Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Jean Claude Drapier"'
Autor:
Sylvie Riquier, Jacques Breton, Kahina Abbas, David Cornu, Cécile Bouton, Jean-Claude Drapier
Publikováno v:
Redox Biology, Vol 2, Iss C, Pp 777-785 (2014)
Peroxiredoxins (Prxs) are a family of thiol peroxidases that participate in hydroperoxide detoxification and regulates H2O2 signaling. In mammals, the four typical 2-Cys Prxs (Prxs 1, 2, 3 and 4) are known to regulate H2O2-mediated intracellular sign
Externí odkaz:
https://doaj.org/article/f8e73d3b7f2f4fe8a1b385d782b1cb02
Autor:
Jean-Claude Drapier, Michel B. Toledano, Jacques Breton, Jérôme Bignon, Anne-Gaëlle Planson, Cécile Bouton, Kahina Abbas, Cendrine Seguin, Sylvie Riquier
Publikováno v:
Free Radical Biology and Medicine
Free Radical Biology and Medicine, Elsevier, 2011, 51 (1), pp.107-114. ⟨10.1016/j.freeradbiomed.2011.03.039⟩
Free Radical Biology and Medicine, Elsevier, 2011, 51 (1), pp.107-114. ⟨10.1016/j.freeradbiomed.2011.03.039⟩
International audience; Malaria represents a major public health problem and an important cause of mortality and morbidity. The malaria parasites are becoming resistant to drugs used to treat the disease and still no efficient vaccine has been develo
Autor:
Marie Wattenhofer-Donzé, Jean-Claude Drapier, Blanche Guillon, Bertrand Friguet, Anne-Laure Bulteau, Hélène Puccio, Stéphane Schmucker, Cécile Bouton
Publikováno v:
FEBS Journal. 276:1036-1047
Friedreich ataxia (FRDA) is a rare hereditary neurodegenerative disease characterized by progressive ataxia and cardiomyopathy. The cause of the disease is a defect in mitochondrial frataxin, an iron chaperone involved in the maturation of Fe-S clust
Publikováno v:
Archives of Biochemistry and Biophysics
Archives of Biochemistry and Biophysics, Elsevier, 2007, 465 (1), pp.282-92. ⟨10.1016/j.abb.2007.06.003⟩
Archives of Biochemistry and Biophysics, Elsevier, 2007, 465 (1), pp.282-92. ⟨10.1016/j.abb.2007.06.003⟩
International audience; Biogenesis of iron-sulfur (Fe-S) clusters in mammals involves a complex mitochondrial machinery that provides inorganic sulfide and iron for their assembly and insertion into apo-proteins. Mechanisms of Fe-S cluster assembly a
Autor:
Marie-Jeanne Chauveau, Michel Negrerie, Martin-Pierre Sauviat, Anthony Colas, Jean-Claude Drapier
Publikováno v:
Journal of Natural Products
Journal of Natural Products, American Chemical Society, 2007, 70 (4), pp.510-514. ⟨10.1021/np060309h⟩
Journal of Natural Products, American Chemical Society, 2007, 70 (4), pp.510-514. ⟨10.1021/np060309h⟩
The effects and the mode of action of hypericin (1) were studied, in the dark, on the action potential (AP) and the L-type Ca2+ channel of frog atrial heart muscle, using intracellular microelectrode and patch-clamp techniques, respectively. In the p
Autor:
Jean-Claude Drapier, Ana Sofia Gonçalves, Françoise Muzeau, Ewa Smuda, Paweł Lipiński, Rafał R. Starzyński, Zofia Tyrolczyk, Carole Beaumont
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 2006, 400(Part2), pp.367-375. ⟨10.1042/BJ20060623⟩
Biochemical Journal, Portland Press, 2006, 400(Part2), pp.367-375. ⟨10.1042/BJ20060623⟩
RNA-binding activity of IRP1 (iron regulatory protein 1) is regulated by the insertion/extrusion of a [4Fe-4S] cluster into/from the IRP1 molecule. NO (nitic oxide), whose ability to activate IRP1 by removing its [4Fe-4S] cluster is well known, has a
Autor:
Marie-Jeanne Chauveau, Cécile Bouton, Blanche Guillon, Jean-Claude Drapier, Cédric Fosset, Frédéric Canal
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281(35), pp.25398-25406. ⟨10.1074/jbc.M602979200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281(35), pp.25398-25406. ⟨10.1074/jbc.M602979200⟩
In prokaryotes and yeast, the general mechanism of biogenesis of iron-sulfur (Fe-S) clusters involves activities of several proteins among which IscS and Nfs1p provide, through cysteine desulfuration, elemental sulfide for Fe-S core formation. Althou
Publikováno v:
Journal of Biological Chemistry. 279:43345-43351
Iron regulatory protein-1 (IRP-1) is a bifunctional [4Fe-4S] protein that functions as a cytosolic aconitase or as a trans-regulatory factor controlling iron homeostasis at a post-transcriptional level. Because IRP-1 is a sensitive target protein for
Autor:
Tony A. Mattioli, Charilaos Goussias, Jean-Claude Drapier, Emmanuelle Soum, Cécile Bouton, Jean-Marc Moulis, Xavier Brazzolotto
Publikováno v:
Biochemistry. 42:7648-7654
Iron regulatory protein 1 (IRP1) is a redox-sensitive protein which exists in two active forms in the cytosol of eukaryotic cells. Holo-IRP1 containing a [4Fe-4S] cluster exhibits aconitase activity which catalyzes the isomerization of citrate and is
Publikováno v:
Journal of Biological Chemistry. 277:31220-31227
Iron regulatory proteins (IRPs) control iron metabolism by specifically interacting with iron-responsive elements (IREs) on mRNAs. Nitric oxide (NO) converts IRP-1 from a [4Fe-4S] aconitase to a trans-regulatory protein through Fe-S cluster disassemb