Evidence map›Paper›PMID 15990871›Full record

ArticleThe EMBO journal2005

The HRDC domain of BLM is required for the dissolution of double Holliday junctions.

Leonard Wu, Kok Lung Chan, Christine Ralf, Douglas A Bernstein, Patrick L Garcia, Vilhelm A Bohr, Alessandro Vindigni, Pavel Janscak, James L Keck, Ian D Hickson

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

102 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  6. Review
  7. Article
  8. Article
  9. Frontiers in plant science · 2023
    Article
  10. Article
  11. The convergence of head-on DNA unwinding forks induces helicase oligomerization and activity transition.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. Review

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

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

10 authors at 6 institutions in 4 countries.

Leonard WuCancer Research UK Laboratories, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford, UK.
Kok Lung Chan
Christine Ralf
Douglas A Bernstein
Patrick L Garcia
Vilhelm A Bohr
Alessandro Vindigni
Pavel Janscak
James L Keck
Ian D Hickson
Cancer Research UK · GBUniversity of Oxford · GBUniversity of Wisconsin–Madison · USUniversity of Zurich · CHInternational Centre for Genetic Engineering and Biotechnology · ITNational Institutes of Health · US

Funding

Function of RecQ helicases in genome stabilityZIAAG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT · 2009 to 2025
$13.1M
Function of RecQ helicases in genome stabilityZ01AG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 1993 to 2008
$2.9M
6 · The paper itself

Abstract

Bloom's syndrome is a hereditary cancer-predisposition disorder resulting from mutations in the BLM gene. In humans, BLM encodes one of five members of the RecQ helicase family. One function of BLM is to act in concert with topoisomerase IIIalpha (TOPO IIIalpha) to resolve recombination intermediates containing double Holliday junctions by a process called double Holliday junction dissolution, herein termed dissolution. Here, we show that dissolution is highly specific for BLM among human RecQ helicases and critically depends upon a functional HRDC domain in BLM. We show that the HRDC domain confers DNA structure specificity, and is required for the efficient binding to and unwinding of double Holliday junctions, but not for the unwinding of a simple partial duplex substrate. Furthermore, we show that lysine-1270 of BLM, which resides in the HRDC domain and is predicted to play a role in mediating interactions with DNA, is required for efficient dissolution.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBloom SyndromeDNA, CruciformDNA HelicasesHumansLysineMolecular Sequence DataProtein Structure, TertiaryRecQ HelicasesSequence Analysis, ProteinAdenosine TriphosphatasesBloom syndrome proteinDNA, CruciformDNA HelicasesLysineRecQ Helicases

Identifiers

PMID15990871
PMCPMC1176466
OpenAlexW2151037827

What OpenQuestion holds

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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.