Evidence map›Paper›PMID 36951107›Full record

ArticleNucleic acids research2023

Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution.

Simone Pellegrino, Kyle C Dent, Tobias Spikes, Alan J Warren

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Small nucleolar RNAs: the hidden precursors of cancer ribosomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Analysis of RNA and Its Modifications.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024
    Review
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Simone PellegrinoDepartment of Haematology, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.ORCID 0000-0001-6302-2774
Kyle C DentDepartment of Haematology, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.
Tobias SpikesDepartment of Haematology, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.
Alan J WarrenDepartment of Haematology, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.ORCID 0000-0001-9277-4553
Wellcome/MRC Cambridge Stem Cell Institute · GB

Funding

Medical Research Council MC_U105161083Medical Research Council MR/T012412/1Wellcome TrustWellcome Trust 202905/Z/16/ZWellcome Trust 206171/Z/17/Z
6 · The paper itself

Abstract

The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialisation in development and disease. However, the inability to accurately visualise these modifications has limited mechanistic understanding of the role of these modifications in ribosome function. Here we report the 2.15 Å resolution cryo-EM reconstruction of the human 40S ribosomal subunit. We directly visualise post-transcriptional modifications within the 18S rRNA and four post-translational modifications of ribosomal proteins. Additionally, we interpret the solvation shells in the core regions of the 40S ribosomal subunit and reveal how potassium and magnesium ions establish both universally conserved and eukaryote-specific coordination to promote the stabilisation and folding of key ribosomal elements. This work provides unprecedented structural details for the human 40S ribosomal subunit that will serve as an important reference for unravelling the functional role of ribosomal RNA modifications.

Indexed as

Ribosomal ProteinsRibosome Subunits, Small, EukaryoticCryoelectron MicroscopyHumansRibosomesRNA, RibosomalRNA, Ribosomal, 18SRibosomal ProteinsRNA, RibosomalRNA, Ribosomal, 18S

Identifiers

PMID36951107
PMCPMC10164566
OpenAlexW4353112023

What OpenQuestion holds

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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.