AAAAAA

   
Results: 1-11 |
Results: 11
Interaction of bacterial lipopolysaccharide with mouse surfactant protein C inserted into lipid vesicles
Authors: Augusto, L Le Blay, K Auger, G Blanot, D Chaby, R
Citation: L. Augusto et al., Interaction of bacterial lipopolysaccharide with mouse surfactant protein C inserted into lipid vesicles, AM J P-LUNG, 281(4), 2001, pp. L776-L785
Synthesis and biochemical evaluation of some novel N-acyl phosphono- and phosphinoalanine derivatives as potential inhibitors of the D-glutamic acid-adding enzyme
Authors: Gobec, S Urleb, U Auger, G Blanot, D
Citation: S. Gobec et al., Synthesis and biochemical evaluation of some novel N-acyl phosphono- and phosphinoalanine derivatives as potential inhibitors of the D-glutamic acid-adding enzyme, PHARMAZIE, 56(4), 2001, pp. 295-297
Evidence of a functional requirement for a carbamoylated lysine residue inMurD, MurE and MufF synthetases as established by chemical rescue experiments
Authors: Dementin, S Bouhss, A Auger, G Parquet, C Mengin-Lecreulx, D Dideberg, O van Heijenoort, J Blanot, D
Citation: S. Dementin et al., Evidence of a functional requirement for a carbamoylated lysine residue inMurD, MurE and MufF synthetases as established by chemical rescue experiments, EUR J BIOCH, 268(22), 2001, pp. 5800-5807
The nitrogen source-dependent 126-kDa protein from Synechococcus PCC 7942 plasmalemma: A trimer of the NrtA nitrate-binding protein
Authors: Fresneau, C Zinovieva, M Blanot, D Batelier, G Arrio, B
Citation: C. Fresneau et al., The nitrogen source-dependent 126-kDa protein from Synechococcus PCC 7942 plasmalemma: A trimer of the NrtA nitrate-binding protein, IUBMB LIFE, 49(6), 2000, pp. 527-532
"Open" structures of MurD: Domain movements and structural similarities with folylpolyglutamate synthetase
Authors: Bertrand, JA Fanchon, E Martin, L Chantalat, L Auger, G Blanot, D van Heijenoort, J Dideberg, O
Citation: Ja. Bertrand et al., "Open" structures of MurD: Domain movements and structural similarities with folylpolyglutamate synthetase, J MOL BIOL, 301(5), 2000, pp. 1257-1266
Determination of the MurD mechanism through crystallographic analysis of enzyme complexes
Authors: Bertrand, JA Auger, G Martin, L Fanchon, E Blanot, D La Beller, D van Heijenoort, J Dideberg, O
Citation: Ja. Bertrand et al., Determination of the MurD mechanism through crystallographic analysis of enzyme complexes, J MOL BIOL, 289(3), 1999, pp. 579-590
Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-L-alanyl-D-glutamate : L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth
Authors: Mengin-Lecreulx, D Falla, T Blanot, D van Heijenoort, J Adams, DJ Chopra, I
Citation: D. Mengin-lecreulx et al., Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-L-alanyl-D-glutamate : L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth, J BACT, 181(19), 1999, pp. 5909-5914
Formation of adenosine 5 '-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli
Authors: Bouhss, A Dementin, S van Heijenoort, J Parquet, C Blanot, D
Citation: A. Bouhss et al., Formation of adenosine 5 '-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli, FEBS LETTER, 453(1-2), 1999, pp. 15-19
Reaction mechanism of phosphoglucosamine mutase from Escherichia coli (vol262, pg 202, 1999)
Authors: Jolly, L Ferrari, P Blanot, D van Heijenoort, J Fassy, F Mengin-Lecreulx, D
Citation: L. Jolly et al., Reaction mechanism of phosphoglucosamine mutase from Escherichia coli (vol262, pg 202, 1999), EUR J BIOCH, 262(3), 1999, pp. 947-947
Reaction mechanism of phosphoglucosamine mutase from Escherichia coli
Authors: Jolly, L Ferrari, P Blanot, D van Heijenoort, J Fassy, F Mengin-Lecreulx, D
Citation: L. Jolly et al., Reaction mechanism of phosphoglucosamine mutase from Escherichia coli, EUR J BIOCH, 262(1), 1999, pp. 202-210
Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine : D-glutamate ligase (MurD)
Authors: Bouhss, A Dementin, S Parquet, C Mengin-Lecreulx, D Bertrand, JA Le Beller, D Dideberg, O van Heijenoort, J Blanot, D
Citation: A. Bouhss et al., Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine : D-glutamate ligase (MurD), BIOCHEM, 38(38), 1999, pp. 12240-12247
Risultati: 1-11 |