Evidence map›Paper›PMID 24357410›Full record

ArticleNucleic acids research2014

Nucleolar proteins Bfr2 and Enp2 interact with DEAD-box RNA helicase Dbp4 in two different complexes.

Sahar Soltanieh, Martin Lapensée, François Dragon

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. RiboCop surveils pre-rRNA processing by Dicer in cellular quiescence.bioRxiv : the preprint server for biology · 2025
    Article
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  4. HumanFrontiers in genetics · 2023
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  7. Article
  8. Article
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  14. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  15. Review
  16. Article
  17. Article
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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.

Sahar SoltaniehDépartement des sciences biologiques and Centre de recherche BioMed, Université du Québec à Montréal, Montréal, Québec, Canada.
Martin Lapensée
François Dragon
Université du Québec à Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Different pre-ribosomal complexes are formed during ribosome biogenesis, and the composition of these complexes is highly dynamic. Dbp4, a conserved DEAD-box RNA helicase implicated in ribosome biogenesis, interacts with nucleolar proteins Bfr2 and Enp2. We show that, like Dbp4, Bfr2 and Enp2 are required for the early processing steps leading to the production of 18S ribosomal RNA. We also found that Bfr2 and Enp2 associate with the U3 small nucleolar RNA (snoRNA), the U3-specific protein Mpp10 and various pre-18S ribosomal RNA species. Thus, we propose that Bfr2, Dbp4 and Enp2 are components of the small subunit (SSU) processome, a large complex of ∼80S. Sucrose gradient sedimentation analyses indicated that Dbp4, Bfr2 and Enp2 sediment in a peak of ∼50S and in a peak of ∼80S. Bfr2, Dbp4 and Enp2 associate together in the 50S complex, which does not include the U3 snoRNA; however, they associate with U3 snoRNA in the 80S complex (SSU processome). Immunoprecipitation experiments revealed that U14 snoRNA associates with Dbp4 in the 50S complex, but not with Bfr2 or Enp2. The assembly factor Tsr1 is not part of the '50S' complex, indicating this complex is not a pre-40S ribosome. A combination of experiments leads us to propose that Bfr2, Enp2 and Dbp4 are recruited at late steps during assembly of the SSU processome.

Indexed as

RNA Processing, Post-TranscriptionalDEAD-box RNA HelicasesNuclear ProteinsPhosphoproteinsRibonucleoproteinsRNA NucleotidyltransferasesRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiae ProteinsBFR2 protein, S cerevisiaeDEAD-box RNA HelicasesHCA4 protein, S cerevisiaeMPP10 protein, S cerevisiaeNuclear ProteinsPhosphoproteinsRibonucleoproteinsRNA NucleotidyltransferasesRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID24357410
PMCPMC3950691
OpenAlexW2020237198

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.