ArticleScience (New York, N.Y.)2009
The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 295 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
295 citing papers in PubMed.
- Article
- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- Exploring molecular mechanisms of aminoglycoside resistance in Escherichia coli MG1655 using the antibiotic resistance growth plate.Scientific reports · 2026Article
- Destabilization of Structured RNAs by OPC and TIP4PD Water Models.Journal of chemical theory and computation · 2026Article
- Inhibition of fusidic acid resistance through restricting conformational flexibility in domain III of EF-G.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025Review
- Multi-Modal Design, Synthesis, and Biological Evaluation of Novel Fusidic Acid Derivatives.Molecules (Basel, Switzerland) · 2025Article
- Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis.Nature communications · 2025Article
- 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
- Elongation factor 2 in cancer: a promising therapeutic target in protein translation.Cellular & molecular biology letters · 2024Review
- Allosteric Effects of EF-G Domain I Mutations Inducing Ribosome Frameshifting Revealed by Multiplexed Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Article
- Alternate conformational trajectories in ribosome translocation.PLoS computational biology · 2024Article
- Developing Multichannel smFRET Approach to Dissecting Ribosomal Mechanisms.Chemical & biomedical imaging · 2024Article
- Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane.Scientific reports · 2024Article
- Drug resistance through ribosome splitting and rRNA disordering in mycobacteria.bioRxiv : the preprint server for biology · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.bioRxiv : the preprint server for biology · 2023Article
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
235 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
6 authors.
Funding
Abstract
Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.
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.