Evidence map›Paper›PMID 20168331›Full record

ArticleEMBO reports2010

Structural basis for the function of DEAH helicases.

Yangzi He, Gregers R Andersen, Klaus H Nielsen

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

73 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  3. Review
  4. Article
  5. Crystal structures of the DExH-box RNA helicase DHX9.Acta crystallographica. Section D, Structural biology · 2023
    Article
  6. Crystal structure of Prp16 in complex with ADP.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  7. Review
  8. Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021
    Article
  18. DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021
    Review
  19. Article
  20. Article

13 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

3 authors at 1 institution in 1 country.

Yangzi HeDepartment of Molecular Biology, Aarhus University, Aarhus, Denmark.
Gregers R Andersen
Klaus H Nielsen
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.

Indexed as

Alternative SplicingAdenosine TriphosphateBinding SitesCrystallography, X-RayDEAD-box RNA HelicasesDNA HelicasesModels, MolecularMolecular ConformationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRNARNA, MessengerRNA SplicingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDEAD-box RNA HelicasesDNA HelicasesPRP43 protein, S cerevisiaeRNARNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID20168331
PMCPMC2838688
OpenAlexW2004838350

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.