Ionotropic glutamate-like receptor δ2 binds d-serine and glycine
By P. Naur, K. Hansen, A. Kristensen, S. Dravid, D. Pickering, L. Olsen, B. Vestergaard, J. Egebjerg, M. Gajhede, S. Traynelis and 1 more. Proceedings of the National Academy of Sciences of the United States of America, 2007
131 citations recorded by the source corpus.
Subfields: Biochemistry, Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b7aad082cefad37814cebca0d85d1ea7f3c8aaf3
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In Cellular and Molecular Neuroscience
- Richard Benton
- Carolina Gomez-Diaz
- Kirsten S. Vannice
- Leslie B. Vosshall
- Bill S. Hansson
- M. Stensmyr
In Molecular Biology
Citations in the corpus
- Variant ionotropic glutamate receptors as chemosensory receptors in Drosophila. (2009, background): “Interestingly, the iGluRs that lack this T residue (NR1, NR3A, delta) have glycine or serine and not glutamate as a preferred ligand (Mayer et al., 2006; Naur et al., 2007).”
- Glutamate Receptor Ion Channels: Structure, Regulation, and Function (2010, background): “…10 (55) 10 (52) 10 (55) 0.0 (0.2) 2 (19) GLUTAMATE RECEPTOR ION CHANNELS 409 nate, and NMDA receptor subunits, both in native cells and in heterologous expression systems (Partin et al., 1993, 1995; Mayat et al., 1995; Zuo et al., 1997; Kohda et al., 2000; Ikeno et al., 2001; Naur et al., 2007).”