The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Domain Interaction Between NMDA Receptor Subunits and the Postsynaptic Density Protein PSD-95
Abstract
The N -methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal t SXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.
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Metadata
- Authors
- Kornau, H.-C., Schenker, L. T., Kennedy, M. B., & Seeburg, P. H.
- Venue
- Science
- Published
- 1995-09-22
- Volume
- 269
- Issue
- 5231
- Pages
- 1737-1740
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093573816
- Cited by
- 1,904
- References
- 6
- FWCI
- 38.63
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
