ArticleNature structural & molecular biology2025
Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Applications and prospects of cryo-electron tomography in drug discovery and understanding disease.Current opinion in structural biology · 2026Review
- Structure of the hibernating Francisella tularensis ribosome and mechanistic insights into its inhibition by antibiotics.Nucleic acids research · 2026Article
- Expression of translation elongation factor P in Kocuria rhizophila is regulated by an inducible weak promoter.BMC microbiology · 2026Article
- Advantages and Limitations of AlphaFold in Structural Biology: Insights from Recent Studies.The protein journal · 2026Review
- Visualizing the translation landscape in human cells at high resolution.Nature communications · 2025Article
- Posttranscriptional 3'-Terminal Modifications ofMicroorganisms · 2025Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- A practical look at cryo-electron tomography image processing: Key considerations for new biological discoveries.Current opinion in structural biology · 2025Review
- In situ cryo-electron microscopy and tomography of cellular and organismal samples.Current opinion in structural biology · 2025Review
- In-cell chromatin structure by Cryo-FIB and Cryo-ET.Current opinion in structural biology · 2025Review
- Structure is beauty, but not always truth.Cell · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome-targeting antibiotics represent an important class of antimicrobial drugs. Chloramphenicol (Cm) is a well-studied ribosomal peptidyl transferase center (PTC) binder and growing evidence suggests that its inhibitory action depends on the sequence of the nascent peptide. How such selective inhibition on the molecular scale manifests on the cellular level remains unclear. Here, we use cryo-electron tomography to analyze the impact of Cm inside the bacterium Mycoplasma pneumoniae. By resolving the Cm-bound ribosomes to 3.0 Å, we elucidate Cm's coordination with natural nascent peptides and transfer RNAs in the PTC. We find that Cm leads to the accumulation of a number of translation elongation states, indicating ongoing futile accommodation cycles, and to extensive ribosome collisions. We, thus, suggest that, beyond its direct inhibition of protein synthesis, the action of Cm may involve the activation of cellular stress responses. This work exemplifies how in-cell structural biology can expand the understanding of mechanisms of action for extensively studied antibiotics.
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Registered trials
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.