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http://purl.uniprot.org/citations/28384476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28384476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28384476http://www.w3.org/2000/01/rdf-schema#comment"During development of the central nervous system, there is a shift in the subunit composition of NMDA receptors (NMDARs) resulting in a dramatic acceleration of NMDAR-mediated synaptic currents. This shift coincides with upregulation of the GluN2A subunit and triheteromeric GluN1/2A/2B receptors with fast deactivation kinetics, whereas expression of diheteromeric GluN1/2B receptors with slower deactivation kinetics is decreased. Here, we show that allosteric interactions occur between the glutamate-binding GluN2 subunits in triheteromeric GluN1/2A/2B NMDARs. This allosterism is dominated by the GluN2A subunit and results in functional properties not predicted by those of diheteromeric GluN1/2A and GluN1/2B NMDARs. These findings suggest that GluN1/2A/2B NMDARs may maintain some signaling properties of the GluN2B subunit while having the kinetic properties of GluN1/2A NMDARs and highlight the complexity in NMDAR signaling created by diversity in subunit composition."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2017.03.018"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2017.03.018"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Sun W."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Sun W."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Hansen K.B."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Hansen K.B."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Jahr C.E."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/author"Jahr C.E."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/pages"58-64"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/pages"58-64"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/title"Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/title"Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties."xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/28384476http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/28384476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28384476
http://purl.uniprot.org/citations/28384476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28384476
http://purl.uniprot.org/citations/28384476http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28384476
http://purl.uniprot.org/citations/28384476http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28384476