Evidence map›Paper›PMID 17984320›Full record

ArticleThe Journal of cell biology2007

Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae.

Carolyn J Decker, Daniela Teixeira, Roy Parker

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 309 papers.

0numbers the graph read from it
0cells of the map it votes in
309citing papers in PubMed
10.6field-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

309 citing papers in PubMed, 479 citations in OpenAlex.

  1. Article
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  3. Assessment ofBio-protocol · 2026
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  17. Article
  18. Roles of P-body factors inbioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Review

249 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.

Carolyn J DeckerDepartment of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721.
Daniela Teixeira
Roy Parker
Howard Hughes Medical Institute · US

Funding

MUTANT GENE RESOURCEP40RR001183 · NCRR · JACKSON LABORATORY · PI DONAHUE, LEAH RAE B · 1985 to 2011
$16.3M
mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
NCRR NIH HHS P40 RR001183NCRR NIH HHS P41 RR1183NIGMS NIH HHS R37 GM045443NIGMS NIH HHS R37 GM45443
6 · The paper itself

Abstract

Processing bodies (P-bodies) are cytoplasmic RNA granules that contain translationally repressed messenger ribonucleoproteins (mRNPs) and messenger RNA (mRNA) decay factors. The physical interactions that form the individual mRNPs within P-bodies and how those mRNPs assemble into larger P-bodies are unresolved. We identify direct protein interactions that could contribute to the formation of an mRNP complex that consists of core P-body components. Additionally, we demonstrate that the formation of P-bodies that are visible by light microscopy occurs either through Edc3p, which acts as a scaffold and cross-bridging protein, or via the "prionlike" domain in Lsm4p. Analysis of cells defective in P-body formation indicates that the concentration of translationally repressed mRNPs and decay factors into microscopically visible P-bodies is not necessary for basal control of translation repression and mRNA decay. These results suggest a stepwise model for P-body assembly with the initial formation of a core mRNA-protein complex that then aggregates through multiple specific mechanisms.

Indexed as

AsparagineCytoplasmGlutamineModels, BiologicalOligonucleotidesProtein BiosynthesisProtein Structure, TertiaryRibonucleoproteinsRibonucleoprotein, U4-U6 Small NuclearRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesAsparagineEDC3 protein, S cerevisiaeGlutamineLSM4 protein, S cerevisiaemessenger ribonucleoproteinOligonucleotidesRibonucleoproteinsRibonucleoprotein, U4-U6 Small NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID17984320
PMCPMC2064791
OpenAlexW2146865209

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.