Boschi-Muller S - Search Results

1

The X-ray structure of the N-terminal domain of PILB from Neisseria meningitidis reveals a thioredoxin-fold.

Ranaivoson FM, Kauffmann B, Neiers F, Wu J, Boschi-Muller S, Panjikar S, Aubry A, Branlant G, Favier F. Ranaivoson FM, et al. J Mol Biol. 2006 Apr 28;358(2):443-54. doi: 10.1016/j.jmb.2006.02.025. Epub 2006 Feb 28. J Mol Biol. 2006. PMID: 16530221

2

Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase.

Boschi-Muller S, Azza S, Pollastro D, Corbier C, Branlant G. Boschi-Muller S, et al. J Biol Chem. 1997 Jun 13;272(24):15106-12. doi: 10.1074/jbc.272.24.15106. J Biol Chem. 1997. PMID: 9182530 Free article.

3

Characterization of Escherichia coli strains with gapA and gapB genes deleted.

Seta FD, Boschi-Muller S, Vignais ML, Branlant G. Seta FD, et al. J Bacteriol. 1997 Aug;179(16):5218-21. doi: 10.1128/jb.179.16.5218-5221.1997. J Bacteriol. 1997. PMID: 9260967 Free PMC article.

4

Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity.

Boschi-Muller S, Muller S, Van Dorsselaer A, Böck A, Branlant G. Boschi-Muller S, et al. FEBS Lett. 1998 Nov 20;439(3):241-5. doi: 10.1016/s0014-5793(98)01377-5. FEBS Lett. 1998. PMID: 9845330 Free article.

5

The active site of phosphorylating glyceraldehyde-3-phosphate dehydrogenase is not designed to increase the nucleophilicity of a serine residue.

Boschi-Muller S, Branlant G. Boschi-Muller S, et al. Arch Biochem Biophys. 1999 Mar 15;363(2):259-66. doi: 10.1006/abbi.1998.1080. Arch Biochem Biophys. 1999. PMID: 10068447

6

Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.

Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S. Fillinger S, et al. J Biol Chem. 2000 May 12;275(19):14031-7. doi: 10.1074/jbc.275.19.14031. J Biol Chem. 2000. PMID: 10799476 Free article.

7

Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli.

Tête-Favier F, Cobessi D, Leonard GA, Azza S, Talfournier F, Boschi-Muller S, Branlant G, Aubry A. Tête-Favier F, et al. Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1194-7. doi: 10.1107/s0907444900009483. Acta Crystallogr D Biol Crystallogr. 2000. PMID: 10957644

8

A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.

Boschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, Branlant G. Boschi-Muller S, et al. J Biol Chem. 2000 Nov 17;275(46):35908-13. doi: 10.1074/jbc.M006137200. J Biol Chem. 2000. PMID: 10964927 Free article.

9

Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution.

Tête-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A. Tête-Favier F, et al. Structure. 2000 Nov 15;8(11):1167-78. doi: 10.1016/s0969-2126(00)00526-8. Structure. 2000. PMID: 11080639 Free article.

10

E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide.

Boschi-Muller S, Azza S, Branlant G. Boschi-Muller S, et al. Protein Sci. 2001 Nov;10(11):2272-9. doi: 10.1110/ps.10701. Protein Sci. 2001. PMID: 11604533 Free PMC article.

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