Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nathalie Rouviere"'
Publikováno v:
Biochemistry. 33:798-806
Flavocytochrome b2 catalyzes the oxidation of lactate at the expense of cytochrome c. After flavin (FMN) reduction by the substrate, reducing equivalents are transferred one by one to heme b2, and from there on to cytochrome c. The crystal structure
Autor:
Chantal Jouteau-Neves, Evelyne Malaquin-Pavan, Martine Nectoux-Lannebere, Patra Ahya, Anne Bahuaud, Anne-Marie Beguin, Marie-Fleur Bernard, Simone Bevan, Isabelle Bonnefondleurs, Christiane Bouillet, Françoise Boule, Martine Combes, Yvette Corvez, Marie-Claude Daydé, Agnès Deroual, Agnès Duremberg, Barbara Edda Messi, Christiane Elias, Margot Estrate, Françoise Ginet, Odile Guillaume, Anne Hamida, Marie-Gabrielle Hentgen, Patrick Javel, Brigitte Jeannin, Frédérique Lapierre, Annelyse Lemaitre, Chantal Loubere, Hedwige Marchand, Domitille Peureux, Marylène Pierrot, Nathalie Rouviere, Patrick Thominet, Delphine Vitry, Chantal Villevieille, Lucy Warren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a6bd0b8423ee3b8efe527bed4e0249d
https://doi.org/10.1016/b978-2-294-70679-0.50010-6
https://doi.org/10.1016/b978-2-294-70679-0.50010-6
Publikováno v:
Biochemistry. 36(24)
The interaction of the immunophilin domain of FKBP59 (FKBP59-I) with immunosuppressant drugs was investigated by steady-state and time-resolved fluorescence of tryptophan. One of the two Trp residues present in this protein (W89), conserved in almost
Autor:
Joël Mispelter, Constantin T. Craescu, Nathalie Rouviere, Esther Cerpolini, A. Popescu, Marie-Claire Lebeau, Etienne-Emile Baulieu
Publikováno v:
Biochemistry. 35(34)
FKBP59 is a protein usually associated with heat-shock protein hsp90 and steroid receptors. The N-terminal domain of the rabbit liver protein (149 amino acids) has a sequence homology with FKBP12, binds FK506 immunosuppressor, and has a peptidyl-prol
Autor:
Mariella Tegoni, Martine Mayer, Florence Lederer, Chantal Capeillère-Blandin, Nathalie Rouviere-Fourmy
Publikováno v:
Biochemical Society Transactions. 24:15S-15S