@article{582f0cf3c1d544c695d8ffd83d68a3e4,
title = "Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites",
abstract = "A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398\% and 308\% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.",
keywords = "Ionotropic glutamate receptor, NMDA, d -cycloserine, d -serine, subtype selectivity, superagonist",
author = "Maolanon, \{Alex R.\} and Rune Risgaard and Wang, \{Shuang Yan\} and Yoran Snoep and Athanasios Papangelis and Feng Yi and David Holley and Barslund, \{Anne F.\} and Niels Svenstrup and Hansen, \{Kasper B.\} and Clausen, \{Rasmus P.\}",
note = "Publisher Copyright: {\textcopyright} 2017 American Chemical Society.",
year = "2017",
month = aug,
day = "16",
doi = "10.1021/acschemneuro.7b00117",
language = "English",
volume = "8",
pages = "1681--1687",
journal = "ACS Chemical Neuroscience",
issn = "1948-7193",
publisher = "American Chemical Society",
number = "8",
}