ArticleProceedings of the National Academy of Sciences of the United States of America2025
Mechanism of read-through enhancement by aminoglycosides and mefloquine.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- RiboScreenBiomedicines · 2026Review
- ENSURE: the encyclopedia of suppressor tRNA with an AI assistant.Nucleic acids research · 2026Article
- Innovative application of mefloquine and Methacycline in combating Tet(X3/X4)-positive Escherichia coli infections.BMC microbiology · 2025Article
- Translational readthrough therapy for ADPKD induces polycystin1 expression and partially rescues functional deficits in PKD1 mutant cells.Scientific reports · 2025Article
- Evolution of ribosome X-ray crystallography: from first crystals to atomic resolution.Biophysical reviews · 2025Review
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Authors and funding
13 authors.
Funding
Abstract
Nonsense mutations are associated with numerous and diverse pathologies, yet effective treatment strategies remain elusive. A promising approach to combat these conditions involves the use of aminoglycosides, particularly in combination with stop-codon read-through enhancers, for developing drugs that can rescue the production of full-length proteins. Using X-ray crystallography and single-particle cryo-EM, we obtained structures of the eukaryotic ribosome in complexes with several aminoglycosides (geneticin G418, paromomycin, and hygromycin B) and the antimalarial drug mefloquine (MFQ), which has also been identified as a read-through enhancer. Our study reveals a binding site of MFQ, which holds significant promise for the development of therapies targeting premature termination codon-related genetic and oncological diseases. The results underscore the crucial role of the bridge B7b/c in mediating the effects of MFQ on subunit rotation dynamics. Through a comprehensive analysis of the interactions between the drugs and the eukaryotic ribosome, we propose a unifying hypothesis for read-through enhancement by small molecules, highlighting the role of decoding center rearrangements and intersubunit rotation dynamics.
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