Evidence map›Paper›PMID 25653156›Full record

ArticleNucleic acids research2015

Insights into the mechanism of a G-quadruplex-unwinding DEAH-box helicase.

Michael C Chen, Pierre Murat, Keren Abecassis, Adrian R Ferré-D'Amaré, Shankar Balasubramanian

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Structure-based insights into fluorogenic RNA aptamers.Acta biochimica et biophysica Sinica · 2024
    Review
  9. Article
  10. DHX36 maintains genomic integrity by unwinding G-quadruplexes.Genes to cells : devoted to molecular & cellular mechanisms · 2023
    Article
  11. Article
  12. Review
  13. Non-G Base Tetrads.Molecules (Basel, Switzerland) · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

5 authors.

Michael C ChenDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK National Heart, Lung and Blood Institute, 50 South Drive, MSC-8012, Bethesda, MD 20892-8012, USA.
Pierre MuratDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Keren AbecassisDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Adrian R Ferré-D'AmaréNational Heart, Lung and Blood Institute, 50 South Drive, MSC-8012, Bethesda, MD 20892-8012, USA adrian.ferre@nih.gov.
Shankar BalasubramanianDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK Cancer Research UK Cambridge Institute, Li Ka Shing Centre, Cambridge, UK sb10031@cam.ac.uk.

Funding

RNA: Tools for Cell BiologyZIAHL006188 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2014 to 2025
$9.5M
Cancer Research UK 11961Intramural NIH HHS
6 · The paper itself

Abstract

The unwinding of nucleic acid secondary structures within cells is crucial to maintain genomic integrity and prevent abortive transcription and translation initiation. DHX36, also known as RHAU or G4R1, is a DEAH-box ATP-dependent helicase highly specific for DNA and RNA G-quadruplexes (G4s). A fundamental mechanistic understanding of the interaction between helicases and their G4 substrates is important to elucidate G4 biology and pave the way toward G4-targeted therapies. Here we analyze how the thermodynamic stability of G4 substrates affects binding and unwinding by DHX36. We modulated the stability of the G4 substrates by varying the sequence and the number of G-tetrads and by using small, G4-stabilizing molecules. We found an inverse correlation between the thermodynamic stability of the G4 substrates and rates of unwinding by DHX36. In stark contrast, the ATPase activity of the helicase was largely independent of substrate stability pointing toward a decoupling mechanism akin to what has been observed for many double-stranded DEAD-box RNA helicases. Our study provides the first evidence that DHX36 uses a local, non-processive mechanism to unwind G4 substrates, reminiscent of that of eukaryotic initiation factor 4A (eIF4A) on double-stranded substrates.

Indexed as

G-QuadruplexesAdenosine TriphosphateDEAD-box RNA HelicasesLigandsTemperatureAdenosine TriphosphateDEAD-box RNA HelicasesLigands

Identifiers

PMID25653156
PMCPMC4344499

What OpenQuestion holds

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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.