Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Sylvie Gillet"'
Autor:
Sylvie Gillet-Bresson
Publikováno v:
Les Enjeux de l'information et de la communication. :6-17
Autor:
Svitlana Havrylenko, Paulette Decottignies, Boris Negrutskii, Pierre Le Maréchal, Monika Kaminska, Marc Mirande, Sylvie Gillet
Publikováno v:
Journal of Biological Chemistry. 284:6053-6060
The spatio-temporal organization of proteins within the cytoplasm of eukaryotic cells rests in part on the assembly of stable and transient multiprotein complexes. Here we examined the assembly of the multiaminoacyl-tRNA synthetase complex (MARS) in
Publikováno v:
Protein Science
Protein Science, Wiley, 1997, 6 (11), pp.2426. ⟨10.1002/pro.5560061116⟩
Protein Science, Wiley, 1997, 6 (11), pp.2426. ⟨10.1002/pro.5560061116⟩
International audience; Methionyl-adenylate, the mixed carboxylic-phosphoric acid anhydride synthesized by methionyl-tRNA synthetase (MetRS) is capable of reacting with this synthetase or other proteins, by forming an isopeptide bond with the epsilon
Publikováno v:
Molecular bioSystems. 10(11)
While acting upon chromatin compaction, histone post-translational modifications (PTMs) are involved in modulating gene expression through histone–DNA affinity and protein–protein interactions. These dynamic and environment-sensitive modification
Publikováno v:
The Journal of Biochemistry. 116:493-501
Lysyl-tRNA synthetase (LysRS), a representative of the class 2 aminoacyl-tRNA synthetases, occurs as two species in Escherichia coli: LysRSs and LysRSu. To identify the ATP-binding site in this enzyme, we have applied affinity labeling with reactive
Publikováno v:
The Journal of Biochemistry. 116:502-507
Pyridoxal 5'-phosphate (PLP) and pyridoxal 5'-diphosphate (PLDP) were used to identify lysyl residues at the phosphate-binding locus in the lysS-encoded and the lysU-encoded lysyl-tRNA synthetases (LysRSs and LysRSu, respectively) from Escherichia co
Publikováno v:
Photosynthesis research. 89(2-3)
A proteomic approach including two-dimensional electrophoresis and MALDI-TOF analysis has been developed to identify the soluble proteins of the unicellular photosynthetic algae Chlamydomonas reinhardtii. We first described the partial 2D-picture of
Autor:
Alain Eychène, Marie-Paule Felder-Schmittbuhl, Karine Sii-Felice, Laure Lecoin, Jean-Antoine Girault, Celio Pouponnot, Sylvie Gillet
Publikováno v:
FEBS letters. 579(17)
Basic-leucine zipper transcription factors of the Maf family are key regulators of various developmental and differentiation processes. We previously reported that the phosphorylation status of MafA is a critical determinant of its biological functio
Autor:
Bernard Pineau, Catherine Gérard-Hirne, Stephan Eberhard, Sylvie Gillet, Paulette Decottignies, Jacqueline Girard-Bascou, Antoine Tremolieres, Yves Choquet, Annick Bennardo-Connan, Francis-André Wollman
Publikováno v:
European journal of biochemistry. 271(2)
Two mutants of Chlamydomonas reinhardtii, mf1 and mf2, characterized by a marked reduction in their phosphatidylglycerol content together with a complete loss in its Delta3-trans hexadecenoic acid-containing form, also lost photosystem II (PSII) acti
Autor:
Sylvie Gillet, Alain Mazé, Grégory Boël, Vianney Pichereau, Jean-Christophe Giard, Axel Hartke, Josef Deutscher, Sandrine Poncet, Yanick Auffray, Ivan Mijakovic
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2004, 337 (2), pp.485-496. ⟨10.1016/j.jmb.2003.12.082⟩
Journal of Molecular Biology, Elsevier, 2004, 337 (2), pp.485-496. ⟨10.1016/j.jmb.2003.12.082⟩
International audience; We observed that in vivo and in vitro a small fraction of the glycolytic enzyme enolase became covalently modified by its substrate 2-phosphoglycerate (2-PG). In modified Escherichia coli enolase, 2-PG was bound to Lys341, whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d10b25afc8594c5be3f28798175d5c2a
https://www.bib.irb.hr/147757
https://www.bib.irb.hr/147757