Evidence map›Paper›PMID 24913268›Full record

ArticleeLife2014

Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine.

Wilson Wong, Xiao-chen Bai, Alan Brown, Israel S Fernandez, Eric Hanssen, Melanie Condron, Yan Hong Tan, Jake Baum, Sjors H W Scheres

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 194 papers.

0numbers the graph read from it
0cells of the map it votes in
194citing papers in PubMed
14.0field-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

194 citing papers in PubMed, 364 citations in OpenAlex.

  1. Article
  2. Article
  3. Unpacking boxes: identification of novel inhibitors of malaria parasite invasion.International journal for parasitology. Drugs and drug resistance · 2026
    Article
  4. Article
  5. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
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134 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 at 2 institutions in 2 countries.

Wilson WongDivision of Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
Xiao-chen BaiStructural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Alan BrownStructural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Israel S FernandezStructural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Eric HanssenElectron Microscopy Unit, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia.
Melanie CondronDivision of Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
Yan Hong TanDivision of Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
Jake BaumDivision of Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.ORCID http://orcid.org/0000-0002-0275-352X
Sjors H W ScheresStructural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
The University of Melbourne · AUMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184332Medical Research Council MC_UP_A025_1013Wellcome Trust 100993Wellcome Trust 100993/Z/13/ZWellcome Trust WT096570
6 · The paper itself

Abstract

Malaria inflicts an enormous burden on global human health. The emergence of parasite resistance to front-line drugs has prompted a renewed focus on the repositioning of clinically approved drugs as potential anti-malarial therapies. Antibiotics that inhibit protein translation are promising candidates for repositioning. We have solved the cryo-EM structure of the cytoplasmic ribosome from the human malaria parasite, Plasmodium falciparum, in complex with emetine at 3.2 Å resolution. Emetine is an anti-protozoan drug used in the treatment of ameobiasis that also displays potent anti-malarial activity. Emetine interacts with the E-site of the ribosomal small subunit and shares a similar binding site with the antibiotic pactamycin, thereby delivering its therapeutic effect by blocking mRNA/tRNA translocation. As the first cryo-EM structure that visualizes an antibiotic bound to any ribosome at atomic resolution, this establishes cryo-EM as a powerful tool for screening and guiding the design of drugs that target parasite translation machinery.

Indexed as

AnimalsAntimalarialsBinding SitesCryoelectron MicroscopyCytoplasmDrug DesignEmetineErythrocytesHumansModels, MolecularPactamycinPlasmodium falciparumProtein BindingRibosomal ProteinsRibosomesRNA, MessengerAntimalarialsEmetinePactamycinRibosomal ProteinsRNA, Messengerbiophysicscryo-EMdrug developmentmalariaPlasmodium falciparumribosomestructural biology

Identifiers

PMID24913268
PMCPMC4086275
OpenAlexW2138390185

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.