446252-22-8Relevant articles and documents
3,4-Dihydropyrimidin-2(1 H)-ones as Antagonists of the Human A2BAdenosine Receptor: Optimization, Structure-Activity Relationship Studies, and Enantiospecific Recognition
Majellaro, María,Jespers, Willem,Crespo, Abel,Nú?ez, María J.,Novio, Silvia,Azuaje, Jhonny,Prieto-Díaz, Rubén,Gioé, Claudia,Alispahic, Belma,Brea, José,Loza, María I.,Freire-Garabal, Manuel,Garcia-Santiago, Carlota,Rodríguez-García, Carlos,García-Mera, Xerardo,Caama?o, Olga,Fernandez-Masaguer, Christian,Sardina, Javier F.,Stefanachi, Angela,El Maatougui, Abdelaziz,Mallo-Abreu, Ana,?qvist, Johan,Gutiérrez-De-Terán, Hugo,Sotelo, Eddy
supporting information, p. 458 - 480 (2021/01/13)
We present and thoroughly characterize a large collection of 3,4-dihydropyrimidin-2(1H)-ones as A2BAR antagonists, an emerging strategy in cancer (immuno) therapy. Most compounds selectively bind A2BAR, with a number of potent and selective antagonists fu
Discovery of 3,4-dihydropyrimidin-2(1 H)-ones as a novel class of potent and selective A2B adenosine receptor antagonists
Crespo, Abel,El Maatougui, Abdelaziz,Biagini, Pierfrancesco,Azuaje, Jhonny,Coelho, Alberto,Brea, Jose,Loza, Maria Isabel,Cadavid, Maria Isabel,Garcia-Mera, Xerardo,Gutierrez-De-Teran, Hugo,Sotelo, Eddy
, p. 1031 - 1036 (2013/12/04)
We describe the discovery and optimization of 3,4-dihydropyrimidin-2(1H)- ones as a novel family of (nonxanthine) A2B receptor antagonists that exhibit an unusually high selectivity profile. The Biginelli-based hit optimization process enabled a thoughtful exploration of the structure-activity and structure-selectivity relationships for this chemotype, enabling the identification of ligands that combine structural simplicity with excellent hA2B AdoR affinity and remarkable selectivity profiles.
