Structural basis for the binding of IRES RNAs to the head of the ribosomal 40S subunit
Nucleic Acids Research, ISSN: 0305-1048, Vol: 39, Issue: 12, Page: 5264-5275
2011
- 42Citations
- 84Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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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
- Citations42
- Citation Indexes42
- 42
- CrossRef34
- Captures84
- Readers84
- 84
Article Description
Some viruses exploit internal initiation for their propagation in the host cell. This type of initiation is facilitated by structured elements (internal ribosome entry site, IRES) upstream of the initiator AUG and requires only a reduced number of canonical initiation factors. An important example are IRES of the virus family Dicistroviridae that bind to the inter-subunit side of the small ribosomal 40S subunit and lead to the formation of elongation-competent 80S ribosomes without the help of any initiation factor. Here, we present a comprehensive functional and structural analysis of eukaryotic-specific ribosomal protein rpS25 in the context of this type of initiation and propose a structural model explaining the essential involvement of rpS25 for hijacking the ribosome. © 2011 The Author(s).
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79960207638&origin=inward; http://dx.doi.org/10.1093/nar/gkr114; http://www.ncbi.nlm.nih.gov/pubmed/21378123; https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkr114; https://dx.doi.org/10.1093/nar/gkr114; https://academic.oup.com/nar/article/39/12/5264/2411537
Oxford University Press (OUP)
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