Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties

N-methyl-d-aspartate-receptors (NMDARs) are glutamate receptors critical for synaptic transmission, plasticity, and cognition. Here, the authors look at four neurodevelopmental disease-related mutations of NMDAR, gaining insight into binding of Mg2+ and mechanism of memantine, an NMDAR antagonist.

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Autores principales:	Laura Fedele, Joseph Newcombe, Maya Topf, Alasdair Gibb, Robert J. Harvey, Trevor G. Smart
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0335c41e3ce04f4db7a70da75d5832f0
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spelling	oai:doaj.org-article:0335c41e3ce04f4db7a70da75d5832f02021-12-02T16:50:08ZDisease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties10.1038/s41467-018-02927-42041-1723https://doaj.org/article/0335c41e3ce04f4db7a70da75d5832f02018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-02927-4https://doaj.org/toc/2041-1723N-methyl-d-aspartate-receptors (NMDARs) are glutamate receptors critical for synaptic transmission, plasticity, and cognition. Here, the authors look at four neurodevelopmental disease-related mutations of NMDAR, gaining insight into binding of Mg2+ and mechanism of memantine, an NMDAR antagonist.Laura FedeleJoseph NewcombeMaya TopfAlasdair GibbRobert J. HarveyTrevor G. SmartNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Laura Fedele Joseph Newcombe Maya Topf Alasdair Gibb Robert J. Harvey Trevor G. Smart Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
description	N-methyl-d-aspartate-receptors (NMDARs) are glutamate receptors critical for synaptic transmission, plasticity, and cognition. Here, the authors look at four neurodevelopmental disease-related mutations of NMDAR, gaining insight into binding of Mg2+ and mechanism of memantine, an NMDAR antagonist.
format	article
author	Laura Fedele Joseph Newcombe Maya Topf Alasdair Gibb Robert J. Harvey Trevor G. Smart
author_facet	Laura Fedele Joseph Newcombe Maya Topf Alasdair Gibb Robert J. Harvey Trevor G. Smart
author_sort	Laura Fedele
title	Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
title_short	Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
title_full	Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
title_fullStr	Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
title_full_unstemmed	Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties
title_sort	disease-associated missense mutations in glun2b subunit alter nmda receptor ligand binding and ion channel properties
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/0335c41e3ce04f4db7a70da75d5832f0
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Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties

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