ArticleNature communications2015
Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 143 citations in OpenAlex.
- Article
- Article
- Synthetic circRNAs employ IRES activity for translation in cells and in cell-free translation systems.bioRxiv : the preprint server for biology · 2026Article
- IRES-TrAPPr reveals novel insights into viral and cellular mRNA translation.bioRxiv : the preprint server for biology · 2026Article
- Distribution and structural diversity of type IV internal ribosome entry sites.RNA (New York, N.Y.) · 2026Article
- The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES.The EMBO journal · 2026Article
- A bicistronic viral genome uses a compact type IV IRES near its 3' end to express a transmembrane protein.Cell reports · 2026Article
- Structures of the eIF4G-binding RNA domains among picornaviral IRES types are topologically conserved.Nature communications · 2026Article
- A ribosome-bound pseudoknot in the HCV coding region stimulates viral growth by tuning viral translation.Cell reports · 2026Article
- Structural insights into the role of eIF3 in translation mediated by the HCV IRES.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Integrating rna structure and protein interactions to uncover the mechanisms of viral and cellular ires function.Biology direct · 2025Article
- IRES-Mediated Translation: Expanding the Toolkits of RNA Therapy.International journal of molecular sciences · 2025Review
- The intrinsic properties of mRNAs define their translation efficiency at ribosome shortage.Nucleic acids research · 2025Article
- DNA to RNA Tuning of a Pyrrolidine-Derived Quinoxaline Scaffold: Magnesium Induces Binding and Inhibition of Internal Ribosomal Entry Site RNA-Mediated Translational of Hepatitis C Virus.ACS pharmacology & translational science · 2025Article
- Internal ribosome entry sites enhance translation in trans in antisense non-coding SINEUP and circular RNAs.Nucleic acids research · 2025Article
- Distinct non-canonical translation initiation modes arise for specific host and viral mRNAs during poxvirus-induced shutoff.Nature microbiology · 2025Article
- Discovery of functional factorless internal ribosome entry site-like structures through virome mining.PLoS pathogens · 2025Article
- Inconsistencies in the published rabbit ribosomal rRNAs: a proposal for uniformity in sequence and site numbering.RNA (New York, N.Y.) · 2025Article
- A conserved class of viral RNA structures regulates translation reinitiation through dynamic ribosome interactions.Cell reports · 2025Article
- Host-like RNA Elements Regulate Virus Translation.Viruses · 2024Review
38 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV), a widespread human pathogen, is dependent on a highly structured 5'-untranslated region of its mRNA, referred to as internal ribosome entry site (IRES), for the translation of all of its proteins. The HCV IRES initiates translation by directly binding to the small ribosomal subunit (40S), circumventing the need for many eukaryotic translation initiation factors required for mRNA scanning. Here we present the cryo-EM structure of the human 40S ribosomal subunit in complex with the HCV IRES at 3.9 Å resolution, determined by focused refinement of an 80S ribosome-HCV IRES complex. The structure reveals the molecular details of the interactions between the IRES and the 40S, showing that expansion segment 7 (ES7) of the 18S rRNA acts as a central anchor point for the HCV IRES. The structural data rationalizes previous biochemical and genetic evidence regarding the initiation mechanism of the HCV and other related IRESs.
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