Thinking outside the synapse: Glycine at extrasynaptic NMDA receptors

John Gray; Roger A. Nicoll

doi:10.1016/j.cell.2012.07.013

Thinking outside the synapse: Glycine at extrasynaptic NMDA receptors

John Gray, Roger A. Nicoll

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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	https://doi.org/10.1016/j.cell.2012.07.013
State	Published - Aug 3 2012
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/j.cell.2012.07.013

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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.",

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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.

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Thinking outside the synapse: Glycine at extrasynaptic NMDA receptors

Abstract

ASJC Scopus subject areas

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