ArticleThe EMBO journal2011
eIF2A mediates translation of hepatitis C viral mRNA under stress conditions.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 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
79 citing papers in PubMed, 126 citations in OpenAlex.
- Genetic Variants Associated With Nonpulmonary Vein Triggers of Atrial Fibrillation: A Genome-Wide Association Study.JACC. Advances · 2026Article
- The nuclear cap-binding complex safeguards stress-resistant protein synthesis and proliferation of stem cells.Science advances · 2026Article
- 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
- Loss of non-canonical translation initiation factors impairs perinatal cardiac function in mice.Experimental animals · 2025Article
- Eukaryotic translation initiation factor 2A protects pancreatic beta cells during endoplasmic reticulum stress while rescuing global translation inhibition.Diabetologia · 2025Article
- eIF2A regulates cell migration in a translation-independent manner.Science advances · 2025Article
- Article
- Hepatovirus translation requires PDGFA-associated protein 1, an eIF4E-binding protein regulating endoplasmic reticulum stress responses.Science advances · 2024Article
- eIF2B localization and its regulation during the integrated stress response is cell-type specific.iScience · 2024Article
- Host-like RNA Elements Regulate Virus Translation.Viruses · 2024Review
- Yeast eIF2A has a minimal role in translation initiation and uORF-mediated translational control in vivo.eLife · 2024Article
- An epitope encoded by uORF ofMolecular therapy oncolytics · 2023Article
- Increased levels of eIF2A inhibit translation by sequestering 40S ribosomal subunits.Nucleic acids research · 2023Article
- The enterovirus genome can be translated in an IRES-independent manner that requires the initiation factors eIF2A/eIF2D.PLoS biology · 2023Article
- Article
- Non-canonical initiation factors modulate repeat-associated non-AUG translation.Human molecular genetics · 2022Article
- Mechanistic convergence across initiation sites for RAN translation in fragile X associated tremor ataxia syndrome.Human molecular genetics · 2022Article
- Review
- Genomic Analyses for Selective Signatures and Genes Involved in Hot Adaptation Among Indigenous Chickens From Different Tropical Climate Regions.Frontiers in genetics · 2022Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation of most mRNAs is suppressed under stress conditions. Phosphorylation of the α-subunit of eukaryotic translation initiation factor 2 (eIF2), which delivers initiator tRNA (Met-tRNA(i)) to the P site of the 40S ribosomal subunit, is responsible for such translational suppression. However, translation of hepatitis C viral (HCV) mRNA is refractory to the inhibitory effects of eIF2α phosphorylation, which prevents translation by disrupting formation of the eIF2-GTP-Met-tRNA(i) ternary complex. Here, we report that eIF2A, an alternative initiator tRNA-binding protein, has a key role in the translation of HCV mRNA during HCV infection, in turn promoting eIF2α phosphorylation by activating the eIF2α kinase PKR. Direct interaction of eIF2A with the IIId domain of the HCV internal ribosome entry site (IRES) is required for eIF2A-dependent translation. These data indicate that stress-independent translation of HCV mRNA occurs by recruitment of eIF2A to the HCV IRES via direct interaction with the IIId domain and subsequent loading of Met-tRNA(i) to the P site of the 40S ribosomal subunit.
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.