-strand break repair. Using AlphaFold, we show that hnRNPUL1 has a central folded region consisting of tightly juxtaposed SPRY and dead polynucleotide kinase (dPNK) domains flanked by intrinsically disordered regions (IDRs). The dPNK domain binds both nucleotides and RNA. Remarkably, polynucleotide kinase activity can be reactivated with a single amino acid substitution. Mutations altering nucleotide binding also change the ability of the entire protein to bind RNA and regulate homotypic versus heterotypic protein interactions driven by the IDRs. A mutation that prevents nucleotide binding also destabilizes the protein. In a small number of amyotrophic lateral sclerosis patients, we identify rare coding variants in the

Indexed as

Molecular interactionProtein structure aspects

Identifiers

PMID41971996
PMCPMC13066744

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.