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- W2042669315 endingPage "37" @default.
- W2042669315 startingPage "23" @default.
- W2042669315 abstract "Various combinations of subunits assemble to form the NMDA-type glutamate receptor (NMDAR), generating diversity in its functions. Here we review roles of the unique NMDAR subunit, NR3A, which acts in a dominant-negative manner to suppress receptor activity. NR3A-containing NMDARs display striking regional and temporal expression specificity, and, unlike most other NMDAR subtypes, they have a low conductance, are only modestly permeable to Ca2+, and pass current at hyperpolarized potentials in the presence of magnesium. While glutamate activates triheteromeric NMDARs composed of NR1/NR2/NR3A subunits, glycine is sufficient to activate diheteromeric NR1/NR3A-containing receptors. NR3A dysfunction may contribute to neurological disorders involving NMDARs, and the subunit offers an attractive therapeutic target given its distinct pharmacological and structural properties." @default.
- W2042669315 created "2016-06-24" @default.
- W2042669315 creator A5041197792 @default.
- W2042669315 creator A5048007911 @default.
- W2042669315 creator A5051099055 @default.
- W2042669315 creator A5060282927 @default.
- W2042669315 date "2010-05-01" @default.
- W2042669315 modified "2023-09-23" @default.
- W2042669315 title "Influence of the NR3A subunit on NMDA receptor functions" @default.
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