The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
Open accessAbstract
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.
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MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950 · cited 4×
“5 Å compared to the native path of mRNA (Brodersen et al., 2000) thereby blocking mRNA/tRNA entry into the E-site during the translocation step of protein synthesis (Dinos et al.”
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Cited by
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
Barad, B. A., Echols, N., Wang, R. Y.-R., Cheng, Y., DiMaio, F., Adams, P. D., & Fraser, J. S. (2015) · Nature Methods · doi:10.1038/nmeth.3541 · Cited by 886
Repurposing approved drugs for cancer therapy
Schein, C. H. (2021) · British Medical Bulletin · doi:10.1093/bmb/ldaa045 · Cited by 78
DeepCryoPicker: fully automated deep neural network for single protein particle picking in cryo-EM
Al-Azzawi, A., Ouadou, A., Max, H., Duan, Y., Tanner, J. J., & Cheng, J. (2020) · BMC Bioinformatics · doi:10.1186/s12859-020-03809-7 · Cited by 74
Cryo-EM: the resolution revolution and drug discovery
de Oliveira, T. M., van Beek, L., Shilliday, F., Debreczeni, J. É., & Phillips, C. (2021) · SLAS DISCOVERY · doi:10.1177/2472555220960401 · Cited by 73
CryoDRGN-AI: neural ab initio reconstruction of challenging cryo-EM and cryo-ET datasets
Levy, A., Raghu, R., Feathers, J. R., Grzadkowski, M., Poitevin, F., Johnston, J. D., Vallese, F., Clarke, O. B., Wetzstein, G., & Zhong, E. D. (2025) · Nature Methods · doi:10.1038/s41592-025-02720-4 · Cited by 25
Metadata
- Authors
- Wong, W., Bai, X.-C., Brown, A., Fernandez, I. S., Hanssen, E., Condron, M., Tan, Y. H., Baum, J., & Scheres, S. H.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2014-06-09
- Volume
- 3
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W2138390185
- Cited by
- 351
- References
- 3
- FWCI
- 11.56
- Type
- journal article
- Language
- en
- Open access
- gold
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