ReviewWiley interdisciplinary reviews. RNA
The structures of nonprotein-coding RNAs that drive internal ribosome entry site function.
Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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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.
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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
39 citing papers in PubMed, 55 citations in OpenAlex.
- Roadblocks and fast tracks: How RNA binding proteins affect the viral RNA journey in the cell.Seminars in cell & developmental biology · 2021Review
- A translation enhancer element from black beetle virus engages yeast eIF4G1 to drive cap-independent translation initiation.Scientific reports · 2021Article
- Gene- and Species-Specific Hox mRNA Translation by Ribosome Expansion Segments.Molecular cell · 2020Article
- The DDX23 Negatively Regulates Translation and Replication of Foot-and-Mouth Disease Virus and Is Degraded by 3C Proteinase.Viruses · 2020Article
- 5'-UTR recruitment of the translation initiation factor eIF4GI or DAP5 drives cap-independent translation of a subset of human mRNAs.The Journal of biological chemistry · 2020Article
- IRESpy: an XGBoost model for prediction of internal ribosome entry sites.BMC bioinformatics · 2019Article
- A peptide encoded by circular form of LINC-PINT suppresses oncogenic transcriptional elongation in glioblastoma.Nature communications · 2018Article
- Functional Insights into the Adjacent Stem-Loop in Honey Bee Dicistroviruses That Promotes Internal Ribosome Entry Site-Mediated Translation and Viral InfectionJournal of virology · 2018Article
- The Initiation Factors eIF2, eIF2A, eIF2D, eIF4A, and eIF4G Are Not Involved in Translation Driven by Hepatitis C Virus IRES in Human Cells.Frontiers in microbiology · 2018Article
- Distinct roles for the IIId2 sub-domain in pestivirus and picornavirus internal ribosome entry sites.Nucleic acids research · 2017Article
- Crystal Structure of the C-terminal Domain of Human eIF2D and Its Implications on Eukaryotic Translation Initiation.Journal of molecular biology · 2017Article
- Advancing viral RNA structure prediction: measuring the thermodynamics of pyrimidine-rich internal loops.RNA (New York, N.Y.) · 2017Article
- Molecular analysis of the factorless internal ribosome entry site in Cricket Paralysis virus infection.Scientific reports · 2016Article
- IRES inhibition induces terminal differentiation and synchronized death in triple-negative breast cancer and glioblastoma cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Molecular Pathophysiology of Fragile X-Associated Tremor/Ataxia Syndrome and Perspectives for Drug Development.Cerebellum (London, England) · 2016Review
- Hydrogen peroxide induces La cytoplasmic shuttling and increases hepatitis C virus internal ribosome entry site-dependent translation.The Journal of general virology · 2016Article
- Biological function of Foot-and-mouth disease virus non-structural proteins and non-coding elements.Virology journal · 2016Review
- Linking Α to Ω: diverse and dynamic RNA-based mechanisms to regulate gene expression by 5'-to-3' communication.F1000Research · 2016Review
- A Unique 5' Translation Element Discovered in Triticum Mosaic Virus.Journal of virology · 2015Article
- Conformational flexibility of viral RNA switches studied by FRET.Methods (San Diego, Calif.) · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Internal ribosome entry sites (IRESs) are RNA sequences that can recruit the translation machinery independent of the 5' end of the messenger RNA. IRESs are found in both viral and cellular RNAs and are important for regulating gene expression. There is great diversity in the mechanisms used by IRESs to recruit the ribosome and this is reflected in a variety of RNA sequences that function as IRESs. The ability of an RNA sequence to function as an IRES is conferred by structures operating at multiple levels from primary sequence through higher-order three-dimensional structures within dynamic ribonucleoproteins (RNPs). When these diverse structures are compared, some trends are apparent, but overall it is not possible to find universal rules to describe IRES structure and mechanism. Clearly, many different sequences and structures have evolved to perform the function of recruiting, positioning, and activating a ribosome without using the canonical cap-dependent mechanism. However, as our understanding of the specific sequences, structures, and mechanisms behind IRES function improves, more common features may emerge to link these diverse RNAs.
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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 OpenQuestion graph.