Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Marie-Thérèse Froment"'
Autor:
Patrick Masson, Florian Nachon, Oksana Lockridge, Eugénie Carletti, Jacques-Philippe Colletier, Martin Weik, Lawrence M. Schopfer, Marie Thérèse Froment
Publikováno v:
Chemical Research in Toxicology. 24:797-808
Aerotoxic syndrome is assumed to be caused by exposure to tricresyl phosphate (TCP), an antiwear additive in jet engine lubricants and hydraulic fluid. CBDP (2-(ortho-cresyl)-4H-1,2,3-benzodioxaphosphoran-2-one) is the toxic metabolite of triortho-cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::456d3d36e116644585143fd2e64dd997
https://doi.org/10.1021/tx100447k
https://doi.org/10.1021/tx100447k
Autor:
Florian Nachon, Patrick Masson, Marie-Thérèse Froment, Israel Silman, Benoît Sanson, Martin Weik, Jacques-Philippe Colletier, Lilly Toker, Yaacov Ashani, Harry M. Greenblatt, Joel L. Sussman
Publikováno v:
Journal of Medicinal Chemistry. 52:7593-7603
Organophosphate compounds (OP) are potent inhibitors of acetylcholinesterases (AChEs) and can cause lethal poisoning in humans. Inhibition of AChEs by the OP soman involves phosphonylation of the catalytic serine, and subsequent dealkylation produces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dec696c55f9211c73bd57bbf0d7284b
https://doi.org/10.1021/jm900433t
https://doi.org/10.1021/jm900433t
Autor:
Frank Gabel, Patrick Masson, Giuseppe Zaccai, Bhupendra P. Doctor, Martin Weik, Ashima Saxena, Israel Silman, Marie-Thérèse Froment
Publikováno v:
Biophysical Journal. 96:1489-1494
An incoherent elastic neutron scattering study of the molecular dynamics of native human butyrylcholinesterase and its “aged” soman-inhibited conjugate revealed a significant change in molecular flexibility on an angstrom-nanosecond scale as a fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32811b1d4881ac067e2381fff3b2c3e3
https://doi.org/10.1016/j.bpj.2008.10.029
https://doi.org/10.1016/j.bpj.2008.10.029
Autor:
Patrick Masson, Marie-Thérèse Froment, Frédérique Renault, Guy Lallement, A. Alonso, Frédéric Dorandeu, Claire Delacour, R. Briot, Josiane Denis, Annie Foquin
Publikováno v:
Toxicology. 248:151-157
Organophosphorus chemical warfare agents (nerve agents) are to be feared in military operations as well as in terrorist attacks. Among them, VX (O-ethyl-S-[2-(diisopropylamino)ethyl] methylphosphonothioate) is a low volatility liquid that represents
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dab2db9caaa99ff684e2760562bd984
https://doi.org/10.1016/j.tox.2008.03.013
https://doi.org/10.1016/j.tox.2008.03.013
Autor:
Lawrence M. Schopfer, Emilie Gillon, Oksana Lockridge, Patrick Masson, Florian Nachon, Marie Thérèse Froment
Publikováno v:
FEBS Journal. 275:2617-2631
The effects of tyramine, serotonin and benzalkonium on the esterase and aryl acylamidase activities of wild-type human butyrylcholinesterase and its peripheral anionic site mutant, D70G, were investigated. The kinetic study was carried out under stea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab2fce570187ce84ef516030cbcca7a5
https://doi.org/10.1111/j.1742-4658.2008.06409.x
https://doi.org/10.1111/j.1742-4658.2008.06409.x
Autor:
Oksana Lockridge, Emilie Gillon, Jean Claude Debouzy, Lawrence M. Schopfer, Laurent Verdier, Bin Li, Bernardo Brasme, Marie Thérèse Froment, Florian Nachon, Patrick Masson
Publikováno v:
Chemical Research in Toxicology. 21:421-431
Human plasma and fatty acid free human albumin were incubated with soman at pH 8.0 and 25 degrees C. Four methods were used to monitor the reaction of albumin with soman: progressive inhibition of the aryl acylamidase activity of albumin, the release
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2586f6aa91e8695bf2983d68c0a66474
https://doi.org/10.1021/tx700339m
https://doi.org/10.1021/tx700339m
Autor:
Oksana Lockridge, Lawrence M. Schopfer, Marie Thérèse Froment, Sultan Darvesh, Patrick Masson
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry. 22:463-469
Albumin is generally regarded as an inert protein with no enzyme activity. However, albumin has esterase activity as well as aryl acylamidase activity. A new acetanilide substrate, o-nitrotrifluoroacetanilide (o-NTFNAC), which is more reactive than t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04b8f233e1fb18dc4101c0f0540715f2
https://doi.org/10.1080/14756360701383932
https://doi.org/10.1080/14756360701383932
Autor:
Thomas Poyot, Oksana Lockridge, Florian Nachon, Patrick Masson, Mélanie Loiodice, Stacy Wieseler, Lawrence M. Schopfer, Marie Thérèse Froment
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764:1470-1478
Enzymes hydrolysing highly toxic organophosphate esters (OPs) are promising alternatives to pharmacological countermeasures against OPs poisoning. Bungarus fasciatus acetylcholinesterase (BfAChE) was engineered to acquire organophosphate hydrolase (O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::795137f1ea4f8f598abf9c03866b858b
https://doi.org/10.1016/j.bbapap.2006.07.008
https://doi.org/10.1016/j.bbapap.2006.07.008
Autor:
Jean Claude Debouzy, Patrick Masson, Florian Nachon, Oksana Lockridge, Lawrence M. Schopfer, Emilie Gillon, Anna Hrabovska, Boris N. Goldstein, Marie Thérèse Froment
Publikováno v:
Chemico-Biological Interactions. :143-152
Butyrylcholinesterase (BChE) displays hysteretic behavior with certain neutral and charged substrates in the approach to steady state. Previous studies led us to interpret this phenomenon in terms of slow transitions between two enzyme conformers E a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39bd0a5e2b31721161b2565230cfe3b6
https://doi.org/10.1016/j.cbi.2005.10.019
https://doi.org/10.1016/j.cbi.2005.10.019
Autor:
Patrick Masson, Jean Claude Debouzy, Boris N. Goldstein, Lawrence M. Schopfer, Marie Thérèse Froment, Oksana Lockridge
Publikováno v:
European Journal of Biochemistry. 271:220-234
Steady-state kinetics for the hydrolysis of benzoylcholine (BzCh) and benzoylthiocholine (BzSCh) by wild-type human butyrylcholinesterase (BuChE) and by the peripheral anionic site mutant D70G were compared. kcat/Km for the hydrolysis of BzSCh was 17
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e389a35f44008f245563b6500c6be13
https://doi.org/10.1046/j.1432-1033.2003.03924.x
https://doi.org/10.1046/j.1432-1033.2003.03924.x