The DOI matches its Crossref record; 369 of the 369 references it cites were found in a registry or an index.
The A-Z of bacterial translation inhibitors
Abstract
Protein synthesis is one of the major targets in the cell for antibiotics. This review endeavors to provide a comprehensive "post-ribosome structure" A-Z of the huge diversity of antibiotics that target the bacterial translation apparatus, with an emphasis on correlating the vast wealth of biochemical data with more recently available ribosome structures, in order to understand function. The binding site, mechanism of action, and modes of resistance for 26 different classes of protein synthesis inhibitors are presented, ranging from ABT-773 to Zyvox. In addition to improving our understanding of the process of translation, insight into the mechanism of action of antibiotics is essential to the development of novel and more effective antimicrobial agents to combat emerging bacterial resistance to many clinically-relevant drugs.
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“Given that the RNA component of the ribosome plays a critical role in all stages of protein synthesis, translation inhibitors typically bind to rRNA, and consequentially, target-based antibiotic resistance mutations are often associated with discrete rRNA nucleotide changes (2).”
From Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors (2016) · cites this paper as [2]
In the citing paper
“Tetracyclines are broad-spectrum antibiotic agents that bind to elongating ribosomes and inhibit delivery of the ternary complex EF-Tu, GTP and aminoacylated-tRNA (EF-Tu•GTP•aa-tRNA) to the A-site (1).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [1]
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Cited by
Sorted by citations
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Self-citationRevisiting the structures of several antibiotics bound to the bacterial ribosome
Bulkley, D., Innis, C. A., Blaha, G., & Steitz, T. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008685107 · Cited by 308
The bacterial translation stress response.
Starosta, A. L., Lassak, J., Jung, K., & Wilson, D. N. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12083 · Cited by 210
Self-citationStructural basis for TetM-mediated tetracycline resistance
Dönhöfer, A., Franckenberg, S., Wickles, S., Berninghausen, O., Beckmann, R., & Wilson, D. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208037109 · Cited by 217
Self-citationRetapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome
Meydan, S., Marks, J., Klepacki, D., Sharma, V., Baranov, P. V., Firth, A. E., Margus, T., Kefi, A., Vázquez-Laslop, N., & Mankin, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.017 · Cited by 184
Jenner, L., Starosta, A. L., Terry, D. S., Mikolajka, A., Filonava, L., Yusupov, M., Blanchard, S. C., Wilson, D. N., & Yusupova, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216691110 · Cited by 204
Self-citationMarks, J., Kannan, K., Roncase, E. J., Klepacki, D., Kefi, A., Orelle, C., Vázquez-Laslop, N., & Mankin, A. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613055113 · Cited by 159
Target- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic
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Paternoga, H., Crowe-McAuliffe, C., Bock, L. V., Koller, T. O., Morici, M., Beckert, B., Myasnikov, A. G., Grubmüller, H., Nováček, J., & Wilson, D. N. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01047-y · Cited by 94
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Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA
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Metadata
- Authors
- Wilson, D. N.
- Affiliations
- Center for Integrated Protein Science Munich (DE)
- Corresponding author
- Wilson, Daniel N.
- ORCID
- Wilson, Daniel N.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 2009-11-20
- Volume
- 44
- Issue
- 6
- Pages
- 393-433
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2104276827
- Cited by
- 322
- References
- 369
- Citations by year
- 2026: 13 · 2025: 12 · 2024: 16 · 2023: 16 · 2022: 14 · 2021: 17 · 2020: 17 · 2019: 19 · 2018: 28 · 2017: 13 · 2016: 34 · 2015: 22 · 2014: 22 · 2013: 21 · 2012: 21
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Critical Reviews in Biochemistry and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
- Keywords
- translation inhibitors, antibiotics, bacterial translation, ribosome structure, protein synthesis inhibitors, antibiotic binding sites, mechanism of action, antibiotic resistance, antimicrobial drug development, ribosome-targeted antibiotics
- MeSH terms
- Animals, Anti-Bacterial Agents, Bacteria, Bacterial Proteins, Humans, Protein Binding, Protein Synthesis Inhibitors, Protein Biosynthesis, Gene Expression Regulation, Bacterial, Drug Resistance, Bacterial
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