ArticleNature structural & molecular biology2022
Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 87 citations in OpenAlex.
- Halting translation by the letter with sequence-selective small molecules.Nature chemical biology · 2026Review
- Sparsomycin inhibits translation through a conserved mechanism across all domains of life.Nucleic acids research · 2026Article
- Off-target anti-leukemic effects of antibiotics: mechanisms and therapeutic insights.Cancer chemotherapy and pharmacology · 2026Review
- Context-dependent translation inhibition as a cancer therapeutic modality.Nature communications · 2026Article
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- Fighting the invader: strategies against intracellular bacteria.Frontiers in pharmacology · 2026Review
- Hybrid Antibiotics Targeting the Bacterial Ribosome.ACS central science · 2025Article
- Structural insights into context-specific inhibition of bacterial translation by macrolides.Nature communications · 2025Article
- Prodrug florfenicol amine is activated by intrinsic resistance to target Mycobacterium abscessus.Nature microbiology · 2025Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin.bioRxiv : the preprint server for biology · 2025Article
- A rapid, simple, and economical method for the isolation of ribosomes and translational machinery for structural and functional studies.Nature communications · 2025Article
- Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.Science (New York, N.Y.) · 2025Article
- Mechanisms of action and resistance prevention of synergistic thymol and carvacrol combinations with antibiotics in Staphylococcus aureus and Acinetobacter baumannii.Natural products and bioprospecting · 2025Article
- Article
- HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells.Nature structural & molecular biology · 2025Article
- Context-specific inhibition of mitochondrial ribosomes by phenicol and oxazolidinone antibiotics.Nucleic acids research · 2025Article
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
- Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.EMBO reports · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Ribosome-targeting antibiotics serve as powerful antimicrobials and as tools for studying the ribosome, the catalytic peptidyl transferase center (PTC) of which is targeted by many drugs. The classic PTC-acting antibiotic chloramphenicol (CHL) and the newest clinically significant linezolid (LZD) were considered indiscriminate inhibitors of protein synthesis that cause ribosome stalling at every codon of every gene being translated. However, recent discoveries have shown that CHL and LZD preferentially arrest translation when the ribosome needs to polymerize particular amino acid sequences. The molecular mechanisms that underlie the context-specific action of ribosome inhibitors are unknown. Here we present high-resolution structures of ribosomal complexes, with or without CHL, carrying specific nascent peptides that support or negate the drug action. Our data suggest that the penultimate residue of the nascent peptide directly modulates antibiotic affinity to the ribosome by either establishing specific interactions with the drug or by obstructing its proper placement in the binding site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.