| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1378023 | Bioorganic & Medicinal Chemistry Letters | 2007 | 6 Pages |
Abstract
This Letter describes, for the first time, the synthesis and SAR, developed through an iterative analog library approach, that led to the discovery of the positive allosteric modulator (PAM) of the metabotropic glutamate receptor mGluR5 CPPHA. Binding to a unique allosteric binding site distinct from other mGluR5 PAMs, CPPHA has been the focus of numerous pharmacology studies by several laboratories.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Zhijian Zhao, David D. Wisnoski, Julie A. O’Brien, Wei Lemaire, David L. Williams Jr., Marlene A. Jacobson, Marion Wittman, Sookhee N. Ha, Herve Schaffhauser, Cyrille Sur, Doug J. Pettibone, Mark E. Duggan, P. Jeffrey Conn, George D. Hartman,