Evidence map›Paper›PMID 29150525›Full record

ReviewBiochemical Society transactions2017

Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs.

Benjamin Gilman, Pilar Tijerina, Rick Russell

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Functions and mechanisms of RNA helicases in plants.Journal of experimental botany · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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.

Benjamin GilmanDepartment of Molecular Biosciences and the Institute for Cellular & Molecular Biology, University of Texas at Austin, Austin, TX 78712, U.S.A.
Pilar TijerinaDepartment of Molecular Biosciences and the Institute for Cellular & Molecular Biology, University of Texas at Austin, Austin, TX 78712, U.S.A.
Rick RussellDepartment of Molecular Biosciences and the Institute for Cellular & Molecular Biology, University of Texas at Austin, Austin, TX 78712, U.S.A. rick_russell@cm.utexas.edu.

Funding

Time-resolved small angle X-ray scatteringP01GM066275 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2003 to 2017
$17.8M
Physical and functional probing of DEAD-box proteins as general RNA chaperonesR01GM070456 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI RUSSELL, RICK · 2004 to 2017
$3.6M
NIGMS NIH HHS P01 GM066275NIGMS NIH HHS R01 GM070456
6 · The paper itself

Abstract

Structured RNAs and RNA-protein complexes (RNPs) fold through complex pathways that are replete with misfolded traps, and many RNAs and RNPs undergo extensive conformational changes during their functional cycles. These folding steps and conformational transitions are frequently promoted by RNA chaperone proteins, notably by superfamily 2 (SF2) RNA helicase proteins. The two largest families of SF2 helicases, DEAD-box and DEAH-box proteins, share evolutionarily conserved helicase cores, but unwind RNA helices through distinct mechanisms. Recent studies have advanced our understanding of how their distinct mechanisms enable DEAD-box proteins to disrupt RNA base pairs on the surfaces of structured RNAs and RNPs, while some DEAH-box proteins are adept at disrupting base pairs in the interior of RNPs. Proteins from these families use these mechanisms to chaperone folding and promote rearrangements of structured RNAs and RNPs, including the spliceosome, and may use related mechanisms to maintain cellular messenger RNAs in unfolded or partially unfolded conformations.

Indexed as

Nucleic Acid ConformationProtein ConformationRibonucleoproteinsRNARNA HelicasesRibonucleoproteinsRNARNA HelicaseshelicaseRNA structureself-splicing intronsplicingunwinding

Identifiers

PMID29150525
PMCPMC5960804

What OpenQuestion holds

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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.