RNA tetraplex as a primordial peptide synthesis scaffold
Biosystems, ISSN: 0303-2647, Vol: 109, Issue: 2, Page: 145-150
2012
- 7Citations
- 10Captures
Metric Options: CountsSelecting 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
- Citations7
- Citation Indexes7
- CrossRef7
- Captures10
- Readers10
- 10
Article Description
Peptide bond formation at the peptidyl transferase center on the ribosome is a crucial phenomenon in life systems. In this study, we conceptually propose possible roles of the RNA tetraplex as a scaffold for two aminoacyl minihelices that enable peptide bond formation. The basic rationale of this model is that “parallel” complementary templates composed of only 10-mer nucleotides can position two amino acids in close proximity, which is conceptually and essentially similar to the situation observed in ribosomes. Using supportive experimental data, we discuss the origin and evolution of peptide bond formation in early biological systems.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0303264712000536; http://dx.doi.org/10.1016/j.biosystems.2012.03.003; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84863480961&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22465151; https://linkinghub.elsevier.com/retrieve/pii/S0303264712000536; https://dx.doi.org/10.1016/j.biosystems.2012.03.003
Elsevier BV
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