Jing Zhang

TL;DR: Assessing genetic variation across GluN2 domains determined that the agonist binding domain, transmembrane domain, and the linker regions between these domains were particularly intolerant to functional variation, which allowed investigations of pharmacologic strategies to correct NMDAR function to be investigated.

TL;DR: Functional analysis of a de novo missense mutation (L812M) in a gene encoding NMDAR subunit GluN2A (GRIN2A) suggests that this mechanism underlies the patient’s epileptic phenotype as well as cerebral atrophy and drives neuronal hyperexcitability.

TL;DR: It is shown through cryoelectron microscopy that the presence of the exon 5 motif in GluN1 alters the local architecture of heterotetrameric GLUN1-GluN2 NMDA receptors and creates contacts with the ligand-binding domains (LBDs) of the Glu n1 and Glun2 subunits, which are absent in NMDA receptor receptors lacking the ex on 5 motif.

TL;DR: Application of the selective adenosine A2A receptor antagonist preladenant, which restores microglial response to cellular damage in a mouse model of Parkinson's disease, reduced the hypermotility of plaque-associated microglia, but did not restore motility toward damaged cells in slices from 5xFAD mice.