ArticleNature communications2023
Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Review
- Article
- An RNA Language Model trained on sequence alone reveals the structural logic of Internal Ribosome Entry Sites.bioRxiv : the preprint server for biology · 2026Article
- The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES.The EMBO journal · 2026Article
- Structures of the eIF4G-binding RNA domains among picornaviral IRES types are topologically conserved.Nature communications · 2026Article
- Goatpox virus Hrf-063 interacts with host eIF4A1 and is associated with altered expression of antiviral signaling-related factors.Frontiers in cellular and infection microbiology · 2026Article
- Ins and outs of IRES elements: function and significance.Biochemical Society transactions · 2025Review
- Review
- The Influence of Extra-Ribosomal Functions of Eukaryotic Ribosomal Proteins on Viral Infection.Biomolecules · 2024Review
- Translation of Overlapping Open Reading Frames Promoted by Type 2 IRESs in Avian Calicivirus Genomes.Viruses · 2024Article
- ScreeningBreeding science · 2024Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many RNA viruses employ internal ribosome entry sites (IRESs) in their genomic RNA to commandeer the host's translational machinery for replication. The IRES from encephalomyocarditis virus (EMCV) interacts with eukaryotic translation initiation factor 4 G (eIF4G), recruiting the ribosomal subunit for translation. Here, we analyze the three-dimensional structure of the complex composed of EMCV IRES, the HEAT1 domain fragment of eIF4G, and eIF4A, by cryo-electron microscopy. Two distinct eIF4G-interacting domains on the IRES are identified, and complex formation changes the angle therebetween. Further, we explore the dynamics of these domains by using solution NMR spectroscopy, revealing conformational equilibria in the microsecond to millisecond timescale. In the lowly-populated conformations, the base-pairing register of one domain is shifted with the structural transition of the three-way junction, as in the complex structure. Our study provides insights into the viral RNA's sophisticated strategy for optimal docking to hijack the host protein.
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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.