ArticleTrends in biochemical sciences2013
Anticodon G recognition by tRNA synthetases mimics the tRNA core.
Article in Trends in biochemical sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Breaking a single hydrogen bond in the mitochondrial tRNAThe FEBS journal · 2020Article
- Structural Insights into the Polyphyletic Origins of Glycyl tRNA Synthetases.The Journal of biological chemistry · 2016Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Ancient mechanisms for nucleotide base recognition in the RNA world are candidates for mimicking by early proteins like tRNA synthetases. In the core of the tRNA, conserved G22 interacts with two internal bases in a complex further stabilized by stacking interactions. This particular tRNA format for G recognition is shown here to be adapted by nine different and even nonhomologous anticodon binding domains (ABDs) of tRNA synthetases, in which amino acid side chains mimic all of the tRNA G22 base interactions. We offer the possibility that mimicking this RNA-based mechanism for guanine recognition is perhaps one of the selective pressures for choosing amino acids for the genetic code.
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