Discovery and SAR of a novel series of non-MPEP site mGlu5 PAMs based on an aryl glycine sulfonamide scaffold
Graphical abstract
Section snippets
Acknowledgments
This work was supported in part by grants from the NIH (NS031373, MH062646, and MH89870) and from an industry sponsored contract from Johnson & Johnson. Vanderbilt is a member of the MLPCN and houses the Vanderbilt Specialized Chemistry Center for Accelerated Probe Development (U54MH084659). The authors thank Daryl F. Venable and Kiran K. Gogi for technical assistance.
References and notes (27)
- et al.
Trends Pharm. Sci.
(2009) - et al.
Neuropharmacology
(2011) - et al.
Bioorg. Med. Chem. Lett.
(2010) - et al.
Bioorg. Med. Chem. Lett.
(2007) - et al.
Bioorg. Med. Chem. Lett.
(2008) - et al.
Bioorg. Med. Chem. Lett.
(2011) - et al.
Curr. Topics Med. Chem.
(2005) - et al.
Curr. Opin. Drug Disc. Dev.
(2005) - et al.
Nat. Rev. Drug Disc.
(2009) - et al.
Curr. Topics Med. Chem.
(2006)
Nature
(1976)
Mol. Pharmacol.
(2003)
J. Med. Chem.
(2004)
Cited by (16)
Molecular insights into allosteric modulation of Class C G protein-coupled receptors
2017, Pharmacological ResearchCitation Excerpt :The NAM, BMS compound 1, does not displace a radiolabelled analogue of the CaSR phenylalkylamine, NPS 2143 [156]. Further, CPPHA, NCFP, VU0357121 and VU0400100 do not fully displace the radiolabelled mGlu5 NAM, [3H]mPEPy [92,134,157,158]. To date, a single residue within TM1 has been shown to influence CPPHA and NCFP potentiation of mGlu5 activity (Fig. 4 [134,157]).
Development of 1H-Pyrazolo[3,4-b]pyridines as Metabotropic Glutamate Receptor 5 Positive Allosteric Modulators
2016, ACS Medicinal Chemistry Letters
Copyright © 2012 Elsevier Ltd. All rights reserved.