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Cited by 573

The DOI matches its Crossref record; 342 of the 342 references it cites were found in a registry or an index.

Structure, function, and allosteric modulation of NMDA receptors

Open access
Hansen, Kasper B., Yi, Feng, Perszyk, Riley E., Furukawa, Hiro, Wollmuth, Lonnie P., Gibb, Alasdair J., Traynelis, Stephen F.·2018·Journal of General Physiology

Abstract

NMDA-type glutamate receptors are ligand-gated ion channels that mediate a Ca2+-permeable component of excitatory neurotransmission in the central nervous system (CNS). They are expressed throughout the CNS and play key physiological roles in synaptic function, such as synaptic plasticity, learning, and memory. NMDA receptors are also implicated in the pathophysiology of several CNS disorders and more recently have been identified as a locus for disease-associated genomic variation. NMDA receptors exist as a diverse array of subtypes formed by variation in assembly of seven subunits (GluN1, GluN2A-D, and GluN3A-B) into tetrameric receptor complexes. These NMDA receptor subtypes show unique structural features that account for their distinct functional and pharmacological properties allowing precise tuning of their physiological roles. Here, we review the relationship between NMDA receptor structure and function with an emphasis on emerging atomic resolution structures, which begin to explain unique features of this receptor.

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Metadata

Authors
Hansen, K. B., Yi, F., Perszyk, R. E., Furukawa, H., Wollmuth, L. P., Gibb, A. J., & Traynelis, S. F.
Venue
Journal of General Physiology
Published
2018-07-23
Volume
150
Issue
8
Pages
1081-1105
ISSN
  • 0022-1295 (ISSN-L)
  • 1540-7748
OpenAlex
W2891053092
Cited by
573
References
342
FWCI
20.18
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structure, function, and allosteric modulation of NMDA receptors. https://app.cochat.ai/papers/10.1085/jgp.201812032
The paper
Hansen, K. B., Yi, F., Perszyk, R. E., Furukawa, H., Wollmuth, L. P., Gibb, A. J., & Traynelis, S. F. (2018). Structure, function, and allosteric modulation of NMDA receptors. Journal of General Physiology. https://doi.org/10.1085/jgp.201812032

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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.