Evidence map›Paper›PMID 19632996›Full record

ArticleThe Journal of biological chemistry2009

Bloom syndrome helicase stimulates RAD51 DNA strand exchange activity through a novel mechanism.

Dmitry V Bugreev, Olga M Mazina, Alexander V Mazin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The RecD2 helicase balances RecA activities.Nucleic acids research · 2022
    Article
  9. Article
  10. Review
  11. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Eukaryotic resectosomes: A single-molecule perspective.Progress in biophysics and molecular biology · 2017
    Review
  18. Review
  19. Review
  20. 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

3 authors at 2 institutions in 2 countries.

Dmitry V BugreevDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102-1192, USA.
Olga M Mazina
Alexander V Mazin
Drexel University · USInstitute of Chemical Biology and Fundamental Medicine · RU

Funding

Repair of DNA breaks in human: the role of Rad54 proteinR01CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2003 to 2013
$2.6M
Repair of DNA breaks in humans: the role of Rad54 proteinR56CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2008 to 2008
$260k
A Screen for Modulators of Human Rad51, a Key DNA Repair ProteinR03MH084119 · NIMH · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2008 to 2008
$25k
NCI NIH HHS CA100839NCI NIH HHS R01 CA100839NCI NIH HHS R56 CA100839NIMH NIH HHS MH084119NIMH NIH HHS R03 MH084119
6 · The paper itself

Abstract

Loss or inactivation of BLM, a helicase of the RecQ family, causes Bloom syndrome, a genetic disorder with a strong predisposition to cancer. Although the precise function of BLM remains unknown, genetic data has implicated BLM in the process of genetic recombination and DNA repair. Previously, we demonstrated that BLM can disrupt the RAD51-single-stranded DNA filament that promotes the initial steps of homologous recombination. However, this disruption occurs only if RAD51 is present in an inactive ADP-bound form. Here, we investigate interactions of BLM with the active ATP-bound form of the RAD51-single-stranded DNA filament. Surprisingly, we found that BLM stimulates DNA strand exchange activity of RAD51. In contrast to the helicase activity of BLM, this stimulation does not require ATP hydrolysis. These data suggest a novel BLM function that is stimulation of the RAD51 DNA pairing. Our results demonstrate the important role of the RAD51 nucleoprotein filament conformation in stimulation of DNA pairing by BLM.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBase PairingCalciumDNADNA-Binding ProteinsDNA HelicasesDNA RepairDNA, Single-StrandedHumansModels, GeneticMutationNuclear ProteinsNucleic Acid ConformationRad51 RecombinaseRecombination, GeneticAdenosine TriphosphatasesAdenosine TriphosphateBloom syndrome proteinCalciumDNADNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedNuclear ProteinsRad51 RecombinaseRAD54L protein, humanRecQ Helicases

Identifiers

PMID19632996
PMCPMC2786030
OpenAlexW2054678629

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.