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Biotechnology and Bioengineering|July 22, 2008
New formulae for folding catalysts make them multi-purpose enzymesM Moutiez, R Guthapfel, P Gueguen, et al.
FEBS Letters|September 15, 2001
Interaction of human cyclophilin hCyp-18 with short peptides suggests the existence of two functionally independent subsitesL Demange, M Moutiez, K Vaudry, et al.
Nature|January 24, 1998
Engineering cyclophilin into a proline-specific endopeptidaseE Quéméneur, M Moutiez, J B Charbonnier, et al.
Protein Science : a Publication of the Protein Society|April 21, 1999
On the non-respect of the thermodynamic cycle by DsbA variantsM Moutiez, T V Burova, T Haertlé, et al.
Biochemistry|June 1, 2000
Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complexJ Couprie, F Vinci, C Dugave, et al.
Biochimica Et Biophysica Acta|October 19, 1995
Compared recognition of di- and trisulfide substrates by glutathione and trypanothione reductasesM Moutiez, M Aumercier, B Parmentier, et al.
Biochemical and Biophysical Research Communications|August 15, 1994
Reduction of a trisulfide derivative of glutathione by glutathione reductaseM Moutiez, M Aumercier, E Teissier, et al.
Protein Science : a Publication of the Protein Society|April 21, 1999
On the role of the cis-proline residue in the active site of DsbAJ B Charbonnier, P Belin, M Moutiez, et al.
The Biochemical Journal|February 15, 1997
Glutathione-dependent activities of Trypanosoma cruzi p52 makes it a new member of the thiol:disulphide oxidoreductase familyM Moutiez, E Quéméneur, C Sergheraert, et al.
Biochemistry|December 12, 2001
Slow folding of three-fingered toxins is associated with the accumulation of native disulfide-bonded intermediatesM Ruoppolo, F Talamo, P Pucci, et al.
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