Positioning of subdomain IIId and apical loop of domain II of the hepatitis C IRES on the human 40S ribosome
Nucleic Acids Research, ISSN: 0305-1048, Vol: 37, Issue: 4, Page: 1141-1151
2009
- 52Citations
- 26Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations52
- Citation Indexes52
- 52
- CrossRef45
- Captures26
- Readers26
- 26
Article Description
The 5′-untranslated region of the hepatitis C virus (HCV) RNA contains a highly structured motif called IRES (Internal Ribosome Entry Site) responsible for the cap-independent initiation of the viral RNA translation. At first, the IRES binds to the 40S subunit without any initiation factors so that the initiation AUG codon falls into the P site. Here using an original site-directed cross-linking strategy, we identified 40S subunit components neighboring subdomain IIId, which is critical for HCV IRES binding to the subunit, and apical loop of domain II, which was suggested to contact the 40S subunit from data on cryo-electron microscopy of ribosomal complexes containing the HCV IRES. HCV IRES derivatives that bear a photoactivatable group at nucleotide A275 or at G263 in subdomain IIId cross-link to ribosomal proteins S3a, S14 and S16, and HCV IRES derivatized at the C83 in the apex of domain II cross-link to proteins S14 and S16. © 2009 The Author(s).
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=62549152278&origin=inward; http://dx.doi.org/10.1093/nar/gkn1026; http://www.ncbi.nlm.nih.gov/pubmed/19129232; https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkn1026; https://dx.doi.org/10.1093/nar/gkn1026; https://academic.oup.com/nar/article/37/4/1141/2409853
Oxford University Press (OUP)
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