ArticleJournal of molecular biology2008
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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The trial behind it
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
44 citing papers in PubMed, 86 citations in OpenAlex.
- Mutations in apicoplast rRNA genes are associated with clindamycin resistance and impair the ability of malaria parasites to infect mosquitoes.Antimicrobial agents and chemotherapy · 2026Article
- Structure of an archaeal ribosome reveals a divergent active site and hibernation factor.Nature microbiology · 2025Article
- Systematic Exploration of Functional Group Relevance for Anti-Leishmanial Activity of Anisomycin.Biomedicines · 2023Article
- High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation.Nature communications · 2022Article
- The dark side of the ribosome life cycle.RNA biology · 2022Article
- DrugPred_RNA-A Tool for Structure-Based Druggability Predictions for RNA Binding Sites.Journal of chemical information and modeling · 2021Article
- Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens.Nature communications · 2021Article
- Simulation Study of the Plasticity of k-Turn Motif in Different Environments.Biophysical journal · 2020Article
- Base-intercalated and base-wedged stacking elements in 3D-structure of RNA and RNA-protein complexes.Nucleic acids research · 2020Article
- Tiamulin-Resistant Mutants of the Thermophilic BacteriumAntibiotics (Basel, Switzerland) · 2020Article
- RNAfitme: a webserver for modeling nucleobase and nucleoside residue conformation in fixed-backbone RNA structures.BMC bioinformatics · 2018Article
- Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design.Annual review of biochemistry · 2018Review
- Critical 23S rRNA interactions for macrolide-dependent ribosome stalling on the ErmCL nascent peptide chain.Nucleic acids research · 2017Article
- Article
- Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Ribosomal Antibiotics: Contemporary Challenges.Antibiotics (Basel, Switzerland) · 2016Review
- Inhibition of translation initiation complex formation by GE81112 unravels a 16S rRNA structural switch involved in P-site decoding.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Kink Turn, a Key Architectural Element in RNA Structure.Journal of molecular biology · 2016Review
- Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.
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What OpenQuestion holds
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 OpenQuestion graph.