Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Josiane Chen"'
Autor:
Christine Lazennec, Pierre Plateau, Sylvain Blanquet, Josiane Chen, Annie Brevet, Stéphane Commans
Publikováno v:
Journal of Biological Chemistry. 278:30927-30935
The highly conserved aspartyl-, asparaginyl-, and lysyl-tRNA synthetases compose one subclass of aminoacyl-tRNA synthetases, called IIb. The three enzymes possess an OB-folded extension at their N terminus. The function of this extension is to specif
Publikováno v:
Journal of Bacteriology. 180:2345-2349
The putative human tumor suppressor gene FHIT (fragile histidine triad) (M. Ohta et al., Cell 84:587–597, 1996) encodes a protein behaving in vitro as a dinucleoside 5′,5′′′-P 1 ,P 3 -triphosphate (Ap 3 A) hydrolase. In this report, we show
Publikováno v:
Journal of Biological Chemistry. 270:14439-14444
In Escherichia coli, lysyl-tRNA synthetase activity is encoded by either a constitutive lysS gene or an inducible one, lysU. The two corresponding enzymes could be purified at homogeneity from a delta lysU and a delta lysS strain, respectively. Compa
Autor:
Annie, Brevet, Josiane, Chen, Stéphane, Commans, Christine, Lazennec, Sylvain, Blanquet, Pierre, Plateau
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (33), pp.30927-35. ⟨10.1074/jbc.M302618200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (33), pp.30927-35. ⟨10.1074/jbc.M302618200⟩
International audience; The highly conserved aspartyl-, asparaginyl-, and lysyl-tRNA synthetases compose one subclass of aminoacyl-tRNA synthetases, called IIb. The three enzymes possess an OB-folded extension at their N terminus. The function of thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::8e70014030dfa1a9d071115415e8e64a
https://hal-polytechnique.archives-ouvertes.fr/hal-00770714
https://hal-polytechnique.archives-ouvertes.fr/hal-00770714
Autor:
Gianluigi Desogus, Sylvain Blanquet, Pierre Plateau, Silvia Onesti, Peter Brick, Josiane Chen, Annie Brevet
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2000, 39 (42), pp.12853-61. ⟨10.1021/bi001487r⟩
Biochemistry, American Chemical Society, 2000, 39 (42), pp.12853-61. ⟨10.1021/bi001487r⟩
International audience; Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f95eb3acd18d6616bb7f5c059dc5c6d3
https://hal-polytechnique.archives-ouvertes.fr/hal-00771811
https://hal-polytechnique.archives-ouvertes.fr/hal-00771811
Publikováno v:
Proceedings of the National Academy of Sciences. 86:8275-8279
The role of aminoacyl-tRNA synthetases in the in vivo synthesis of adenylylated bis(5'-nucleosidyl) tetraphosphates (Ap4N) was studied by measuring the concentration of these nucleotides in Escherichia coli cells overproducing lysyl-, methionyl- phen
Publikováno v:
Journal of chromatography. 258
A new method for the purification of human erythrocyte phosphoglycerate-kinase involving affinity chromatography on dye-ligand media (Red A), in the presence of 3-phosphoglycerate and ATP, is described. The method is rapid and technically simple. The