Evidence map›Paper›PMID 25831490›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structures.

Ashley C W Pike, Shivasankari Gomathinayagam, Paolo Swuec, Matteo Berti, Ying Zhang, Christina Schnecke, Francesca Marino, Frank von Delft, Ludovic Renault, Alessandro Costa and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Structural Chemistry of Helicase Inhibition.Journal of medicinal chemistry · 2025
    Review
  10. Cold stress enhances cryotolerance inCurrent research in microbial sciences · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Mechanism of Bloom syndrome complex assembly required for double Holliday junction dissolution and genome stability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Recombination and restart at blocked replication forks.Current opinion in genetics & development · 2021
    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

12 authors at 4 institutions in 3 countries.

Ashley C W PikeStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom;
Shivasankari GomathinayagamEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO 63104;
Paolo SwuecCancer Research UK Clare Hall Laboratories, South Mimms EN6 3LD, United Kingdom; and.
Matteo BertiEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO 63104;
Ying ZhangStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom; opher.gileadi@sgc.ox.ac.uk avindign@slu.edu.
Christina SchneckeStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom;
Francesca MarinoStructural Biology Laboratory, Sincrotrone Trieste, Trieste 34149, Italy.
Frank von DelftStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom;
Ludovic RenaultCancer Research UK Clare Hall Laboratories, South Mimms EN6 3LD, United Kingdom; and.
Alessandro CostaCancer Research UK Clare Hall Laboratories, South Mimms EN6 3LD, United Kingdom; and.
Opher GileadiStructural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom; opher.gileadi@sgc.ox.ac.uk avindign@slu.edu.ORCID http://orcid.org/0000-0001-6886-898X
Alessandro VindigniEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO 63104; opher.gileadi@sgc.ox.ac.uk avindign@slu.edu.
University of Oxford · GBSaint Louis University · USUniversity of Cambridge · GBElettra-Sincrotrone Trieste S.C.p.A. · IT

Funding

New Mechanisms of Replication Stress ResponseR01GM108648 · NIGMS · SAINT LOUIS UNIVERSITY · PI VINDIGNI, ALESSANDRO · 2014 to 2018
$1.4M
Cancer Research UK 15852NIGMS NIH HHS R01 GM108648NIGMS NIH HHS R01GM108648Wellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

RecQ helicases are a widely conserved family of ATP-dependent motors with diverse roles in nearly every aspect of bacterial and eukaryotic genome maintenance. However, the physical mechanisms by which RecQ helicases recognize and process specific DNA replication and repair intermediates are largely unknown. Here, we solved crystal structures of the human RECQ1 helicase in complexes with tailed-duplex DNA and ssDNA. The structures map the interactions of the ssDNA tail and the branch point along the helicase and Zn-binding domains, which, together with reported structures of other helicases, define the catalytic stages of helicase action. We also identify a strand-separating pin, which (uniquely in RECQ1) is buttressed by the protein dimer interface. A duplex DNA-binding surface on the C-terminal domain is shown to play a role in DNA unwinding, strand annealing, and Holliday junction (HJ) branch migration. We have combined EM and analytical ultracentrifugation approaches to show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in HJ recognition. This tetrameric arrangement suggests a platform for coordinated activity at the advancing and receding duplexes of an HJ during branch migration.

Indexed as

AnimalsChromatography, GelCrystallizationCrystallography, X-RayDNADNA, CruciformDNA HelicasesDNA, Single-StrandedEscherichia coliHumansInsectaMolecular ConformationNucleic Acid DenaturationNucleotidesProtein BindingProtein Structure, TertiaryDNADNA, CruciformDNA HelicasesDNA, Single-StrandedNucleotidesRecQ HelicasesRECQL protein, humanZincDNA helicasesfork reversalgenome stabilityHolliday junctionRecQ

Identifiers

PMID25831490
PMCPMC4394259
OpenAlexW1972610823

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.