Asparagine

glutamate ionotropic receptor NMDA type subunit 1 ; Homo sapiens







11 Article(s)
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1 34321660 Structural basis of ketamine action on human NMDA receptors. 2021 Aug 1
2 26045554 Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-d-aspartate (NMDA) Receptors from the Endoplasmic Reticulum. 2015 Jul 24 3
3 20958962 Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+ block. 2010 Oct 19 1
4 18988464 [Native and chiral modified NMDA-receptor NR1-binding core ligands modeling]. 2008 Jul-Aug 1
5 11423399 High-affinity Zn block in recombinant N-methyl-D-aspartate receptors with cysteine substitutions at the Q/R/N site. 2001 Jul 1
6 9481670 Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+. 1998 Jan 1 1
7 9481671 Intracellular Mg2+ interacts with structural determinants of the narrow constriction contributed by the NR1-subunit in the NMDA receptor channel. 1998 Jan 1 4
8 9545041 Altered voltage dependence of fractional Ca2+ current in N-methyl-D-aspartate channel pore mutants with a decreased Ca2+ permeability. 1998 Apr 1
9 9584221 The selectivity filter of the N-methyl-D-aspartate receptor: a tryptophan residue controls block and permeation of Mg2+. 1998 May 1
10 8780657 Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines. 1996 Aug 1
11 1382314 Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor. 1992 Sep 4 1