ArticleProteins2011
Molecular dynamics of EF-G during translocation.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed.
- Exploring molecular mechanisms of aminoglycoside resistance in Escherichia coli MG1655 using the antibiotic resistance growth plate.Scientific reports · 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
- Anaerobiosis and Mutations Can Reduce Susceptibility ofPathogens (Basel, Switzerland) · 2025Article
- Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.The journal of physical chemistry. B · 2024Article
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- Global reprogramming of virulence and antibiotic resistance inThe Journal of biological chemistry · 2020Article
- Target protection as a key antibiotic resistance mechanism.Nature reviews. Microbiology · 2020Review
- Fusidic acid resistance through changes in the dynamics of the drug target.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.Nucleic acids research · 2018Article
- The translation elongation cycle-capturing multiple states by cryo-electron microscopy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- EF4 reveals the energy barrier for tRNA back-translocation in the peptidyl transferase center.RNA biology · 2016Article
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Advances in the molecular dynamics flexible fitting method for cryo-EM modeling.Methods (San Diego, Calif.) · 2016Article
- Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.RNA (New York, N.Y.) · 2016Article
- A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance.Scientific reports · 2016Article
- Universal and domain-specific sequences in 23S-28S ribosomal RNA identified by computational phylogenetics.RNA (New York, N.Y.) · 2015Article
- Movement of elongation factor G between compact and extended conformations.Journal of molecular biology · 2015Article
- Genomic analysis reveals distinct concentration-dependent evolutionary trajectories for antibiotic resistance in Escherichia coli.DNA research : an international journal for rapid publication of reports on genes and genomes · 2014Article
- Article
- EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex.Nature structural & molecular biology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Elongation factor G (EF-G) plays a crucial role in two stages of mRNA-(tRNA)(2) translocation. First, EF-G•GTP enters the pre-translocational ribosome in its intersubunit-rotated state, with tRNAs in their hybrid (P/E and A/P) positions. Second, a conformational change in EF-G's Domain IV induced by GTP hydrolysis disengages the mRNA-anticodon stem-loops of the tRNAs from the decoding center to advance relative to the small subunit when the ribosome undergoes a backward inter-subunit rotation. These events take place as EF-G undergoes a series of large conformational changes as visualized by cryo-EM and X-ray studies. The number and variety of these structures leave open many questions on how these different configurations form during the dynamic translocation process. To understand the molecular mechanism of translocation, we examined the molecular motions of EF-G in solution by means of molecular dynamics simulations. Our results show: (1) rotations of the super-domain formed by Domains III-V with respect to the super-domain formed by I-II, and rotations of Domain IV with respect to Domain III; (2) flexible conformations of both 503- and 575-loops; (3) large conformational variability in the bound form caused by the interaction between Domain V and the GTPase-associated center; (4) after GTP hydrolysis, the Switch I region seems to be instrumental for effecting the conformational change at the end of Domain IV implicated in the disengagement of the codon-anticodon helix from the decoding center.
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.