@article {Christopoulos918, author = {Arthur Christopoulos and Jean-Pierre Changeux and William A. Catterall and Doriano Fabbro and Thomas P. Burris and John A. Cidlowski and Richard W. Olsen and John A. Peters and Richard R. Neubig and Jean-Philippe Pin and Patrick M. Sexton and Terry P. Kenakin and Frederick J. Ehlert and Michael Spedding and Christopher J. Langmead}, editor = {Ohlstein, Eliot H.}, title = {International Union of Basic and Clinical Pharmacology. XC. Multisite Pharmacology: Recommendations for the Nomenclature of Receptor Allosterism and Allosteric Ligands}, volume = {66}, number = {4}, pages = {918--947}, year = {2014}, doi = {10.1124/pr.114.008862}, publisher = {American Society for Pharmacology and Experimental Therapeutics}, abstract = {Allosteric interactions play vital roles in metabolic processes and signal transduction and, more recently, have become the focus of numerous pharmacological studies because of the potential for discovering more target-selective chemical probes and therapeutic agents. In addition to classic early studies on enzymes, there are now examples of small molecule allosteric modulators for all superfamilies of receptors encoded by the genome, including ligand- and voltage-gated ion channels, G protein{\textendash}coupled receptors, nuclear hormone receptors, and receptor tyrosine kinases. As a consequence, a vast array of pharmacologic behaviors has been ascribed to allosteric ligands that can vary in a target-, ligand-, and cell-/tissue-dependent manner. The current article presents an overview of allostery as applied to receptor families and approaches for detecting and validating allosteric interactions and gives recommendations for the nomenclature of allosteric ligands and their properties.}, issn = {0031-6997}, URL = {https://pharmrev.aspetjournals.org/content/66/4/918}, eprint = {https://pharmrev.aspetjournals.org/content/66/4/918.full.pdf}, journal = {Pharmacological Reviews} }