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Results: 1-9 |
Results: 9
E-coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide
Authors: Boschi-Muller, S Azza, S Branlant, G
Citation: S. Boschi-muller et al., E-coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide, PROTEIN SCI, 10(11), 2001, pp. 2272-2279
Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 angstrom resolution
Authors: Tete-Favier, F Cobessi, D Boschi-Muller, S Azza, S Branlant, G Aubry, A
Citation: F. Tete-favier et al., Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 angstrom resolution, STRUCTURE, 8(11), 2000, pp. 1167-1178
Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli
Authors: Tete-Favier, F Cobessi, D Leonard, GA Azza, S Talfournier, F Boschi-Muller, S Branlant, G Aubry, A
Citation: F. Tete-favier et al., Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli, ACT CRYST D, 56, 2000, pp. 1194-1197
A sulfenic acid enzyme intermediate is involved in the catalytic mechanismof peptide methionine sulfoxide reductase from Escherichia coli
Authors: Boschi-Muller, S Azza, S Sanglier-Cianferani, S Talfournier, F Van Dorsselear, A Branlant, G
Citation: S. Boschi-muller et al., A sulfenic acid enzyme intermediate is involved in the catalytic mechanismof peptide methionine sulfoxide reductase from Escherichia coli, J BIOL CHEM, 275(46), 2000, pp. 35908-35913
Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
Authors: Fillinger, S Boschi-Muller, S Azza, S Dervyn, E Branlant, G Aymerich, S
Citation: S. Fillinger et al., Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium, J BIOL CHEM, 275(19), 2000, pp. 14031-14037
Modelling the active site of glyceraldehyde-3 phosphate dehydrogenase withthe LSCF formalism
Authors: Cartier, A Brown, D Maigret, B Boschi-Muller, S Rahuel-Clermont, S Branlant, G
Citation: A. Cartier et al., Modelling the active site of glyceraldehyde-3 phosphate dehydrogenase withthe LSCF formalism, THEOR CH AC, 101(1-3), 1999, pp. 241-245
Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry
Authors: Levashov, P Orlov, V Boschi-Muller, S Talfournier, F Asryants, R Bulatnikov, I Muronetz, V Branlant, G Nagradova, N
Citation: P. Levashov et al., Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry, BBA-PROT ST, 1433(1-2), 1999, pp. 294-306
Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities
Authors: Schmalhausen, EV Nagradova, NK Boschi-Muller, S Branlant, G Muronetz, VI
Citation: Ev. Schmalhausen et al., Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities, FEBS LETTER, 452(3), 1999, pp. 219-222
The active site of phosphorylating glyceraldehyde-3-phosphate dehydrogenase is not designed to increase the nucleophilicity of a serine residue
Authors: Boschi-Muller, S Branlant, G
Citation: S. Boschi-muller et G. Branlant, The active site of phosphorylating glyceraldehyde-3-phosphate dehydrogenase is not designed to increase the nucleophilicity of a serine residue, ARCH BIOCH, 363(2), 1999, pp. 259-266
Risultati: 1-9 |