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Results: 1-15 |
Results: 15
Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
Authors: Issakidis-Bourguet, E Mouaheb, N Meyer, Y Miginiac-Maslow, M
Citation: E. Issakidis-bourguet et al., Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin, PLANT J, 25(2), 2001, pp. 127-135
Light-activation of NADP-malate dehydrogenase: A highly controlled processfor an optimized function
Authors: Miginiac-Maslow, M Johansson, K Ruelland, E Issakidis-Bourguet, E Schepens, I Goyer, A Lemaire-Chamley, M Jacquot, JP Le Marechal, P Decottignies, P
Citation: M. Miginiac-maslow et al., Light-activation of NADP-malate dehydrogenase: A highly controlled processfor an optimized function, PHYSL PLANT, 110(3), 2000, pp. 322-329
The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity
Authors: Schepens, I Ruelland, E Miginiac-Maslow, M Le Marechal, P Decottignies, P
Citation: I. Schepens et al., The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity, J BIOL CHEM, 275(46), 2000, pp. 35792-35798
Inhibition of the thioredoxin-dependent activation of the NADP-malate dehydrogenase and cofactor specificity
Authors: Schepens, I Johansson, K Decottignies, P Gillibert, M Hirasawa, M Knaff, DB Miginiac-Maslow, M
Citation: I. Schepens et al., Inhibition of the thioredoxin-dependent activation of the NADP-malate dehydrogenase and cofactor specificity, J BIOL CHEM, 275(28), 2000, pp. 20996-21001
Mechanism of activation of the chloroplast ATP synthase - A kinetic study of the thiol modulation of isolated ATPase and membrane-bound ATP synthase from spinach by Escherichia coli thioredoxin
Authors: He, XD Miginiac-Maslow, M Sigalat, C Keryer, E Haraux, F
Citation: Xd. He et al., Mechanism of activation of the chloroplast ATP synthase - A kinetic study of the thiol modulation of isolated ATPase and membrane-bound ATP synthase from spinach by Escherichia coli thioredoxin, J BIOL CHEM, 275(18), 2000, pp. 13250-13258
The dimer contact area of sorghum NADP-malate dehydrogenase: role of aspartate 101 in dimer stability and catalytic activity
Authors: Schepens, I Decottignies, P Ruelland, E Johansson, K Miginiac-Maslow, M
Citation: I. Schepens et al., The dimer contact area of sorghum NADP-malate dehydrogenase: role of aspartate 101 in dimer stability and catalytic activity, FEBS LETTER, 471(2-3), 2000, pp. 240-244
Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase
Authors: Hirasawa, M Ruelland, E Schepens, I Issakidis-Bourguet, E Miginiac-Maslow, M Knaff, DB
Citation: M. Hirasawa et al., Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase, BIOCHEM, 39(12), 2000, pp. 3344-3350
Regulation of chloroplast enzyme activities by thioredoxins: activation orrelief from inhibition?
Authors: Ruelland, E Miginiac-Maslow, M
Citation: E. Ruelland et M. Miginiac-maslow, Regulation of chloroplast enzyme activities by thioredoxins: activation orrelief from inhibition?, TRENDS PL S, 4(4), 1999, pp. 136-141
Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase
Authors: Chiadmi, M Navaza, A Miginiac-Maslow, M Jacquot, JP Cherfils, J
Citation: M. Chiadmi et al., Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase, EMBO J, 18(23), 1999, pp. 6809-6815
The complex regulation of ferredoxin/thioredoxin-related genes by light and the circadian clock
Authors: Lemaire, SD Stein, M Issakidis-Bourguet, E Keryer, E Benoit, V Pineau, B Gerard-Hirne, C Miginiac-Maslow, M Jacquot, JP
Citation: Sd. Lemaire et al., The complex regulation of ferredoxin/thioredoxin-related genes by light and the circadian clock, PLANTA, 209(2), 1999, pp. 221-229
Heavy-metal regulation of thioredoxin gene expression in Chlamydomonas reinhardtii
Authors: Lemaire, S Keryer, E Stein, M Schepens, I Issakidis-Bourguet, E Gerard-Hirne, C Miginiac-Maslow, M Jacquot, JP
Citation: S. Lemaire et al., Heavy-metal regulation of thioredoxin gene expression in Chlamydomonas reinhardtii, PLANT PHYSL, 120(3), 1999, pp. 773-778
Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition
Authors: Krimm, I Goyer, A Issakidis-Bourguet, E Miginiac-Maslow, M Lancelin, JM
Citation: I. Krimm et al., Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition, J BIOL CHEM, 274(49), 1999, pp. 34539-34542
The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin
Authors: Goyer, A Decottignies, P Lemaire, S Ruelland, E Issakidis-Bourguet, E Jacquot, JP Miginiac-Maslow, M
Citation: A. Goyer et al., The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin, FEBS LETTER, 444(2-3), 1999, pp. 165-169
Structural basis for light activation of a chloroplast enzyme: The structure of sorghum NADP-malate dehydrogenase in its oxidized form
Authors: Johansson, K Ramaswamy, S Saarinen, M Lemaire-Chamley, M Issakidis-Bourguet, E Miginiac-Maslow, M Eklund, H
Citation: K. Johansson et al., Structural basis for light activation of a chloroplast enzyme: The structure of sorghum NADP-malate dehydrogenase in its oxidized form, BIOCHEM, 38(14), 1999, pp. 4319-4326
The autoinhibition of sorghum NADP malate dehydrogenase is mediated by a C-terminal negative charge
Authors: Ruelland, E Johansson, K Decottignies, P Djukic, N Miginiac-Maslow, M
Citation: E. Ruelland et al., The autoinhibition of sorghum NADP malate dehydrogenase is mediated by a C-terminal negative charge, J BIOL CHEM, 273(50), 1998, pp. 33482-33488
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