Evidence map›Paper›PMID 34316696›Full record

ArticleNAR cancer2021

The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core.

Tabitha Jenkins, Sarah J Northall, Denis Ptchelkine, Rebecca Lever, Andrew Cubbon, Hannah Betts, Vincenzo Taresco, Christopher D O Cooper, Peter J McHugh, Panos Soultanas and 1 more

Abstract read
In one paragraph

Article in NAR cancer, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. POLD3 as Controller of Replicative DNA Repair.International journal of molecular sciences · 2024
    Review
  8. Helicase HELQ: Molecular Characters Fit for DSB Repair Function.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Review
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.

Tabitha JenkinsSchool of Life Sciences, The University of Nottingham, NG7 2UH, Nottingham, UK.
Sarah J NorthallSchool of Life Sciences, The University of Nottingham, NG7 2UH, Nottingham, UK.
Denis PtchelkineResearch Complex at Harwell (RCaH), OX11 0FA, Didcot, UK.
Rebecca LeverSchool of Life Sciences, The University of Nottingham, NG7 2UH, Nottingham, UK.
Andrew CubbonSchool of Life Sciences, The University of Nottingham, NG7 2UH, Nottingham, UK.
Hannah BettsSchool of Chemistry, The University of Nottingham, NG7 2RD, Nottingham, UK.
Vincenzo TarescoSchool of Pharmacy, The University of Nottingham, NG7 2RD, Nottingham, UK.
Christopher D O CooperDepartment of Biological and Geographical Sciences, School of Applied Sciences, The University of Huddersfield, HD1 3DH, Huddersfield, UK.
Peter J McHughMRC Weatherall Institute of Molecular Medicine (WIMM), University of Oxford, OX3 9DS, Oxford, UK.ORCID 0000-0002-8679-4627
Panos SoultanasSchool of Chemistry, The University of Nottingham, NG7 2RD, Nottingham, UK.ORCID 0000-0003-3578-5699
Edward L BoltSchool of Life Sciences, The University of Nottingham, NG7 2UH, Nottingham, UK.ORCID 0000-0002-5656-7706

Funding

Medical Research Council MR/R009368/1
6 · The paper itself

Abstract

Genome instability is a characteristic enabling factor for carcinogenesis. HelQ helicase is a component of human DNA maintenance systems that prevent or reverse genome instability arising during DNA replication. Here, we provide details of the molecular mechanisms that underpin HelQ function-its recruitment onto ssDNA through interaction with replication protein A (RPA), and subsequent translocation of HelQ along ssDNA. We describe for the first time a functional role for the non-catalytic N-terminal region of HelQ, by identifying and characterizing its PWI-like domain. We present evidence that this domain of HelQ mediates interaction with RPA that orchestrates loading of the helicase domains onto ssDNA. Once HelQ is loaded onto the ssDNA, ATP-Mg

Identifiers

PMID34316696
PMCPMC8210318

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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.