Evidence map›Paper›PMID 24635478›Full record

ReviewAnnual review of biochemistry2014

RNA helicase proteins as chaperones and remodelers.

Inga Jarmoskaite, Rick Russell

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

158 citing papers in PubMed, 264 citations in OpenAlex.

  1. In Vitro Assay of Bacterial RNA Helicases Liquid-Liquid Phase Separation.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  3. Article
  4. Review
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  10. LOTUS-domain proteins activate Vasa to drive germ granule assembly.bioRxiv : the preprint server for biology · 2026
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

98 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

2 authors at 1 institution in 1 country.

Inga JarmoskaiteDepartment of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712; email: i_jarmoskaite@utexas.edu , rick_russell@cm.utexas.edu.
Rick Russell
The University of Texas at Austin · US

Funding

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 GM070456NIGMS NIH HHS R01 GM070456
6 · The paper itself

Abstract

Superfamily 2 helicase proteins are ubiquitous in RNA biology and have an extraordinarily broad set of functional roles. Central among these roles are the promotion of rearrangements of structured RNAs and the remodeling of ribonucleoprotein complexes (RNPs), allowing formation of native RNA structure or progression through a functional cycle of structures. Although all superfamily 2 helicases share a conserved helicase core, they are divided evolutionarily into several families, and it is principally proteins from three families, the DEAD-box, DEAH/RHA, and Ski2-like families, that function to manipulate structured RNAs and RNPs. Strikingly, there are emerging differences in the mechanisms of these proteins, both between families and within the largest family (DEAD-box), and these differences appear to be tuned to their RNA or RNP substrates and their specific roles. This review outlines basic mechanistic features of the three families and surveys individual proteins and the current understanding of their biological substrates and mechanisms.

Indexed as

G-QuadruplexesAlternative SplicingCatalysisDNA HelicasesEscherichia coliHumansIntronsMolecular ChaperonesProtein BiosynthesisProtein Structure, SecondaryProtein Structure, TertiaryRibonucleoproteins, Small NuclearRibosomesRNARNA HelicasesRNA SplicingDNA HelicasesMolecular ChaperonesRibonucleoproteins, Small NuclearRNARNA HelicasesATPaseRNA foldingRNA structureRNA unwindingself-splicing intron

Identifiers

PMID24635478
PMCPMC4143424
OpenAlexW2125655241

What OpenQuestion holds

Textmetadata
LicenceTDM
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.