ArticleCell reports2016
Binding of Macrolide Antibiotics Leads to Ribosomal Selection against Specific Substrates Based on Their Charge and Size.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed.
- Macrolide antibiotic action, resistance, and tolerance, and approaches to improve their activity against Gram-negative bacteria.The Journal of antibiotics · 2026Review
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- A streamlined, nanopore-compatible 5PSeq protocol for rapid phenotypic antimicrobial sensitivity testing.Cell reports methods · 2026Article
- Structural insights into context-specific inhibition of bacterial translation by macrolides.Nature communications · 2025Article
- Antechodynamics and Antechokinetics: Dynamics and Kinetics of Antibiotic Resistance Biomolecules.Biomolecules · 2025Review
- Macrolones target bacterial ribosomes and DNA gyrase and can evade resistance mechanisms.Nature chemical biology · 2024Article
- Riboformer: a deep learning framework for predicting context-dependent translation dynamics.Nature communications · 2024Article
- Synthesis of Peptidyl-tRNA Mimics for Structural Biology Applications.Accounts of chemical research · 2023Review
- Novel read through agent: ZKN-0013 demonstrates efficacy in APCJournal of molecular medicine (Berlin, Germany) · 2023Article
- Insights into the ribosome function from the structures of non-arrested ribosome-nascent chain complexes.Nature chemistry · 2023Article
- Context-based sensing of orthosomycin antibiotics by the translating ribosome.Nature chemical biology · 2022Article
- Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine.Nucleic acids research · 2022Article
- The landscape of translational stall sites in bacteria revealed by monosome and disome profiling.RNA (New York, N.Y.) · 2022Article
- Structural and mechanistic basis for translation inhibition by macrolide and ketolide antibiotics.Nature communications · 2021Article
- Ribosome Protection Proteins-"New" Players in the Global Arms Race with Antibiotic-Resistant Pathogens.International journal of molecular sciences · 2021Review
- Context-specific action of macrolide antibiotics on the eukaryotic ribosome.Nature communications · 2021Article
- Amine-to-Azide Conversion on Native RNA via Metal-Free Diazotransfer Opens New Avenues for RNA Manipulations.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Amine-to-Azide Conversion on Native RNA via Metal-Free Diazotransfer Opens New Avenues for RNA Manipulations.Angewandte Chemie (International ed. in English) · 2021Article
- ABC-F translation factors: from antibiotic resistance to immune response.FEBS letters · 2021Review
- Advanced Methods for Studying Structure and Interactions of Macrolide Antibiotics.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Macrolide antibiotic binding to the ribosome inhibits catalysis of peptide bond formation between specific donor and acceptor substrates. Why particular reactions are problematic for the macrolide-bound ribosome remains unclear. Using comprehensive mutational analysis and biochemical experiments with synthetic substrate analogs, we find that the positive charge of these specific residues and the length of their side chains underlie inefficient peptide bond formation in the macrolide-bound ribosome. Even in the absence of antibiotic, peptide bond formation between these particular donors and acceptors is rather inefficient, suggesting that macrolides magnify a problem present for intrinsically difficult substrates. Our findings emphasize the existence of functional interactions between the nascent protein and the catalytic site of the ribosomal peptidyl transferase center.
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Registered trials
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