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Results: 1-8 |
Results: 8
Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability
Authors: Tehei, M Madern, D Pfister, C Zaccai, G
Citation: M. Tehei et al., Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability, P NAS US, 98(25), 2001, pp. 14356-14361
Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation
Authors: Steen, IH Madern, D Karlstrom, M Lien, T Ladenstein, R Birkeland, NK
Citation: Ih. Steen et al., Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation, J BIOL CHEM, 276(47), 2001, pp. 43924-43931
S179D-human PRL, a pseudophosphorylated human PRL analog, is an agonist and not an antagonist
Authors: Bernichtein, S Kinet, S Jeay, S Llovera, M Madern, D Martial, JA Kelly, PA Goffin, V
Citation: S. Bernichtein et al., S179D-human PRL, a pseudophosphorylated human PRL analog, is an agonist and not an antagonist, ENDOCRINOL, 142(9), 2001, pp. 3950-3963
Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus
Authors: Madern, D Ebel, C Dale, HA Lien, T Steen, IH Birkeland, NK Zaccai, G
Citation: D. Madern et al., Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus, BIOCHEM, 40(34), 2001, pp. 10310-10316
Halophilic adaptation of enzymes
Authors: Madern, D Ebel, C Zaccai, G
Citation: D. Madern et al., Halophilic adaptation of enzymes, EXTREMOPHIL, 4(2), 2000, pp. 91-98
The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase
Authors: Madern, D
Citation: D. Madern, The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase, MOL MICROB, 37(6), 2000, pp. 1515-1520
Halophilic adaptation: Novel solvent protein interactions observed in the 2.9 and 2.6 a resolution structures of the wild type and a mutant of malatedehydrogenase from Haloarcula marismortui
Authors: Richard, SB Madern, D Garcin, E Zaccai, G
Citation: Sb. Richard et al., Halophilic adaptation: Novel solvent protein interactions observed in the 2.9 and 2.6 a resolution structures of the wild type and a mutant of malatedehydrogenase from Haloarcula marismortui, BIOCHEM, 39(5), 2000, pp. 992-1000
Insights into the molecular relationships between malate and lactate dehydrogenases: Structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Holorcula marismortui
Authors: Madern, D Ebel, C Mevarech, M Richard, SB Pfister, C Zaccai, G
Citation: D. Madern et al., Insights into the molecular relationships between malate and lactate dehydrogenases: Structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Holorcula marismortui, BIOCHEM, 39(5), 2000, pp. 1001-1010
Risultati: 1-8 |