Evidence map›Paper›PMID 24005329›Full record

ArticleNature2013

HELQ promotes RAD51 paralogue-dependent repair to avert germ cell loss and tumorigenesis.

Carrie A Adelman, Rafal L Lolo, Nicolai J Birkbak, Olga Murina, Kenichiro Matsuzaki, Zuzana Horejsi, Kalindi Parmar, Valérie Borel, J Mark Skehel, Gordon Stamp and 4 more

Abstract read
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
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

71 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. HELQ Maintains Genome Stability of Primordial Germ Cells by Inhibiting LINE-1 Expression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Helicase HELQ: Molecular Characters Fit for DSB Repair Function.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. A Human HomozygousGenes · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

11 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 4 countries.

Carrie A AdelmanDNA Damage Response Laboratory, London Research Institute, Cancer Research UK, Clare Hall, South Mimms EN6 3LD, UK.
Rafal L Lolo
Nicolai J Birkbak
Olga Murina
Kenichiro Matsuzaki
Zuzana Horejsi
Kalindi Parmar
Valérie Borel
J Mark Skehel
Gordon Stamp
Alan D'Andrea
Alessandro A Sartori
Charles Swanton
Simon J Boulton
Cancer Research UK · GBDana-Farber Cancer Institute · USThe Honourable Society of Lincoln's Inn · GBUniversity of Zurich · CHMRC Laboratory of Molecular Biology · GBTechnical University of Denmark · DK

Funding

STRUCTURE AND FUNCTION OF THE ERYTHROPOIETIN RECEPTORR01DK043889 · NIDDK · DANA-FARBER CANCER INSTITUTE · PI D'ANDREA, ALAN D. · 1992 to 2014
$5.3M
Cancer Research UK 11581Cancer Research UK A3549Medical Research Council G0701935NIDDK NIH HHS R01 DK043889NIDDK NIH HHS R01-DK43889
6 · The paper itself

Abstract

Repair of interstrand crosslinks (ICLs) requires the coordinated action of the intra-S-phase checkpoint and the Fanconi anaemia pathway, which promote ICL incision, translesion synthesis and homologous recombination (reviewed in refs 1, 2). Previous studies have implicated the 3'-5' superfamily 2 helicase HELQ in ICL repair in Drosophila melanogaster (MUS301 (ref. 3)) and Caenorhabditis elegans (HELQ-1 (ref. 4)). Although in vitro analysis suggests that HELQ preferentially unwinds synthetic replication fork substrates with 3' single-stranded DNA overhangs and also disrupts protein-DNA interactions while translocating along DNA, little is known regarding its functions in mammalian organisms. Here we report that HELQ helicase-deficient mice exhibit subfertility, germ cell attrition, ICL sensitivity and tumour predisposition, with Helq heterozygous mice exhibiting a similar, albeit less severe, phenotype than the null, indicative of haploinsufficiency. We establish that HELQ interacts directly with the RAD51 paralogue complex BCDX2 and functions in parallel to the Fanconi anaemia pathway to promote efficient homologous recombination at damaged replication forks. Thus, our results reveal a critical role for HELQ in replication-coupled DNA repair, germ cell maintenance and tumour suppression in mammals.

Indexed as

CarcinogenesisDNA RepairAnimalsDNA DamageDNA HelicasesDNA ReplicationFanconi AnemiaFanconi Anemia Complementation Group D2 ProteinFemaleGene DeletionGerm CellsMaleMiceMultiprotein ComplexesOvarian NeoplasmsOvaryDNA HelicasesFancd2 protein, mouseFanconi Anemia Complementation Group D2 ProteinHELQ protein, mouseMultiprotein ComplexesRad51 protein, mouseRad51 Recombinase

Identifiers

PMID24005329
PMCPMC3836231
OpenAlexW2015969693

What OpenQuestion holds

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LicenceTDM
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.