John D. McCorvy, Ph.D.

Medicinal Chemistry and Molecular Pharmacology Purdue University, West Lafayette, IN, United States 
Dopamine and Serotonin Agonists
"John McCorvy"
Mean distance: 18.16 (cluster 11)


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David E. Nichols grad student 2012 Purdue
 (Mapping the binding site of the 5-HT2A receptor using mutagenesis and ligand libraries: Insights into the molecular actions of psychedelics.)
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Zhang G, McCorvy JD, Shen S, et al. (2019) Design of fluorinated cyclopropane derivatives of 2-phenylcyclopropylmethylamine leading to identification of a selective serotonin 2C (5-HT) receptor agonist without 5-HT agonism. European Journal of Medicinal Chemistry. 182: 111626
Martini ML, Ray C, Yu X, et al. (2019) Designing Functionally Selective Non-Catechol Dopamine D1 Receptor Agonists with Potent In Vivo Antiparkinsonian Activity. Acs Chemical Neuroscience
Stauch B, Johansson LC, McCorvy JD, et al. (2019) Publisher Correction: Structural basis of ligand recognition at the human MT melatonin receptor. Nature
Stauch B, Johansson LC, McCorvy JD, et al. (2019) Structural basis of ligand recognition at the human MT melatonin receptor. Nature
Johansson LC, Stauch B, McCorvy JD, et al. (2019) XFEL structures of the human MT melatonin receptor reveal the basis of subtype selectivity. Nature
Shen Y, McCorvy JD, Martini ML, et al. (2019) D2 Dopamine Receptor G protein-biased Partial Agonists Based on Cariprazine. Journal of Medicinal Chemistry
Martini ML, Liu J, Ray C, et al. (2019) Defining Structure-Functional Selectivity Relationships (SFSR) for a Class of Non-Catechol Dopamine D1 Receptor Agonists. Journal of Medicinal Chemistry
McCorvy JD, Wacker D, Wang S, et al. (2018) Structural determinants of 5-HT receptor activation and biased agonism. Nature Structural & Molecular Biology
Qin S, Meng M, Yang D, et al. (2018) High-throughput identification of G protein-coupled receptor modulators through affinity mass spectrometry screening. Chemical Science. 9: 3192-3199
Peng Y, McCorvy JD, Harpsøe K, et al. (2018) 5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology. Cell
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