Fragment evolution for GPCRs: the role of secondary binding sites in optimization
Florent Chevillard(Philipps University of Marburg), György M. Keserű(Gedeon Richter (Hungary)), Ádám A. Kelemen(HUN-REN Research Centre for Natural Sciences), Peter Kolb(Philipps University of Marburg), Jillian G. Baker(Nottingham University Hospitals NHS Trust), Frank Balzer(Philipps University of Marburg), Vivien A. Aranyodi(HUN-REN Research Centre for Natural Sciences)
Cited by 7
Related Papers
Structure of a β1-adrenergic G-protein-coupled receptor
|Nature|2008|1.3k
Expanding the medicinal chemistry synthetic toolbox
|Nature Reviews Drug Discovery|2018|693
The structural basis for agonist and partial agonist action on a β1-adrenergic receptor
|Nature|2011|623
The selectivity of β‐adrenoceptor agonists at human β<sub>1</sub>‐, β<sub>2</sub>‐ and β<sub>3</sub>‐adrenoceptors
|British Journal of Pharmacology|2010|586
The selectivity of <i>β</i>‐adrenoceptor antagonists at the human <i>β</i>1, <i>β</i>2 and <i>β</i>3 adrenoceptors
|British Journal of Pharmacology|2005|535