Unravelling multiple ligand-activation binding sites using RASSL receptors
- 31 October 2003
- journal article
- review article
- Published by Elsevier in Trends in Pharmacological Sciences
- Vol. 24 (10) , 504-507
- https://doi.org/10.1016/j.tips.2003.08.007
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- A Single Mutation in the 5-HT4 Receptor (5-HT4-R D100(3.32)A) Generates a Gs-coupled Receptor Activated Exclusively by Synthetic Ligands (RASSL)Published by Elsevier ,2003
- Engineering receptors activated solely by synthetic ligands (RASSLs)Trends in Pharmacological Sciences, 2001
- Modification of the β2-Adrenergic Receptor to Engineer a Receptor-Effector Complex for Gene TherapyPublished by Elsevier ,2001
- Inverse, protean, and ligand‐selective agonism: matters of receptor conformationThe FASEB Journal, 2001
- Diverse signalling by 5-hydroxytryptamine (5-HT) receptorsBiochemical Pharmacology, 2000
- Heterogeneous ligand-mediated Ca++ responses at wt and mutant α2A-adrenoceptors suggest multiple ligand activation binding sites at the α2A-adrenoceptorNeuropharmacology, 2000
- Disparate ligand‐mediated Ca2+ responses by wild‐type, mutant Ser200Ala and Ser204Ala α2A‐adrenoceptor : Gα15 fusion proteins: evidence for multiple ligand‐activation binding sitesBritish Journal of Pharmacology, 2000
- Three-dimensional Models of α2A-Adrenergic Receptor Complexes Provide a Structural Explanation for Ligand BindingJournal of Biological Chemistry, 1999
- Controlling signaling with a specifically designed G i -coupled receptorProceedings of the National Academy of Sciences, 1998
- Structural basis of β‐adrenergic receptor functionThe FASEB Journal, 1989