Evidence map›Paper›PMID 25209664›Full record

ArticleNature2014

Structural basis for the inhibition of the eukaryotic ribosome.

Nicolas Garreau de Loubresse, Irina Prokhorova, Wolf Holtkamp, Marina V Rodnina, Gulnara Yusupova, Marat Yusupov

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 300 papers.

0numbers the graph read from it
0cells of the map it votes in
300citing papers in PubMed
16.5field-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

300 citing papers in PubMed, 562 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
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  11. Review
  12. Article
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  15. Article
  16. Article
  17. Asymmetric Total Synthesis of (-)-Verrucarol.Angewandte Chemie (International ed. in English) · 2026
    Article
  18. Article
  19. Article
  20. Article

240 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Nicolas Garreau de LoubresseInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), INSERM U964, CNRS UMR7104, Université de Strasbourg, 67404, Illkirch, France.
Irina ProkhorovaInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), INSERM U964, CNRS UMR7104, Université de Strasbourg, 67404, Illkirch, France.
Wolf HoltkampDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Gulnara YusupovaInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), INSERM U964, CNRS UMR7104, Université de Strasbourg, 67404, Illkirch, France.
Marat YusupovInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), INSERM U964, CNRS UMR7104, Université de Strasbourg, 67404, Illkirch, France.
Institut de génétique et de biologie moléculaire et cellulaire · FRMax Planck Institute for Biophysical Chemistry · DEUniversité de Strasbourg · FR

Funding

European Research Council 294312
6 · The paper itself

Abstract

The ribosome is a molecular machine responsible for protein synthesis and a major target for small-molecule inhibitors. Compared to the wealth of structural information available on ribosome-targeting antibiotics in bacteria, our understanding of the binding mode of ribosome inhibitors in eukaryotes is currently limited. Here we used X-ray crystallography to determine 16 high-resolution structures of 80S ribosomes from Saccharomyces cerevisiae in complexes with 12 eukaryote-specific and 4 broad-spectrum inhibitors. All inhibitors were found associated with messenger RNA and transfer RNA binding sites. In combination with kinetic experiments, the structures suggest a model for the action of cycloheximide and lactimidomycin, which explains why lactimidomycin, the larger compound, specifically targets the first elongation cycle. The study defines common principles of targeting and resistance, provides insights into translation inhibitor mode of action and reveals the structural determinants responsible for species selectivity which could guide future drug development.

Indexed as

Base SequenceBinding SitesCrystallography, X-RayCycloheximideDrug ResistanceEukaryotic CellsKineticsMacrolidesModels, MolecularMolecular Targeted TherapyMolecular WeightPeptide Chain Elongation, TranslationalPeptidyl TransferasesPiperidonesProtein Synthesis InhibitorsRibosomesCycloheximidelactimidomycinMacrolidesPeptidyl TransferasesPiperidonesProtein Synthesis InhibitorsRNA, MessengerRNA, Transfer

Identifiers

PMID25209664
OpenAlexW2013779315

What OpenQuestion holds

Textmetadata
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.