Evidence map›Paper›PMID 18162578›Full record

ArticleMolecular biology of the cell2008

The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies.

Carla Beckham, Angela Hilliker, Anne-Marie Cziko, Amine Noueiry, Mani Ramaswami, Roy Parker

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

68 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023
    Review
  11. Rapid Cryopurification of the Yeast Mitochondrial Ribosome.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. TheGenes · 2021
    Article
  19. Review
  20. Article

8 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Carla BeckhamDepartment of Cell Biology and Anatomy, University of Arizona, Tucson, AZ 85721-0206, USA.
Angela Hilliker
Anne-Marie Cziko
Amine Noueiry
Mani Ramaswami
Roy Parker
Howard Hughes Medical Institute · USSociety for Neuroscience · USUniversity of Arizona · USWest Virginia University · US

Funding

Stress Granules in Yeast and MammalsR01GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 1991 to 2021
$3.3M
mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
Fos, Jun &synaptic plasticityR01DA015495 · NIDA · UNIVERSITY OF ARIZONA · PI BOSCO, GIOVANNI · 2003 to 2007
$1.9M
Fos, Jun &Transcriptional Control of Synaptic PlasticityK02DA017749 · NIDA · UNIVERSITY OF ARIZONA · PI RAMASWAMI, MANI · 2004 to 2007
$306k
Howard Hughes Medical InstituteNIDA NIH HHS DA15495NIDA NIH HHS DA17749NIDA NIH HHS K02 DA017749NIDA NIH HHS R01 DA015495NIGMS NIH HHS GM45443NIGMS NIH HHS R01 GM045443NIGMS NIH HHS R37 GM045443
6 · The paper itself

Abstract

Recent results suggest that cytoplasmic mRNAs can form translationally repressed messenger ribonucleoprotein particles (mRNPs) capable of decapping and degradation, or accumulation into cytoplasmic processing bodies (P-bodies), which can function as sites of mRNA storage. The proteins that function in transitions between the translationally repressed mRNPs that accumulate in P-bodies and mRNPs engaged in translation are largely unknown. Herein, we demonstrate that the yeast translation initiation factor Ded1p can localize to P-bodies. Moreover, depletion of Ded1p leads to defects in P-body formation. Overexpression of Ded1p results in increased size and number of P-bodies and inhibition of growth in a manner partially suppressed by loss of Pat1p, Dhh1p, or Lsm1p. Mutations that inactivate the ATPase activity of Ded1p increase the overexpression growth inhibition of Ded1p and prevent Ded1p from localizing in P-bodies. Combined with earlier work showing Ded1p can have a positive effect on translation, these results suggest that Ded1p is a bifunctional protein that can affect both translation initiation and P-body formation.

Indexed as

Adenosine TriphosphateAnimalsChemical FractionationCytoplasmic StructuresDEAD-box RNA HelicasesDrosophilaGene DeletionGreen Fluorescent ProteinsHydrolysisProtein BiosynthesisProtein TransportRecombinant Fusion ProteinsRibonucleoproteinsRibosomesRNA StabilitySaccharomyces cerevisiaeAdenosine TriphosphateDEAD-box RNA HelicasesDED1 protein, S cerevisiaeGreen Fluorescent ProteinsRecombinant Fusion ProteinsRibonucleoproteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID18162578
PMCPMC2262982
OpenAlexW2131197002

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.