ArticleScientific reports2019
Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 56 citations in OpenAlex.
- Structure of the hibernating Francisella tularensis ribosome and mechanistic insights into its inhibition by antibiotics.Nucleic acids research · 2026Article
- Autonomous biogenesis of all thirty proteins of the Escherichia coli translation machinery.Nature communications · 2025Article
- On the Completeness of Existing RNA Fragment Structures.Genomics, proteomics & bioinformatics · 2025Article
- Structural studies on ribosomes of differentially macrolide-resistantLife science alliance · 2025Article
- Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Article
- Acetyl-proteome profiling revealed the role of lysine acetylation in erythromycin resistance ofHeliyon · 2024Article
- RlmQ: a newly discovered rRNA modification enzyme bridging RNA modification and virulence traits inRNA (New York, N.Y.) · 2024Article
- The structure of a hibernating ribosome in a Lyme disease pathogen.Nature communications · 2023Article
- Interactions between terminal ribosomal RNA helices stabilize theRNA (New York, N.Y.) · 2023Article
- Anionic G•U pairs in bacterial ribosomal rRNAs.RNA (New York, N.Y.) · 2023Article
- Article
- Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM.Structure (London, England : 1993) · 2023Review
- Article
- Using deep-learning predictions of inter-residue distances for model validation.Acta crystallographica. Section D, Structural biology · 2022Article
- Cryo-EM structure ofEmerging microbes & infections · 2022Article
- Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci.Nucleic acids research · 2022Article
- Cryo-EM structure of the ancient eukaryotic ribosome from the human parasite Giardia lamblia.Nucleic acids research · 2022Article
- Peptidyl transferase center decompaction and structural constraints during early protein elongation on the ribosome.Scientific reports · 2021Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The clinical use of the antibiotic erythromycin (ery) is hampered owing to the spread of resistance genes that are mostly mutating rRNA around the ery binding site at the entrance to the protein exit tunnel. Additional effective resistance mechanisms include deletion or insertion mutations in ribosomal protein uL22, which lead to alterations of the exit tunnel shape, located 16 Å away from the drug's binding site. We determined the cryo-EM structures of the Staphylococcus aureus 70S ribosome, and its ery bound complex with a two amino acid deletion mutation in its ß hairpin loop, which grants the bacteria resistance to ery. The structures reveal that, although the binding of ery is stable, the movement of the flexible shorter uL22 loop towards the tunnel wall creates a wider path for nascent proteins, thus enabling bypass of the barrier formed by the drug. Moreover, upon drug binding, the tunnel widens further.
Indexed as
Identifiers
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.