ArticleThe EMBO journal2022
Molecular architecture of 40S translation initiation complexes on the hepatitis C virus IRES.
Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.
- Structure and function of type IV IRES in picornaviruses: a systematic review.Frontiers in microbiology · 2024Pooled it
- Review
- Article
- Genetic mechanisms underlying the structural elaboration and dissemination of viral internal ribosomal entry sites.Nucleic acids research · 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
- 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
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Viral helicase and methyltransferase promote genotype one-hepatitis e virus internal ribosome entry site-like element activity.Npj viruses · 2025Article
- eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025Article
- Ins and outs of IRES elements: function and significance.Biochemical Society transactions · 2025Review
- Review
- 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
- Ribosome biogenesis: A central player in liver diseases.Genes & diseases · 2025Review
- Crystallographic and cryoEM analyses reveal SARS-CoV-2 SL5 is a mobile T-shaped four-way junction with deep pockets.RNA (New York, N.Y.) · 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
- Structural basis of AUC codon discrimination during translation initiation in yeast.Nucleic acids research · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Hepatitis C virus mRNA contains an internal ribosome entry site (IRES) that mediates end-independent translation initiation, requiring a subset of eukaryotic initiation factors (eIFs). Biochemical studies revealed that direct binding of the IRES to the 40S ribosomal subunit places the initiation codon into the P site, where it base pairs with eIF2-bound Met-tRNAiMet forming a 48S initiation complex. Subsequently, eIF5 and eIF5B mediate subunit joining, yielding an elongation-competent 80S ribosome. Initiation can also proceed without eIF2, in which case Met-tRNAiMet is recruited directly by eIF5B. However, the structures of initiation complexes assembled on the HCV IRES, the transitions between different states, and the accompanying conformational changes have remained unknown. To fill these gaps, we now obtained cryo-EM structures of IRES initiation complexes, at resolutions up to 3.5 Å, that cover all major stages from the initial ribosomal association, through eIF2-containing 48S initiation complexes, to eIF5B-containing complexes immediately prior to subunit joining. These structures provide insights into the dynamic network of 40S/IRES contacts, highlight the role of IRES domain II, and reveal conformational changes that occur during the transition from eIF2- to eIF5B-containing 48S complexes and prepare them for subunit joining.
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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.