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.
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-02927-4 |
| _version_ | 1818716814011531264 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-17T19:25:14Z |
| format | Article |
| id | doaj.art-0335c41e3ce04f4db7a70da75d5832f0 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-17T19:25:14Z |
| publishDate | 2018-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-0335c41e3ce04f4db7a70da75d5832f02022-12-21T21:35:24ZengNature PortfolioNature Communications2041-17232018-03-019111510.1038/s41467-018-02927-4Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel propertiesLaura Fedele0Joseph Newcombe1Maya Topf2Alasdair Gibb3Robert J. Harvey4Trevor G. Smart5Department of Pharmacology, UCL School of Pharmacy Brunswick SquareDepartment of Biological Sciences, Birkbeck College, University of LondonDepartment of Biological Sciences, Birkbeck College, University of LondonDepartment of Neuroscience, Physiology & Pharmacology UCLSchool of Health and Sport Sciences, University of the Sunshine CoastDepartment of Neuroscience, Physiology & Pharmacology UCLN-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.https://doi.org/10.1038/s41467-018-02927-4 |
| spellingShingle | 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 Nature Communications |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41467-018-02927-4 |
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