Evidence map›Paper›PMID 39965657›Full record

ArticleOpen biology2025

The human HELQ helicase and XRN2 exoribonuclease cooperate in R-loop resolution.

J M Pan, H Betts, A Cubbon, L He, E L Bolt, P Soultanas

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Open biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

6 authors.

J M PanBiodiscovery Institute, School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
H BettsBiodiscovery Institute, School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
A CubbonSchool of Life Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
L HeSchool of Life Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
E L BoltSchool of Life Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
P SoultanasBiodiscovery Institute, School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.ORCID 0000-0003-3578-5699

Funding

BBSRCNanna TherapeuticsSchool of Chemistry PhD
6 · The paper itself

Abstract

The human HELQ helicase is a superfamily 2, 3'-5 helicase homologous to POLQ and RNA helicases of the Ski2-like subfamily. It is involved in diverse aspects of DNA repair and is an emerging prognosis biomarker and novel drug target for cancer therapy. HELQ interacts with RPA through its inherently disordered N-HELQ domain and hence is recruited to RPA-bound DNA substrates. Our study reveals a novel role for HELQ in R-loop resolution. We show in cells and

Indexed as

DNA HelicasesExoribonucleasesR-Loop StructuresHumansProtein BindingDNA HelicasesExoribonucleasesXRN2 protein, humanDNA repairHELQ helicaseR-loopsRPAXRN2 exoribonuclease

Identifiers

PMID39965657
PMCPMC11835494

What OpenQuestion holds

Textmetadata
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.