Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution
Proceedings of the National Academy of Sciences of the United States of America, ISSN: 1091-6490, Vol: 107, Issue: 46, Page: 19748-19753
2010
- 176Citations
- 335Captures
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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.
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Metrics Details
- Citations176
- Citation Indexes176
- 176
- CrossRef163
- Captures335
- Readers335
- 335
Article Description
Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98% of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES-ES and r-protein-ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=78650546283&origin=inward; http://dx.doi.org/10.1073/pnas.1009999107; http://www.ncbi.nlm.nih.gov/pubmed/20980660; https://pnas.org/doi/full/10.1073/pnas.1009999107; https://dx.doi.org/10.1073/pnas.1009999107; https://www.pnas.org/content/107/46/19748
Proceedings of the National Academy of Sciences
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