Title : Inhibition of NMDA receptor function with an anti-GluN1-S2 antibody impairs human platelet function and thrombosis.

Pub. Date : 2017 Dec

PMID : 28277064






4 Functional Relationships(s)
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1 Platelet effects of a mouse monoclonal antibody targeting the glycine-binding region of GluN1 (GluN1-S2) were tested in assays of platelet activation, aggregation and thrombus formation. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
2 Platelet effects of a mouse monoclonal antibody targeting the glycine-binding region of GluN1 (GluN1-S2) were tested in assays of platelet activation, aggregation and thrombus formation. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
3 The epitope of anti-GluN1-S2 was mapped to alpha-helix H located within the glycine-binding clamshell of GluN1, where the antibody binding was computationally predicted to impair opening of the NMDAR channel. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
4 The epitope of anti-GluN1-S2 was mapped to alpha-helix H located within the glycine-binding clamshell of GluN1, where the antibody binding was computationally predicted to impair opening of the NMDAR channel. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens