M
Manuela Argentini
Researcher at Université Paris-Saclay
Publications - 6
Citations - 478
Manuela Argentini is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: Signal peptide & Corynebacterium glutamicum. The author has an hindex of 6, co-authored 6 publications receiving 440 citations. Previous affiliations of Manuela Argentini include Vision Institute & Centre national de la recherche scientifique.
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Journal ArticleDOI
Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A
Christophe Cans,Brent Passer,V. F. Shalak,Vanessa Nancy-Portebois,Virginie Crible,Nathalie Amzallag,David Allanic,Rowena Tufino,Manuela Argentini,Dino Moras,Giusy Fiucci,Bruno Goud,Marc Mirande,Robert Amson,Adam Telerman +14 more
TL;DR: The data suggest that TCTP has guanine nucleotide dissociation inhibitor activity, and, moreover, implicate T CTP in the elongation step of protein synthesis.
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The in vivo mitochondrial two-step maturation of human frataxin
TL;DR: Evidence is provided that mature human frataxin corresponds to m(81)-FXN, and can rescue the lethal phenotype of fibroblasts completely deleted for fratXin, and it is demonstrated that all fratxin isoforms are generated and localized within the mitochondria.
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New insights into the incorporation of natural suppressor tRNAs at stop codons in Saccharomyces cerevisiae
TL;DR: This work constitutes the first systematic analysis of the amino acids incorporated at stop codons, providing important new insights into the decoding rules used by the ribosome to read the genetic code.
Journal ArticleDOI
The ppm operon is essential for acylation and glycosylation of lipoproteins in Corynebacterium glutamicum.
Niloofar Mohiman,Niloofar Mohiman,Manuela Argentini,Sarah M. Batt,David Cornu,Muriel Masi,Muriel Masi,Lothar Eggeling,Gurdyal S. Besra,Nicolas Bayan,Nicolas Bayan +10 more
TL;DR: Together, these results show for the first time that Cg-Ppm1 (Ppm synthase) and Cg -Ppm2 (Lnt) operate in a common biosynthetic pathway in which lipoprotein N-acylation and glycosylation are tightly coupled.
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Identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex: the case of lysyl-tRNA synthetase and the scaffold protein p38.
Azaria Remion,Fawzi Khoder-Agha,Fawzi Khoder-Agha,David Cornu,Manuela Argentini,Virginie Redeker,Virginie Redeker,Marc Mirande,Marc Mirande +8 more
TL;DR: The protein interface of the cross‐linked complex is unambiguously identified and it is shown that Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, in agreement with the published cocrystal structure.