The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
How Macrolide Antibiotics Work
Open accessAbstract
Macrolide antibiotics inhibit protein synthesis by targeting the bacterial ribosome. They bind at the nascent peptide exit tunnel and partially occlude it. Thus, macrolides have been viewed as ‘tunnel plugs’ that stop synthesis of every protein. More recent evidence, however, demonstrates that macrolides selectively inhibit translation of a subset of cellular proteins and that their action critically depends on the nascent protein sequence and on the antibiotic structure. Therefore, macrolides emerge as modulators of translation rather than global inhibitors of protein synthesis. The context-specific action of macrolides is the basis for regulation of the expression of resistance genes. Understanding the details of the mechanism of macrolide action may inform rational design of new drugs and unveil important principles of translation regulation.
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Cites
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
Ribosome-targeting antibiotics and mechanisms of bacterial resistance
Wilson, D. N. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3155 · Cited by 1,054
Molecular Mechanism of Drug-Dependent Ribosome Stalling
Vazquez-Laslop, N., Thum, C., & Mankin, A. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.026 · Cited by 260
Self-citationSequence selectivity of macrolide-induced translational attenuation
Davis, A. R., Gohara, D. W., & Yap, M.-N. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410356111 · Cited by 123
Cited by
Molecular mechanisms of antibiotic resistance revisited
Darby, E. M., Trampari, E., Siasat, P., Gaya, M. S., Alav, I., Webber, M. A., & Blair, J. M. A. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00820-y · Cited by 1,398
Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel
Osterman, I. A., Wieland, M., Maviza, T. P., Lashkevich, K. A., Lukianov, D. A., Komarova, E. S., Zakalyukina, Y. V., Buschauer, R., Shiriaev, D. I., Leyn, S. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0578-x · Cited by 75
Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs
Leroy, E. C., Perry, T. N., Renault, T. T., & Innis, C. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01343-0 · Cited by 22
Structural insights into context-specific inhibition of bacterial translation by macrolides
Syroegin, E. A., Aleksandrova, E. V., Kruglov, A. A., Paranjpe, M. N., Svetlov, M. S., & Polikanov, Y. S. (2025) · Nature Communications · doi:10.1038/s41467-025-64692-5 · Cited by 8
Metadata
- Authors
- Vázquez-Laslop, N., & Mankin, A. S.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2018-09
- Volume
- 43
- Issue
- 9
- Pages
- 668-684
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2883557242
- Cited by
- 410
- References
- 4
- FWCI
- 2.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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