Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Arnault Massink"'
Publikováno v:
Medicinal Research Reviews
Medicinal Research Reviews, 40(2), 683-708
Medicinal Research Reviews, 40(2), 683-708
The function of G protein-coupled receptors (GPCRs) can be modulated by compounds that bind to other sites than the endogenous orthosteric binding site, so-called allosteric sites. Structure elucidation of a number of GPCRs has revealed the presence
Autor:
Adriaan P. IJzerman, Thijs Beuming, Eelke B. Lenselink, Woody Sherman, Herman W. T. van Vlijmen, Arnault Massink, Corine van Veen
Publikováno v:
Journal of Computer-Aided Molecular Design
In this work, we present a case study to explore the challenges associated with finding novel molecules for a receptor that has been studied in depth and has a wealth of chemical information available. Specifically, we apply a previously described pr
Autor:
Berend J. H. Huisman, Marie Ranson, Dong Guo, Ilze Adlere, Corine van Veen, Arnault Massink, Eelke B. Lenselink, Gabrielle S. Dijksteel, Michael J. Kelso, Hayden Matthews, Benjamin J. Buckley, Adriaan P. IJzerman, Julien Louvel
Publikováno v:
Journal of Medicinal Chemistry. 59:4769-4777
The sodium ion site is an allosteric site conserved among many G protein-coupled receptors (GPCRs). Amiloride 1 and 5-(N,N-hexamethylene)amiloride 2 (HMA) supposedly bind in this sodium ion site and can influence orthosteric ligand binding. The avail
Autor:
Olga Cruz-Lopez, Katia Varani, Fabrizio Vincenzi, Arnault Massink, Allan R. Moorman, Pier Andrea Borea, Pier Giovanni Baraldi, Carlota Lopez-Cara, Adriaan P. IJzerman, Romeo Romagnoli
Publikováno v:
European Journal of Medicinal Chemistry. 101:185-204
The 2-amino-3-(p-chlorobenzoyl)thiophene scaffold has been widely employed as a pharmacophore for the identification of small molecules acting as allosteric modulators at the adenosine A1 receptor. A new series of 2-amino-3-(p-chlorobenzoyl)-4-benzyl
Autor:
Natalia V. Ortiz Zacarías, Lizi Xia, Raymond C. Stevens, Eelke B. Lenselink, Adriaan P. IJzerman, Laura H. Heitman, Vsevolod Katritch, Hugo Gutiérrez-de-Terán, Arnault Massink
Publikováno v:
Mol Pharmacol
Recently we identified a sodium ion binding pocket in a high-resolution structure of the human adenosine A2A receptor. In the present study we explored this binding site through site-directed mutagenesis and molecular dynamics simulations. Amino acid
Autor:
Olga Cruz-Lopez, Arnault Massink, Giulia Saponaro, Allan R. Moorman, Stefania Baraldi, Pier Giovanni Baraldi, Mojgan Aghazadeh Tabrizi, Pier Andrea Borea, Adriaan P. IJzerman, Romeo Romagnoli, Katia Varani, Luisa Carlota Lopez-Cara, Delia Preti, Fabrizio Vincenzi
Publikováno v:
Journal of Medicinal Chemistry. 57:7673-7686
A Sonogashira coupling strategy was employed to synthesize a new series of allosteric modulators for the A1 adenosine receptor based on the 2-amino-3-(p-chlorobenzoyl)-4-substituted thiophene skeleton, with a two-carbon (rigid or flexible) linker bet
Autor:
Arnault Massink, Adriaan P. IJzerman, Georges Vauquelin, Laura H. Heitman, Jacobus P. D. van Veldhoven, Suzanne N Venhorst, Dong Guo
Publikováno v:
British Journal of Pharmacology. 171:5295-5312
Background and Purpose Many GPCRs can be allosterically modulated by small-molecule ligands. This modulation is best understood in terms of the kinetics of the ligand–receptor interaction. However, many current kinetic assays require at least the (
Autor:
Gerwin Spijksma, M.V. Holzheimer, Adriaan P. IJzerman, A. Holscher, Arnault Massink, Dong Guo, Julien Louvel, Thomas Hankemeier
Publikováno v:
Purinergic Signalling
Conventional methods to measure ligand-receptor binding parameters typically require radiolabeled ligands as probes. Despite the robustness of radioligand binding assays, they carry inherent disadvantages in terms of safety precautions, expensive syn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b17f420f88076874cb8f07de4ae829a
https://hdl.handle.net/1887/49008
https://hdl.handle.net/1887/49008
Autor:
Dong, Guo, Suzanne N, Venhorst, Arnault, Massink, Jacobus P D, van Veldhoven, Georges, Vauquelin, Adriaan P, IJzerman, Laura H, Heitman
Publikováno v:
British journal of pharmacology. 171(23)
Many GPCRs can be allosterically modulated by small-molecule ligands. This modulation is best understood in terms of the kinetics of the ligand-receptor interaction. However, many current kinetic assays require at least the (radio)labelling of the or
Autor:
Adriaan P. IJzerman, Laura H. Heitman, Gye Won Han, Jeremiah S. Joseph, David Rodríguez, Vsevolod Katritch, Hugo Gutiérrez-de-Terán, Arnault Massink, Ilia Katritch, Wei Liu, Lizi Xia, Vadim Cherezov, Raymond C. Stevens
Publikováno v:
Structure (London, England : 1993). 21(12)
SummaryThe function of G protein-coupled receptors (GPCRs) can be modulated by a number of endogenous allosteric molecules. In this study, we used molecular dynamics, radioligand binding, and thermostability experiments to elucidate the role of the r