Abstract
In this issue, Papouin et al. show that glycine is the endogenous coagonist for extrasynaptic NMDA receptors (NMDARs), unlike at synapses where the coagonist is d-serine. By enzymatically degrading endogenous glycine, they begin to address the enigmatic physiological and pathological roles for extrasynaptic NMDARs.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 455-456 |
| Number of pages | 2 |
| Journal | Cell |
| Volume | 150 |
| Issue number | 3 |
| DOIs | |
| State | Published - Aug 3 2012 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Thinking outside the synapse : Glycine at extrasynaptic NMDA receptors. / Gray, John; Nicoll, Roger A.
In: Cell, Vol. 150, No. 3, 03.08.2012, p. 455-456.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Thinking outside the synapse
T2 - Glycine at extrasynaptic NMDA receptors
AU - Gray, John
AU - Nicoll, Roger A.
PY - 2012/8/3
Y1 - 2012/8/3
N2 - In this issue, Papouin et al. show that glycine is the endogenous coagonist for extrasynaptic NMDA receptors (NMDARs), unlike at synapses where the coagonist is d-serine. By enzymatically degrading endogenous glycine, they begin to address the enigmatic physiological and pathological roles for extrasynaptic NMDARs.
AB - In this issue, Papouin et al. show that glycine is the endogenous coagonist for extrasynaptic NMDA receptors (NMDARs), unlike at synapses where the coagonist is d-serine. By enzymatically degrading endogenous glycine, they begin to address the enigmatic physiological and pathological roles for extrasynaptic NMDARs.
UR - http://www.scopus.com/inward/record.url?scp=84864619200&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84864619200&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2012.07.013
DO - 10.1016/j.cell.2012.07.013
M3 - Article
C2 - 22863001
AN - SCOPUS:84864619200
VL - 150
SP - 455
EP - 456
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -