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Magali Frugier

Researcher at University of Strasbourg

Publications -  46
Citations -  1496

Magali Frugier is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Transfer RNA & Aminoacylation. The author has an hindex of 25, co-authored 42 publications receiving 1381 citations. Previous affiliations of Magali Frugier include Massachusetts Institute of Technology & Centre national de la recherche scientifique.

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A population of tRNA-derived small RNAs is actively produced in Trypanosoma cruzi and recruited to specific cytoplasmic granules.

TL;DR: The results showed the production of an abundant class of tRNA-derived small RNAs preferentially restricted to specific isoacceptors and whose production was more accentuated under nutritional stress, favor the idea that tRNA cleavage is unlikely to be the consequence of non-specific degradation but a controlled process, whose biological significance remains to be elucidated.
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A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding

TL;DR: It is demonstrated that the N‐terminal extension in yeast AspRS participates in tRNA binding and this finding is generalized to eukaryotic class IIb aminoacyl‐tRNA synthetases.
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Towards Understanding Human Mitochondrial Leucine Aminoacylation Identity

TL;DR: Structural and aminoacylation properties of in vitro transcribed tRNA(Leu(UUR)) are presented and mutational analysis demonstrates that the discriminator base as well as residue A14 are important leucine identity elements, demonstrating that human mitochondrial leucylation is dependent on rules similar to those that apply in Escherichia coli.
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Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide

TL;DR: It is shown that small RNA helices which recapitulate part or all of the acceptor stem of yeast aspartate tRNA are efficiently aminoacylated by cognate class II aspartyl‐tRNA synthetase, and that the contemporary tRNA(Asp) has quantitatively retained the influence of the major signal for aminoacylation in these substrates.