C
Catherine Guillou
Researcher at Institut de Chimie des Substances Naturelles
Publications - 83
Citations - 1863
Catherine Guillou is an academic researcher from Institut de Chimie des Substances Naturelles. The author has contributed to research in topics: Heck reaction & Intramolecular force. The author has an hindex of 25, co-authored 81 publications receiving 1700 citations. Previous affiliations of Catherine Guillou include Centre national de la recherche scientifique.
Papers
More filters
Journal ArticleDOI
Breakthroughs in Medicinal Chemistry: New Targets and Mechanisms, New Drugs, New Hopes-6.
Arduino A. Mangoni,Catherine Guillou,Jean Jacques Vanden Eynde,Christopher Hulme,Josef Jampilek,Wei Li,Katalin Prokai-Tatrai,Jarkko Rautio,Simona Collina,Tiziano Tuccinardi,Maria Emília Sousa,Jean-Marc Sabatier,Stefania Galdiero,Rafik Karaman,Rafik Karaman,George Kokotos,Giangiacomo Torri,F. Javier Luque,M. Helena Vasconcelos,Dimitra Hadjipavlou-Litina,Carlo Siciliano,Michael Gütschow,Rino Ragno,Paula Gomes,Luigi A. Agrofoglio,Diego Muñoz-Torrero +25 more
TL;DR: Breakthroughs in Medicinal Chemistry: New Targets and Mechanisms, New Drugs, New Hopes is a series of Editorials published on a biannual basis by the Editorial Board of the Medicinal chemistry section of the journal Molecules.
Journal ArticleDOI
The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design.
Harry M. Greenblatt,Catherine Guillou,Daniel Guenard,Anat Argaman,Simone A. Botti,Bernard Badet,Claude Thal,Israel Silman,Joel L. Sussman +8 more
TL;DR: Bifunctional derivatives of the alkaloid galanthamine designed to interact with both the active site of the enzyme acetylcholinesterase and its peripheral cation binding site have been assayed with Torpedo californica AChE, and the three-dimensional structures of their complexes with the enzyme have been solved by X-ray crystallography.
Journal ArticleDOI
Potent acetylcholinesterase inhibitors: design, synthesis, and structure–Activity relationships of bis-interacting ligands in the galanthamine series
TL;DR: New galanthamine derivatives, especially bis-interacting ligands 3-5 and 7-9 were prepared in order to interact with the catalytic and the peripheral sites of acetylcholinesterase (AChE).
Journal ArticleDOI
Acetylcholine nicotinic receptors: finding the putative binding site of allosteric modulators using the “blind docking” approach
TL;DR: Three putative binding sites were identified in the channel pore and one of these sites is localized opposite to the agonist binding site and is probably implicated in the potentiation process of nicotinic acetylcholine receptor (nAChRs) activation.
Journal ArticleDOI
Potent acetylcholinesterase inhibitors: design, synthesis and structure-activity relationships of alkylene linked bis-galanthamine and galanthamine-galanthaminium salts.
TL;DR: Compounds 6b-c were found to be more potent than galanthamine and tacrine in inhibiting AChE and the syntheses, the anticholinesterase activities and structure-activity relationships are reported.