国际基础与临床药理学联合会。XC。多位点药理学：受体变构作用及变构配体命名法建议。
International Union of Basic and Clinical Pharmacology. XC. multisite pharmacology: recommendations for the nomenclature of receptor allosterism and allosteric ligands.
作者信息
Christopoulos Arthur, Changeux Jean-Pierre, Catterall William A, Fabbro Doriano, Burris Thomas P, Cidlowski John A, Olsen Richard W, Peters John A, Neubig Richard R, Pin Jean-Philippe, Sexton Patrick M, Kenakin Terry P, Ehlert Frederick J, Spedding Michael, Langmead Christopher J
机构信息
Drug Discovery Biology and Department of Pharmacology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia (A.C., P.M.S., C.J.L.); Collège de France and CNRS URA 2182, Institut Pasteur, Paris, France (J.-P.C.); Department of Pharmacology, School of Medicine, University of Washington, Seattle, Washington (W.A.C.); PIQUR Therapeutics AG, Basel, Switzerland (D.F.); Department of Pharmacological & Physiological Science, Saint Louis University School of Medicine, St. Louis, Louisiana (T.P.B.); Signal Transduction Laboratory, Molecular Endocrinology Group, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina (J.A.C.); Department of Molecular and Medical Pharmacology, University of California, Los Angeles, California (R.W.O.); Division of Neuroscience, School of Medicine, University of Dundee, Scotland, United Kingdom (J.A.P.); Department of Pharmacology and Toxicology, Michigan State University, East Lansing, Michigan (R.R.N.); Institut de Genomique Fonctionelle, CNRS, Montpellier, France (J.-P.P.); Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina (T.P.K.); Department of Pharmacology, University of California, Irvine, California (F.J.E.); and Research Solutions SARL, Paris, France (M.S.)
Drug Discovery Biology and Department of Pharmacology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia (A.C., P.M.S., C.J.L.); Collège de France and CNRS URA 2182, Institut Pasteur, Paris, France (J.-P.C.); Department of Pharmacology, School of Medicine, University of Washington, Seattle, Washington (W.A.C.); PIQUR Therapeutics AG, Basel, Switzerland (D.F.); Department of Pharmacological & Physiological Science, Saint Louis University School of Medicine, St. Louis, Louisiana (T.P.B.); Signal Transduction Laboratory, Molecular Endocrinology Group, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina (J.A.C.); Department of Molecular and Medical Pharmacology, University of California, Los Angeles, California (R.W.O.); Division of Neuroscience, School of Medicine, University of Dundee, Scotland, United Kingdom (J.A.P.); Department of Pharmacology and Toxicology, Michigan State University, East Lansing, Michigan (R.R.N.); Institut de Genomique Fonctionelle, CNRS, Montpellier, France (J.-P.P.); Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina (T.P.K.); Department of Pharmacology, University of California, Irvine, California (F.J.E.); and Research Solutions SARL, Paris, France (M.S.).
出版信息
Pharmacol Rev. 2014 Oct;66(4):918-47. doi: 10.1124/pr.114.008862.
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-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.
变构相互作用在代谢过程和信号转导中起着至关重要的作用，最近，由于发现更多靶点选择性化学探针和治疗药物的潜力，变构相互作用已成为众多药理学研究的焦点。除了早期对酶的经典研究外，现在还有针对基因组编码的所有受体超家族的小分子变构调节剂实例，包括配体门控和电压门控离子通道、G蛋白偶联受体、核激素受体和受体酪氨酸激酶。因此，大量的药理行为被归因于变构配体，这些行为可能因靶点、配体以及细胞/组织的不同而有所差异。本文概述了应用于受体家族的变构现象以及检测和验证变构相互作用的方法，并对变构配体的命名及其性质提出了建议。
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