Evidence map›Paper›PMID 24151078›Full record

ArticleThe Journal of biological chemistry2013

Binding of G-quadruplexes to the N-terminal recognition domain of the RNA helicase associated with AU-rich element (RHAU).

Markus Meier, Trushar R Patel, Evan P Booy, Oksana Marushchak, Natalie Okun, Soumya Deo, Ryan Howard, Kevin McEleney, Stephen E Harding, Jörg Stetefeld and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Specific binding of G-quadruplex in SARS-CoV-2 RNA by RHAU peptide.Current research in structural biology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Creation and resolution of non-B-DNA structural impediments during replication.Critical reviews in biochemistry and molecular biology · 2022
    Article
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  12. Article
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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 at 2 institutions in 2 countries.

Markus MeierFrom the Departments of Chemistry and.
Trushar R Patel
Evan P Booy
Oksana Marushchak
Natalie Okun
Soumya Deo
Ryan Howard
Kevin McEleney
Stephen E Harding
Jörg Stetefeld
Sean A McKenna
University of Manitoba · CAUniversity of Nottingham · GB

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Polynucleotides containing consecutive tracts of guanines can adopt an intramolecular G-quadruplex structure where multiple planar tetrads of hydrogen-bound guanines stack on top of each other. Remodeling of G-quadruplexes impacts numerous aspects of nucleotide biology including transcriptional and translational control. RNA helicase associated with AU-rich element (RHAU), a member of the ATP-dependent DEX(H/D) family of RNA helicases, has been established as a major cellular quadruplex resolvase. RHAU contains a core helicase domain responsible for ATP binding/hydrolysis/helicase activity and is flanked on either side by N- and C-terminal extensions. The N-terminal extension is required for quadruplex recognition, and we have previously demonstrated complex formation between this domain and a quadruplex from human telomerase RNA. Here we used an integrated approach that includes small angle x-ray scattering, nuclear magnetic resonance spectroscopy, circular dichroism, and dynamic light scattering methods to demonstrate the recognition of G-quadruplexes by the N-terminal domain of RHAU. Based on our results, we conclude that (i) quadruplex from the human telomerase RNA and its DNA analog both adopt a disc shape in solution, (ii) RHAU53-105 adopts a defined and extended conformation in solution, and (iii) the N-terminal domain mediates an interaction with a guanine tetrad face of quadruplexes. Together, these data form the foundation for understanding the recognition of quadruplexes by the N-terminal domain of RHAU.

Indexed as

G-QuadruplexesAmino Acid SequenceAU Rich ElementsBase SequenceBinding SitesCircular DichroismDEAD-box RNA HelicasesHumansModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationPeptide FragmentsProtein ConformationProtein Structure, TertiaryRecombinant ProteinsDEAD-box RNA HelicasesDHX36 protein, humanPeptide FragmentsRecombinant ProteinsRNATelomerasetelomerase RNADHX36DNA HelicaseG4R1G-quadruplexRHAURNA-binding ProteinRNA HelicaseRNA-Protein InteractionX-ray Scattering

Identifiers

PMID24151078
PMCPMC3853254
OpenAlexW1979433605

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.