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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Patrick Masson

Centre de Recherches du Service de Santé des Armées

Département de Toxicologie

Unité d'Enzymologie

BP 87



Name/email consistency: high



  • Centre de Recherches du Service de Santé des Armées, Département de Toxicologie, Unité d'Enzymologie, BP 87, France. 2001 - 2007


  1. Kinetic analysis of butyrylcholinesterase-catalyzed hydrolysis of acetanilides. Masson, P., Froment, M.T., Gillon, E., Nachon, F., Darvesh, S., Schopfer, L.M. Biochim. Biophys. Acta (2007) [Pubmed]
  2. Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate. Masson, P., Froment, M.T., Darvesh, S., Schopfer, L.M., Lockridge, O. J. Enzyme. Inhib. Med. Chem (2007) [Pubmed]
  3. Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate. Masson, P., Goldstein, B.N., Debouzy, J.C., Froment, M.T., Lockridge, O., Schopfer, L.M. Eur. J. Biochem. (2004) [Pubmed]
  4. Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine. Volumetric study of wild-type and D70G mutant behavior. Masson, P., Bec, N., Froment, M.T., Nachon, F., Balny, C., Lockridge, O., Schopfer, L.M. Eur. J. Biochem. (2004) [Pubmed]
  5. High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine. Masson, P., Nachon, F., Bartels, C.F., Froment, M.T., Ribes, F., Matthews, C., Lockridge, O. Eur. J. Biochem. (2003) [Pubmed]
  6. Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite. Masson, P., Schopfer, L.M., Bartels, C.F., Froment, M.T., Ribes, F., Nachon, F., Lockridge, O. Biochim. Biophys. Acta (2002) [Pubmed]
  7. Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior. Masson, P., Froment, M.T., Fort, S., Ribes, F., Bec, N., Balny, C., Schopfer, L.M. Biochim. Biophys. Acta (2002) [Pubmed]
  8. Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase. Masson, P., Xie, W., Froment, M.T., Lockridge, O. Biochim. Biophys. Acta (2001) [Pubmed]
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