ArticleJournal of virology2003
Conserved nucleotides within the J domain of the encephalomyocarditis virus internal ribosome entry site are required for activity and for interaction with eIF4G.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 41 citations in OpenAlex.
- 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
- Translation of Overlapping Open Reading Frames Promoted by Type 2 IRESs in Avian Calicivirus Genomes.Viruses · 2024Article
- Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor.Nature communications · 2023Article
- Insights into Structural and Mechanistic Features of Viral IRES Elements.Frontiers in microbiology · 2017Review
- An accurately preorganized IRES RNA structure enables eIF4G capture for initiation of viral translation.Nature structural & molecular biology · 2016Article
- Cap-dependent translation is mediated by 'RNA looping' rather than 'ribosome scanning'.RNA biology · 2016Article
- Translation initiation mediated by RNA looping.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Local RNA flexibility perturbation of the IRES element induced by a novel ligand inhibits viral RNA translation.RNA biology · 2015Article
- Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.The FEBS journal · 2014Article
- A distinct class of internal ribosomal entry site in members of the Kobuvirus and proposed Salivirus and Paraturdivirus genera of the Picornaviridae.Journal of virology · 2012Article
- SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA cleavage.PLoS pathogens · 2011Article
- The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES.The EMBO journal · 2011Article
- Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors.Nucleic acids research · 2011Article
- Insights into the biology of IRES elements through riboproteomic approaches.Journal of biomedicine & biotechnology · 2010Review
- The impact of RNA structure on picornavirus IRES activity.Trends in microbiology · 2008Article
- Raman and Raman optical activity (ROA) analysis of RNA structural motifs in Domain I of the EMCV IRES.Nucleic acids research · 2007Article
- Evidence of reciprocal tertiary interactions between conserved motifs involved in organizing RNA structure essential for internal initiation of translation.RNA (New York, N.Y.) · 2006Article
- Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation.RNA (New York, N.Y.) · 2005Article
- NMR studies of the structure and Mg2+ binding properties of a conserved RNA motif of EMCV picornavirus IRES element.Nucleic acids research · 2004Article
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 at 3 institutions in 1 country.
Funding
Abstract
The internal ribosome entry site (IRES) elements of cardioviruses (e.g., encephalomyocarditis virus [EMCV] and foot-and-mouth disease virus) are predicted to have very similar secondary structures. Among these complex RNA structures there is only rather limited complete sequence conservation. Within the J domain of the EMCV IRES there are four highly conserved nucleotides (A704, C705, G723, and A724)., which are predicted to be unpaired and have been targeted for mutagenesis. Using an IRES-dependent cell selection system, we have isolated functional IRES elements from a pool of up to 256 mutants. All changes to these conserved nucleotides resulted in IRES elements that were less efficient at directing internal initiation of translation than the wild-type element, and even some of the single point mutants were highly defective. Each of the mutations adversely affected the ability of the RNAs to interact with the translation initiation factor eIF4G.
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.