Le cerveau multidimensionnel

Accueil du site Neuro-PSI > Départements > Molécules & Circuits > Equipe Hervé Daniel



  • S. Chardonnet, S. Sakr, C. Cassier-Chauvat, P. Le Maréchal, F. Chauvat, S. D. Lemaire and P. Decottignies (2015).
    First proteomic study of S-glutathionylation in cyanobacteria.
    Journal of Proteome Research, 14, 59-71.


  • Y. Zivanovic, F. Confalonieri, L. Ponchon, R. Lurz, M. Chami, A. Flayhan, M. Renouard, A. Huet, P. Decottignies, A.R. Davidson, C. Breyton and P. Boulanger (2014).
    Insights into bacteriophage T5 structure from the analysis of its morphogenesis genes and protein components.
    Journal of Virology, 88, 1162-1174.
  • C. Montigny, P. Decottignies, P. Le Maréchal, P. Capy, M. Bublitz, C. Olesen, J.V. Møller, P. Nissen, and M. le Maire (2014)
    S-Palmitoylation and S-oleylation of rabbit and pig sarcolipin.
    J. Biol. Chem., 289, 33850-3386.
  • H. Azouaoui, C. Montigny, M-R. Ash, F. Fijalkowski, A. Jacquot, C. Grønberg, R. López-Marqués, M. G. Palmgren, M. Garrigos, M. le Maire, P. Decottignies, P. Gourdon, P. Nissen, P. Champeil, and G. Lenoir (2014)
    A high-yield co-expression system for the purification of an intact Drs2p-Cdc50p lipid flippase complex, critically dependent on and stabilized by phosphatidylinositol-4-phosphate.
    PLos one, 9 (11):e112176. doi : 10.1371.


  • C. Berrier, A. Pozza, A. de Lacroix de Lavalette, S. Chardonnet, A. Mesneau, C. Jaxel, M. le Maire, and A. Ghazi, “The purified mechanosensitive channel TREK-1 is directly sensitive to membrane tension”, The Journal of biological chemistry. J. Biol. Chem., 288, 27307-27314.
  • P. Le Maréchal, P. Decottignies, C. H. Marchand, J. Degrouard, D. Jaillard, T. Dulermo, M. Froissard, A. Smirnov, V. Chapuis, and M. - J. Virolle, “Comparative proteomic analysis of the wild-type and the ppk mutant of Streptomyces lividans revealed the importance of storage lipids for antibiotic biosynthesis”, Applied and environmental microbiology. 79, 5907-5917.
  • B. Marteyn, S. Sakr, S. Farci, M. Bedhomme, S. Chardonnet, P. Decottignies, S. D. Lemaire, C. Cassier-Chauvat, and F. Chauvat, “The Synechocystis PCC6803 MerA-Like Enzyme Operates in the Reduction of Both Mercury and Uranium under the Control of the Glutaredoxin 1 Enzyme”, Journal of bacteriology, vol. 195, no. 18, p. 4138-4145.
  • P. Rath, O. Saurel, G. Czaplicki, M. Tropis, M. Daffé, A. Ghazi, P. Demange, and A. Milon, “Cord factor (trehalose 6,6’-dimycolate) forms fully stable and non-permeable lipid bilayers required for a functional outer membrane”, Biochimica et biophysica acta, vol. 1828, no. 9, p. 2173-2181.
  • S. Sakr, J. Dutheil, P. Saenkham, H. Bottin, C. Leplat, M. Ortega-Ramos, J. - C. Aude, V. Chapuis, G. Guedeney, P. Decottignies, S. Lemaire, C. Cassier-Chauvat, and F. Chauvat, “The activity of the Synechocystis PCC6803 AbrB2 regulator of hydrogen production can be post-translationally controlled through glutathionylation”, International Journal of Hydrogen Energy, 38, 13547-13555


  • K. Abitbol, H. McLean, T. Bessiron, and H. Daniel, “A new signalling pathway for parallel fibre presynaptic type 4 metabotropic glutamate receptors (mGluR4) in the rat cerebellar cortex”, The Journal of Physiology, vol. 590, no. 13, p. 2977-2994.
  • C. H. Marchand, C. Salmeron, R. Bou Raad, X. Méniche, M. Chami, M. Masi, D. Blanot, M. Daffé, M. Tropis, E. Huc, P. Le Maréchal, P. Decottignies, and N. Bayan, “Biochemical disclosure of the mycolate outer membrane of Corynebacterium glutamicum”, Journal of bacteriology, vol. 194, no. 3, p. 587-597.
  • C. Ramos, S. Chardonnet, C. H. Marchand, P. Decottignies, F. Ango, H. Daniel, and P. Le Maréchal, “Native presynaptic metabotropic glutamate receptor 4 (mGluR4) interacts with exocytosis proteins in rat cerebellum”, The Journal of biological chemistry, vol. 287, no. 24, p. 20176-20186.
  • M. Zaffagnini, M. Bedhomme, H. Groni, C. H. Marchand, C. Puppo, B. Gontero, C. Cassier-Chauvat, P. Decottignies, and S. D. Lemaire, “Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii : a proteomic survey”, Molecular & cellular proteomics : MCP, vol. 11, no. 2, p. M111.014142.


  • C. Berrier, I. Guilvout, N. Bayan, K. - H. Park, A. Mesneau, M. Chami, A. P. Pugsley, and A. Ghazi, “Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL MscL does not need the insertase YidC for insertion in vitro”, Biochimica et biophysica acta, vol. 1808, no. 1, p. 41-46.
  • F. Crépel, M. Galante, S. Habbas, H. McLean, and H. Daniel, “Role of the vesicular transporter VGLUT3 in retrograde release of glutamate by cerebellar Purkinje cells”, Journal of neurophysiology, vol. 105, no. 3, p. 1023-1032.
  • S. Habbas, F. Ango, H. Daniel, and M. Galante, “Purinergic signaling in the cerebellum : Bergmann glial cells express functional ionotropic P2X₇ receptors”, Glia, vol. 59, no. 12, p. 1800-1812.
  • M. P. Hortigón-Vinagre, S. Chardonnet, C. Montigny, Y. Gutiérrez-Martín, P. Champeil, and F. Henao, “Inhibition by 4-hydroxynonenal (HNE) of Ca2+ transport by SERCA1a : low concentrations of HNE open protein-mediated leaks in the membrane”, Free radical biology & medicine, vol. 50, no. 2, p. 323-336.
  • P. Rath, P. Demange, O. Saurel, M. Tropis, M. Daffe, V. Dotsch, A. Ghazi, F. Bernhard, and A. Milon, “Functional Expression of the PorAH Channel from Corynebacterium glutamicum in Cell-free Expression Systems : IMPLICATIONS FOR THE ROLE OF THE NATURALLY OCCURRING MYCOLIC ACID MODIFICATION”, Journal of Biological Chemistry, vol. 286, no. 37, p. 32525-32532.


  • A. Abdine, M. A. Verhoeven, K. - H. Park, A. Ghazi, E. Guittet, C. Berrier, C. Van Heijenoort, and D. E. Warschawski, “Structural study of the membrane protein MscL using cell-free expression and solid-state NMR”, Journal of magnetic resonance (San Diego, Calif. : 1997), vol. 204, no. 1, p. 155-159.
  • T. El Hage, S. Lorin, P. Decottignies, M. Djavaheri-Mergny, and F. Authier, “Proteolysis of Pseudomonas exotoxin A within hepatic endosomes by cathepsins B and D produces fragments displaying in vitro ADP-ribosylating and apoptotic effects”, The FEBS journal, vol. 277, no. 18, p. 3735-3749.
  • X. - H. Gao, M. Zaffagnini, M. Bedhomme, L. Michelet, C. Cassier-Chauvat, P. Decottignies, and S. D. Lemaire, “Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii : kinetics and specificity in deglutathionylation reactions”, FEBS letters, vol. 584, no. 11, p. 2242-2248.
  • E. Huc, X. Meniche, R. Benz, N. Bayan, A. Ghazi, M. Tropis, and M. Daffe, “O-Mycoloylated Proteins from Corynebacterium : AN UNPRECEDENTED POST-TRANSLATIONAL MODIFICATION IN BACTERIA”, Journal of Biological Chemistry, vol. 285, no. 29, p. 21908-21912.
  • C. H. Marchand, H. Vanacker, V. Collin, E. Issakidis-Bourguet, P. L. Maréchal, and P. Decottignies, “Thioredoxin targets in Arabidopsis roots”, Proteomics, vol. 10, no. 13, p. 2418-2428.
  • L. Tarrago, E. Laugier, M. Zaffagnini, C. H. Marchand, P. Le Maréchal, S. D. Lemaire, and P. Rey, “Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid”, The Journal of biological chemistry, vol. 285, no. 20, p. 14964-14972.


  • M. Bedhomme, M. Zaffagnini, C. H. Marchand, X. - H. Gao, M. Moslonka-Lefebvre, L. Michelet, P. Decottignies, and S. D. Lemaire, “Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii”, Journal of Biological Chemistry, vol. 284, no. 52, p. 36282-36291.
  • J. Couturier, C. S. Koh, M. Zaffagnini, A. M. Winger, J. M. Gualberto, C. Corbier, P. Decottignies, J. - P. Jacquot, S. D. Lemaire, C. Didierjean, and N. Rouhier, “Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site”, The Journal of biological chemistry, vol. 284, no. 14, p. 9299-9310.
  • F. Crepel, “Role of Presynaptic Kainate Receptors at Parallel Fiber-Purkinje Cell Synapses in Induction of Cerebellar LTD : Interplay With Climbing Fiber Input”, Journal of Neurophysiology, vol. 102, no. 2, p. 965-973.
  • C. Delarasse, P. Gonnord, M. Galante, R. Auger, H. Daniel, I. Motta, and J. M. Kanellopoulos, “Neural progenitor cell death is induced by extracellular ATP via ligation of P2X7 receptor”, Journal of neurochemistry, vol. 109, no. 3, p. 846-857.
  • C. Dietrich, A. Nato, B. Bost, P. Le Marechal, and A. Guyonvarch, “Regulation of ldh expression during biotin-limited growth of Corynebacterium glutamicum”, Microbiology, vol. 155, no. 4, p. 1360-1375.
  • M. Galante, H. Jani, L. Vanes, H. Daniel, E. M. C. Fisher, V. L. J. Tybulewicz, T. V. P. Bliss, and E. Morice, “Impairments in motor coordination without major changes in cerebellar plasticity in the Tc1 mouse model of Down syndrome”, Human molecular genetics, vol. 18, no. 8, p. 1449-1463.
  • M. Kaminska, S. Havrylenko, P. Decottignies, P. Le Marechal, B. Negrutskii, and M. Mirande, “Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells”, Journal of Biological Chemistry, vol. 284, no. 20, p. 13746-13754.
  • M. Kaminska, S. Havrylenko, P. Decottignies, S. Gillet, P. Le Maréchal, B. Negrutskii, and M. Mirande, “Dissection of the structural organization of the aminoacyl-tRNA synthetase complex”, The Journal of biological chemistry, vol. 284, no. 10, p. 6053-6060.
  • V. Preger, N. Tango, C. Marchand, S. D. Lemaire, D. Carbonera, M. Di Valentin, A. Costa, P. Pupillo, and P. Trost, “Auxin-responsive genes AIR12 code for a new family of plasma membrane b-type cytochromes specific to flowering plants”, Plant physiology, vol. 150, no. 2, p. 606-620.
  • N. Rolland, A. Atteia, P. Decottignies, J. Garin, M. Hippler, G. Kreimer, S. D. Lemaire, M. Mittag, and V. Wagner, “Chlamydomonas proteomics”, Current opinion in microbiology, vol. 12, no. 3, p. 285-291.
  • L. Tarrago, E. Laugier, M. Zaffagnini, C. Marchand, P. Le Maréchal, N. Rouhier, S. D. Lemaire, and P. Rey, “Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins”, The Journal of biological chemistry, vol. 284, no. 28, p. 18963-18971.


  • K. Abitbol, F. Acher, and H. Daniel, “Depression of excitatory transmission at PF-PC synapse by group III metabotropic glutamate receptors is provided exclusively by mGluR4 in the rodent cerebellar cortex”, Journal of neurochemistry, vol. 105, no. 6, p. 2069-2079.
  • S. Chardonnet, P. Le Marechal, H. Cheval, J. - P. Le Caer, P. Decottignies, O. Laprevote, S. Laroche, and S. Davis, “Large-scale study of phosphoproteins involved in long-term potentiation in the rat dentate gyrus in vivo”, The European journal of neuroscience, vol. 27, no. 11, p. 2985-2998.
  • T. El Hage, P. Decottignies, and F. Authier, “Endosomal proteolysis of diphtheria toxin without toxin translocation into the cytosol of rat liver in vivo”, The FEBS journal, vol. 275, no. 8, p. 1708-1722.
  • C. Fabret, B. Cosnier, S. Lekomtsev, S. Gillet, I. Hatin, P. Le Maréchal, and J. Rousset, “A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability”, BMC Molecular Biology, vol. 9, no. 1, p. 22.
  • I. Guilvout, M. Chami, C. Berrier, A. Ghazi, A. Engel, A. P. Pugsley, and N. Bayan, “In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD”, Journal of molecular biology, vol. 382, no. 1, p. 13-23.
  • L. Michelet, M. Zaffagnini, H. Vanacker, P. Le Maréchal, C. Marchand, M. Schroda, S. D. Lemaire, and P. Decottignies, “In vivo targets of S-thiolation in Chlamydomonas reinhardtii”, The Journal of biological chemistry, vol. 283, no. 31, p. 21571-21578.
  • S. L. Poh, F. el Khadali, C. Berrier, R. Lurz, R. Melki, and P. Tavares, “Oligomerization of the SPP1 scaffolding protein”, Journal of molecular biology, vol. 378, no. 3, p. 551-564.
  • J. Ster, F. de Bock, F. Bertaso, K. Abitbol, H. Daniel, J. Bockaert, and L. Fagni, “Epac mediates PACAP-dependent long-term depression in the hippocampus”, The Journal of Physiology, vol. 587, no. 1, p. 101-113.


  • F. Crepel, “Developmental Changes in Retrograde Messengers Involved in Depolarization-Induced Suppression of Excitation at Parallel Fiber-Purkinje Cell Synapses in Rodents”, Journal of Neurophysiology, vol. 97, no. 1, p. 824-836.
  • F. Crepel and H. Daniel, “Developmental changes in agonist-induced retrograde signaling at parallel fiber-Purkinje cell synapses : role of calcium-induced calcium release”, Journal of neurophysiology, vol. 98, no. 5, p. 2550-2565.
  • K. Le Meur, M. Galante, M. C. Angulo, and E. Audinat, “Tonic activation of NMDA receptors by ambient glutamate of non-synaptic origin in the rat hippocampus”, The Journal of physiology, vol. 580, no. Pt. 2, p. 373-383.
  • L. J. Wrobel, M. Ogier, F. Chatonnet, S. Autran, V. Mézières, M. Thoby-Brisson, H. McLean, C. Taeron, and J. Champagnat, “Abnormal inspiratory depth in Phox2a haploinsufficient mice”, Neuroscience, vol. 145, no. 1, p. 384-392.
  • M. Zaffagnini, L. Michelet, C. Marchand, F. Sparla, P. Decottignies, P. Le Maréchal, M. Miginiac-Maslow, G. Noctor, P. Trost, and S. D. Lemaire, “The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation”, The FEBS journal, vol. 274, no. 1, p. 212-226.


  • F. Chatonnet, C. Borday, L. Wrobel, M. Thoby-Brisson, G. Fortin, H. McLean, and J. Champagnat, “Ontogeny of central rhythm generation in chicks and rodents”, Respiratory physiology & neurobiology, vol. 154, no. 1-2, p. 37-46.
  • S. Gillet, P. Decottignies, S. Chardonnet, and P. Le Maréchal, “Cadmium response and redoxin targets in Chlamydomonas reinhardtii : a proteomic approach”, Photosynthesis research, vol. 89, no. 2-3, p. 201-211.
  • S. Graziani, J. Bernauer, S. Skouloubris, M. Graille, C. - Z. Zhou, C. Marchand, P. Decottignies, H. van Tilbeurgh, H. Myllykallio, and U. Liebl, “Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX”, The Journal of biological chemistry, vol. 281, no. 33, p. 24048-24057.
  • E. Issakidis-Bourguet, D. Lavergne, X. Trivelli, P. Decottignies, and M. Miginiac-Maslow, “Transferring redox regulation properties from sorghum NADP-malate dehydrogenase to Thermus NAD-malate dehydrogenase”, Photosynthesis research, vol. 89, no. 2-3, p. 213-223.
  • C. Marchand, P. Le Maréchal, Y. Meyer, and P. Decottignies, “Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin”, Proteomics, vol. 6, no. 24, p. 6528-6537.


  • M. Lepoivre, C. Houée-Levin, K. Coeytaux, P. Decottignies, G. Auger, and G. Lemaire, “Nitration of the tyrosyl radical in ribonucleotide reductase by nitrogen dioxide : a gamma radiolysis study”, Free radical biology & medicine, vol. 38, no. 11, p. 1511-1517.
  • L. Michelet, M. Zaffagnini, C. Marchand, V. Collin, P. Decottignies, P. Tsan, J. - M. Lancelin, P. Trost, M. Miginiac-Maslow, G. Noctor, and S. D. Lemaire, “Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants”, Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 45, p. 16478-16483.
  • K. Sii-Felice, C. Pouponnot, S. Gillet, L. Lecoin, J. - A. Girault, A. Eychène, and M. - P. Felder-Schmittbuhl, “MafA transcription factor is phosphorylated by p38 MAP kinase”, FEBS letters, vol. 579, no. 17, p. 3547-3554.


  • S.D. Lemaire, B. Guillon, P. Le Maréchal, E. Keryer, M. Miginiac-Maslow and P. Decottignies (2004). New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA, 101, 7475-7480.
  • G. Boël, V. Pichereau, I. Mijakovic, A. Mazé, S. Poncet, S. Gillet, J. - C. Giard, A. Hartke, Y. Auffray, and J. Deutscher, “Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export ?”, Journal of molecular biology, vol. 337, no. 2, p. 485-496.
  • L. Bousset, V. Redeker, P. Decottignies, S. Dubois, P. Le Maréchal, and R. Melki, “Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p”, Biochemistry, vol. 43, no. 17, p. 5022-5032.
  • H. Daniel, A. Rancillac, and F. Crepel, “Mechanisms underlying cannabinoid inhibition of presynaptic Ca2+ influx at parallel fibre synapses of the rat cerebellum”, The Journal of physiology, vol. 557, no. Pt 1, p. 159-174.
  • G. Lenoir, M. Picard, C. Gauron, C. Montigny, P. Le Maréchal, P. Falson, M. Le Maire, J. V. Møller, and P. Champeil, “Functional properties of sarcoplasmic reticulum Ca(2+)-ATPase after proteolytic cleavage at Leu119-Lys120, close to the A-domain”, The Journal of biological chemistry, vol. 279, no. 10, p. 9156-9166.
  • C. Marchand, P. Le Maréchal, Y. Meyer, M. Miginiac-Maslow, E. Issakidis-Bourguet, and P. Decottignies, “New targets of Arabidopsis thioredoxins revealed by proteomic analysis”, Proteomics, vol. 4, no. 9, p. 2696-2706.
  • C. Sicard-Roselli, S. Lemaire, J. - P. Jacquot, V. Favaudon, C. Marchand, and C. Houée-Levin, “Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation”, European journal of biochemistry / FEBS, vol. 271, no. 17, p. 3481-3487.


  • L. A. Augusto, P. Decottignies, M. Synguelakis, M. Nicaise, P. Le Maréchal, and R. Chaby, “Histones : a novel class of lipopolysaccharide-binding molecules”, Biochemistry, vol. 42, no. 13, p. 3929-3938.
  • V. Collin, E. Issakidis-Bourguet, C. Marchand, M. Hirasawa, J. - M. Lancelin, D. B. Knaff, and M. Miginiac-Maslow, “The Arabidopsis plastidial thioredoxins : new functions and new insights into specificity”, The Journal of biological chemistry, vol. 278, no. 26, p. 23747-23752.
  • P. Decottignies, V. Flesch, C. Gérard-Hirne, and P. Le Maréchal, “Role of positively charged residues in Chlamydomonas reinhardtii ferredoxin-NADP+-reductase”, Plant Physiology and Biochemistry, vol. 41, no. 6-7, p. 637-642.


  • A. Goyer, C. Haslekås, M. Miginiac-Maslow, U. Klein, P. Le Marechal, J. - P. Jacquot, and P. Decottignies, “Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii”, European journal of biochemistry / FEBS, vol. 269, no. 1, p. 272-282.
  • J. V. Möller, G. Lenoir, C. Marchand, C. Montigny, M. le Maire, C. Toyoshima, B. S. Juul, and P. Champeil, “Calcium transport by sarcoplasmic reticulum Ca(2+)-ATPase. Role of the A domain and its C-terminal link with the transmembrane region”, The Journal of biological chemistry, vol. 277, no. 41, p. 38647-38659.


  • A. Goyer, P. Decottignies, E. Issakidis-Bourguet, and M. Miginiac-Maslow, “Sites of interaction of thioredoxin with sorghum NADP-malate dehydrogenase”, FEBS letters, vol. 505, no. 3, p. 405-408.


  • I. Schepens, P. Decottignies, E. Ruelland, K. Johansson, and M. Miginiac-Maslow, “The dimer contact area of sorghum NADP-malate dehydrogenase : role of aspartate 101 in dimer stability and catalytic activity”, FEBS letters, vol. 471, no. 2-3, p. 240-244.
  • I. Schepens, E. Ruelland, M. Miginiac-Maslow, P. Le Maréchal, and P. Decottignies, “The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity”, The Journal of biological chemistry, vol. 275, no. 46, p. 35792-35798.


  Webmaster Plan du site Planning Crédits
Syndication RSS  
  Format Mobiles
  Dev-Evo Cog-Comp Mol-Circ