Robert P. Compton
G. D. Searle & Company
11 Papers
309 Citations
Robert P. Compton is an academic researcher from G. D. Searle & Company. The author has contributed to research in topics: NMDA receptor & Glycine. The author has an hindex of 8, co-authored 11 publications.
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Papers
D-cycloserine: a ligand for the N-methyl-D-aspartate coupled glycine receptor has partial agonist characteristics.
TL;DR: The stimulation of [3H]TCP binding induced by D-cycloserine in the presence of various fixed concentrations of glycine results in a family of dose-response curves which asymptotically converge to 40-50% of the maximal stimulation induced by glycine alone.
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Characterization df a [3H]Glycine Recognition Site as a Modulatory Site of the N‐Methyl‐D‐Aspartate Receptor Complex
TL;DR: A [3H]glycine recognition site in rat brain synaptic plasma membranes (SPM) has been identified, having characteristics expected of a modulatory component of the N‐methyl‐D‐aspartate receptor complex.
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cis-2,4-methanoglutamate is a potent and selective N-methyl-D-aspartate receptor agonist
Thomas H. Lanthorn,William F. Hood,Gerald B. Watson,Robert P. Compton,Randall K. Rader,Yehiel Gaoni,Joseph B. Monahan +6 more
TL;DR: Cis-2,4-methanoglutamate was 100-fold more potent than L-glutamate in reducing the excitatory postsynaptic potential in CA1 of hippocampal slices and is the most potent, selective NMDA agonist known.
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N-methyl-D-aspartate recognition site ligands modulate activity at the coupled glycine recognition site.
TL;DR: In synaptic plasma membranes from rat forebrain, the potencies of glycine recognition site agonists and antagonists for modulating [3H]1‐[1‐(2‐thienyl)cyclohexyl]piperidine ([3H)TCP) binding are altered in the presence of N‐methyl‐D‐aspartate (NMDA) recognition site ligands.
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Evidence for a functional coupling of the NMDA and glycine recognition sites in synaptic plasma membranes.
TL;DR: Evidence is provided for a functional coupling between the glycine and NMDA recognition sites and further, may provide a mechanism by which compounds interacting at the glycine recognition site may modulate NMDA receptor activity.
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