Ontology highlight
ABSTRACT:
SUBMITTER: Irvine MW
PROVIDER: S-EPMC3269097 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Journal of medicinal chemistry 20111214 1
Competitive N-methyl-d-aspartate receptor (NMDAR) antagonists bind to the GluN2 subunit, of which there are four types (GluN2A-D). We report that some N(1)-substituted derivatives of cis-piperazine-2,3-dicarboxylic acid display improved relative affinity for GluN2C and GluN2D versus GluN2A and GluN2B. These derivatives also display subtype selectivity among the more distantly related kainate receptor family. Compounds 18i and (-)-4 were the most potent kainate receptor antagonists, and 18i was s ...[more]