Evidence map›Paper›PMID 21045543›Full record

ReviewRNA biology

Roles of DEAD-box proteins in RNA and RNP Folding.

Cynthia Pan, Rick Russell

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  2. Article
  3. Review
  4. Substrate Specificities of DDX1: A Human DEAD-box protein.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Mitochondrial ribosome assembly in health and disease.Cell cycle (Georgetown, Tex.) · 2015
    Review
  17. Article
  18. RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014
    Review
  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

2 authors at 1 institution in 2 countries.

Cynthia PanDepartment of Chemistry and Biochemistry, University of Texas, Austin, TX, USA.
Rick Russell
Institut de Biologie Moléculaire et Cellulaire · FR

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

RNAs and RNA-protein complexes (RNPs) traverse rugged energy landscapes as they fold to their native structures, and many continue to undergo conformational rearrangements as they function. Due to the inherent stability of local RNA structure, proteins are required to assist with RNA conformational transitions during initial folding and in exchange between functional structures. DEAD-box proteins are superfamily 2 RNA helicases that are ubiquitously involved in RNA-mediated processes. Some of these proteins use an ATP-dependent cycle of conformational changes to disrupt RNA structure nonprocessively, accelerating structural transitions of RNAs and RNPs in a manner that bears a strong resemblance to the activities of certain groups of protein chaperones. This review summarizes recent work using model substrates and tractable self-splicing intron RNAs, which has given new insights into how DEAD-box proteins promote RNA folding steps and conformational transitions, and it summarizes recent progress in identifying sites and mechanisms of DEAD-box protein activity within more complex cellular targets.

Indexed as

DEAD-box RNA HelicasesHumansIntronsMolecular ChaperonesNucleic Acid ConformationProtein FoldingRibonucleoproteinsRNADEAD-box RNA HelicasesMolecular ChaperonesRibonucleoproteinsRNA

Identifiers

PMID21045543
PMCPMC3073326
OpenAlexW2068956147

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.