Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Fabien Ribes"'
Autor:
Jérôme Quinonero, André Trouet, Jonathan Kearsey, Fabien Ribes, Florence Meyer-Losic, Catherine Mazerolles, Denis Ravel, Elise Assouly, Inès Hor, Céline Nicolazzi, Karine Vialatte, Philippe Rochaix, Vincent Dubois, Jean Pierre Delord
Publikováno v:
Clinical Cancer Research. 14:1258-1265
Purpose: There is a clear clinical need for cytotoxic drugs with a lower systemic toxicity. DTS-201 (CPI-0004Na) is a peptidic prodrug of doxorubicin that shows an improved therapeutic index in experimental models. The purpose of the current study wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01b9f9a6f4557a9a94fb8cb053fbd542
https://doi.org/10.1158/1078-0432.ccr-07-1165
https://doi.org/10.1158/1078-0432.ccr-07-1165
Autor:
Sébastien Fort, Nicole Bec, Patrick Masson, Marie Thérèse Froment, Claude Balny, Fabien Ribes, Lawrence M. Schopfer
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, 2002, 1597 (2), pp.229-243. ⟨10.1016/s0167-4838(02)00265-0⟩
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, 2002, 1597 (2), pp.229-243. ⟨10.1016/s0167-4838(02)00265-0⟩
Hydrolysis of the neutral substrate N-methylindoxyl acetate (NMIA) by wild-type human butyrylcholinesterase (BuChE) and peripheral site mutants (D70G, Y332A, D70G/Y332A) was found to follow the Michaelis-Menten kinetics. K(m) was 0.14 mM for wild-typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7b7a9898122fe05dad78129769c81b3
https://doi.org/10.1016/s0167-4838(02)00265-0
https://doi.org/10.1016/s0167-4838(02)00265-0
Publikováno v:
Electrophoresis. 20:1586-1594
Capillary electrophoresis (CE) was used to analyze the thermal denaturation of bovine beta-lactoglobulin at different pH. This model protein exhibits complex pH- and temperature association/dissociation dependence balances in its quaternary structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82d1b3b16e435587aec908fc19f0c083
https://doi.org/10.1002/(sici)1522-2683(19990601)20:7<1586::aid-elps1586>3.0.co
https://doi.org/10.1002/(sici)1522-2683(19990601)20:7<1586::aid-elps1586>3.0.co
Autor:
Florence Meyer-Losic, Fabien Ribes, Valérie Arranz, Jean-Sébastien Fruchart, Imane Zoubaa, Vincent Dubois, Céline Nicolazzi, Jonathan Kearsey, Denis Ravel, Matthieu Michel, Catherine de Coupade, Matthieu Boukaissi, Anne-Sophie Chéné, Jérôme Quinonero, Isabelle Tranchant
Publikováno v:
Clinical cancer research : an official journal of the American Association for Cancer Research. 14(7)
Purpose: Irinotecan is a prodrug converted to the active cytotoxic molecule SN38 predominantly by the action of liver carboxylesterases. The efficacy of irinotecan is limited by this hepatic activation that results in a low conversion rate, high inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651fa279cf60e8b026ed0e8a0234f237
https://pubmed.ncbi.nlm.nih.gov/18381956
https://pubmed.ncbi.nlm.nih.gov/18381956
Autor:
Fabien Ribes, Patrick Masson, Oksana Lockridge, Florian Nachon, Marie Thérèse Froment, Cedric Matthews, Cynthia F. Bartels
Publikováno v:
European journal of biochemistry. 270(2)
Butyrylcholinesterase is a serine esterase, closely related to acetylcholinesterase. Both enzymes employ a catalytic triad mechanism for catalysis, similar to that used by serine proteases such as alpha-chymotrypsin. Enzymes of this type are generall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92f44dc450eeccee47bd5afa7b91fa47
https://pubmed.ncbi.nlm.nih.gov/12605682
https://pubmed.ncbi.nlm.nih.gov/12605682
Autor:
Patrick Masson, Florian Nachon, Oksana Lockridge, Fabien Ribes, Lawrence M. Schopfer, Marie Thérèse Froment, Cynthia F. Bartels
Publikováno v:
Biochimica et biophysica acta. 1594(2)
Substrate inhibition is considered a defining property of acetylcholinesterase (AChE), whereas substrate activation is characteristic of butyrylcholinesterase (BuChE). To understand the mechanism of substrate inhibition, the pH dependence of acetylth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c7fbf85ab6807ee5fbfe563a52bdce8
https://pubmed.ncbi.nlm.nih.gov/11904227
https://pubmed.ncbi.nlm.nih.gov/11904227
Publikováno v:
Advances in High Pressure Bioscience and Biotechnology ISBN: 9783642643002
Inactivation of human butyrylcholinesterase (BuChE) during and after pressure and/or temperature treatment was investigated. When BuChE was subjected to the combined action of heat and pressure, an intermediate active state was irreversibly formed. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f9ea2d78d3329418ef75c8eca3be756
https://doi.org/10.1007/978-3-642-60196-5_61
https://doi.org/10.1007/978-3-642-60196-5_61
