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The Journal of Biological Chemistry|July 29, 2004
Evidence for a new sub-class of methionine sulfoxide reductases B with an alternative thioredoxin recognition signatureFabrice Neiers, Alexandre Kriznik, Sandrine Boschi-Muller, et al.
Chemico-Biological Interactions|November 26, 2008
Stabilization and conformational isomerization of the cofactor during the catalysis in hydrolytic ALDHsFrançois Talfournier, Arnaud Pailot, Claire Stinès-Chaumeil, et al.
The Journal of Biological Chemistry|May 15, 2007
Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase AAdeline Gand, Mathias Antoine, Sandrine Boschi-Muller, et al.
FEBS Letters|January 18, 2011
The rate-limiting step of sulfiredoxin is associated with the transfer of the γ-phosphate of ATP to the sulfinic acid of overoxidized typical 2-Cys peroxiredoxinsXavier Roussel, Samia Boukhenouna, Sophie Rahuel-Clermont, et al.
The Journal of Biological Chemistry|May 22, 2010
Structural and biochemical characterization of free methionine-R-sulfoxide reductase from Neisseria meningitidisArnaud Gruez, Marouane Libiad, Sandrine Boschi-Muller, et al.
Biochimica Et Biophysica Acta|February 1, 2005
The enzymology and biochemistry of methionine sulfoxide reductasesSandrine Boschi-Muller, Alexandre Olry, Mathias Antoine, et al.
The Journal of Biological Chemistry|January 26, 2005
The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductasesJunzhu Wu, Fabrice Neiers, Sandrine Boschi-Muller, et al.
The Journal of Biological Chemistry|October 26, 2006
Characterization of the amino acids from Neisseria meningitidis MsrA involved in the chemical catalysis of the methionine sulfoxide reduction stepMathias Antoine, Adeline Gand, Sandrine Boschi-Muller, et al.
FEBS Letters|May 17, 2011
Thioredoxin 2 from Escherichia coli is not involved in vivo in the recycling process of methionine sulfoxide reductase activitiesChristophe Jacob, Alexandre Kriznik, Sandrine Boschi-Muller, et al.
Biochemistry|June 12, 2002
Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusOlivier Roitel, Olga Ivinova, Vladimir Muronetz, et al.
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