Alternative splicing of GluN1 gates glycine site–dependent nonionotropic signaling by NMDAR receptor...
Alternative splicing of GluN1 gates glycine site–dependent nonionotropic signaling by NMDAR receptors
About this item
Full title
Author / Creator
Publisher
Washington: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
Washington: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
N-methyl-D-aspartate (NMDA) receptors (NMDARs), a principal subtype of excitatory neurotransmitter receptor, are composed as tetrameric assemblies of two glycine-binding GluN1 subunits and two glutamate-binding GluN2 subunits. NMDARs can signal nonionotropically through binding of glycine alone to its cognate site on GluN1. A consequence of this si...
Alternative Titles
Full title
Alternative splicing of GluN1 gates glycine site–dependent nonionotropic signaling by NMDAR receptors
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8271567
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8271567
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.2026411118
