PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23447622-9 2013 Mutating the GluN2 S/L site of GluN2A subunits from serine (found in GluN2A and GluN2B subunits) to leucine (found in GluN2C and GluN2D) greatly diminished both voltage-dependent gating and slow Mg(o)(2+) unblock. Leucine 100-107 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 31-37 22715100-6 2012 Significant interactions affecting ethanol inhibition and receptor deactivation were observed at four pairs of positions in GluN1/GluN2A: Gly-638/Met-823, Phe-639/Leu-824, Met-818/Phe-636, and Leu-819/Phe-637; the latter pair also interacted with respect to desensitization. Leucine 163-166 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 130-136 22715100-6 2012 Significant interactions affecting ethanol inhibition and receptor deactivation were observed at four pairs of positions in GluN1/GluN2A: Gly-638/Met-823, Phe-639/Leu-824, Met-818/Phe-636, and Leu-819/Phe-637; the latter pair also interacted with respect to desensitization. Leucine 193-196 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 130-136 22715100-7 2012 Two interactions involved a position in M4 of both subunits, GluN1(Met-818) and GluN2A(Leu-824), that does not by itself alter ethanol sensitivity, whereas a previously identified ethanol-sensitive position, GluN2A(Ala-825), did not unequivocally interact with any other position tested. Leucine 87-90 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 80-86 11053122-4 2000 The tryptophan was mutated to a leucine (W-5L) in both the NMDAR1 and NMDAR2A subunits. Leucine 32-39 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 70-77 34321660-7 2021 Two amino acids-leucine 642 on GluN2A (homologous to leucine 643 on GluN2B) and asparagine 616 on GluN1-were identified as key residues that form hydrophobic and hydrogen-bond interactions with ketamine, and mutations at these residues reduced the potency of ketamine in blocking NMDA receptor channel activity. Leucine 16-23 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 31-37 34321660-7 2021 Two amino acids-leucine 642 on GluN2A (homologous to leucine 643 on GluN2B) and asparagine 616 on GluN1-were identified as key residues that form hydrophobic and hydrogen-bond interactions with ketamine, and mutations at these residues reduced the potency of ketamine in blocking NMDA receptor channel activity. Leucine 53-60 glutamate ionotropic receptor NMDA type subunit 2A Homo sapiens 31-37