Evidence map›Paper›PMID 29459436›Full record

ArticleThe EMBO journal2018

Structure of a eukaryotic cytoplasmic pre-40S ribosomal subunit.

Alain Scaiola, Cohue Peña, Melanie Weisser, Daniel Böhringer, Marc Leibundgut, Purnima Klingauf-Nerurkar, Stefan Gerhardy, Vikram Govind Panse, Nenad Ban

Abstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
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

63 citing papers in PubMed.

  1. Article
  2. Many paths to destruction: Family-specific turnover and stress responses for tRNA introns.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  20. Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023
    Review

3 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

9 authors.

Alain ScaiolaDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Cohue PeñaDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Melanie WeisserDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Daniel BöhringerDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Marc LeibundgutDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Purnima Klingauf-NerurkarDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Stefan GerhardyInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Vikram Govind PanseInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland vpanse@imm.uzh.ch ban@mol.biol.ethz.ch.ORCID 0000-0002-4770-7068
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland vpanse@imm.uzh.ch ban@mol.biol.ethz.ch.ORCID 0000-0002-9527-210X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Final maturation of eukaryotic ribosomes occurs in the cytoplasm and requires the sequential removal of associated assembly factors and processing of the immature 20S pre-RNA Using cryo-electron microscopy (cryo-EM), we have determined the structure of a yeast cytoplasmic pre-40S particle in complex with Enp1, Ltv1, Rio2, Tsr1, and Pno1 assembly factors poised to initiate final maturation. The structure reveals that the pre-rRNA adopts a highly distorted conformation of its 3' major and 3' minor domains stabilized by the binding of the assembly factors. This observation is consistent with a mechanism that involves concerted release of the assembly factors orchestrated by the folding of the rRNA in the head of the pre-40S subunit during the final stages of maturation. Our results provide a structural framework for the coordination of the final maturation events that drive a pre-40S particle toward the mature form capable of engaging in translation.

Indexed as

Cryoelectron MicroscopyMolecular Docking SimulationCytoplasmNuclear ProteinsProtein ConformationProtein DomainsProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesRibosomal ProteinsRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsRNA FoldingRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsENP1 protein, S cerevisiaeLTV1 protein, S cerevisiaeNOB1 protein, S cerevisiaeNuclear ProteinsPNO1 protein, S cerevisiaeProtein Serine-Threonine KinasesRibosomal ProteinsRio2 protein, S cerevisiaeRNA-Binding ProteinsRNA, RibosomalRPS21A protein, S cerevisiaeSaccharomyces cerevisiae Proteinscryo‐EMpre‐40S ribosomeribosomeribosome assemblyribosome biogenesis

Identifiers

PMID29459436
PMCPMC5881545

What OpenQuestion holds

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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.