Evidence map›Paper›PMID 33436806›Full record

ArticleScientific reports2021

Evolution of ribosomal protein network architectures.

Youri Timsit, Grégoire Sergeant-Perthuis, Daniel Bennequin

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 62 citations in OpenAlex.

  1. The cellular landscape of druggable RNA-binding proteins.Nature reviews. Drug discovery · 2026
    Review
  2. Article
  3. Review
  4. RiboScreenBiomedicines · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023
    Review
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 3 institutions in 1 country.

Youri TimsitMediterranean Institute of Oceanography UM 110, Aix-Marseille Université, CNRS, IRD, Campus de Luminy, Marseille, France. youri.timsit@mio.osupytheas.fr.
Grégoire Sergeant-PerthuisInstitut de Mathématiques de Jussieu - Paris Rive Gauche (IMJ-PRG), UMR 7586, CNRS, Université Paris Diderot, Paris, France.
Daniel BennequinInstitut de Mathématiques de Jussieu - Paris Rive Gauche (IMJ-PRG), UMR 7586, CNRS, Université Paris Diderot, Paris, France.
Institut de Mathématiques de Jussieu-Paris Rive Gauche · FRInstitut Méditerranéen d’Océanologie · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To perform an accurate protein synthesis, ribosomes accomplish complex tasks involving the long-range communication between its functional centres such as the peptidyl transfer centre, the tRNA bindings sites and the peptide exit tunnel. How information is transmitted between these sites remains one of the major challenges in current ribosome research. Many experimental studies have revealed that some r-proteins play essential roles in remote communication and the possible involvement of r-protein networks in these processes have been recently proposed. Our phylogenetic, structural and mathematical study reveals that of the three kingdom's r-protein networks converged towards non-random graphs where r-proteins collectively coevolved to optimize interconnection between functional centres. The massive acquisition of conserved aromatic residues at the interfaces and along the extensions of the newly connected eukaryotic r-proteins also highlights that a strong selective pressure acts on their sequences probably for the formation of new allosteric pathways in the network.

Indexed as

Evolution, MolecularProtein BiosynthesisProtein Interaction Domains and MotifsBinding SitesHumansModels, MolecularPhylogenyProtein ConformationRibosomal ProteinsRibosomesRNA, TransferRibosomal ProteinsRNA, Transfer

Identifiers

PMID33436806
PMCPMC7804294
OpenAlexW3119938933

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.