Pages that link to "Q71668444"
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The following pages link to Activation of N-methyl-D-aspartate receptors by glycine: role of an aspartate residue in the M3-M4 loop of the NR1 subunit (Q71668444):
Displaying 20 items.
- D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor (Q24675924) (← links)
- Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core (Q27641433) (← links)
- Glutamate receptor ion channels: structure, regulation, and function (Q28290774) (← links)
- Allosteric modulation of [3H]-CGP39653 binding through the glycine site of the NMDA receptor: further studies in rat and human brain (Q28363101) (← links)
- Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors (Q28583397) (← links)
- Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium (Q33591015) (← links)
- Structural determinants of D-cycloserine efficacy at the NR1/NR2C NMDA receptors (Q33821292) (← links)
- E-p-methoxycinnamic acid protects cultured neuronal cells against neurotoxicity induced by glutamate (Q35044198) (← links)
- Glutamate receptors and Parkinson's disease: opportunities for intervention (Q35107721) (← links)
- The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective (Q35861036) (← links)
- A de novo loss-of-function GRIN2A mutation associated with childhood focal epilepsy and acquired epileptic aphasia (Q36275333) (← links)
- Pharmacological insights obtained from structure-function studies of ionotropic glutamate receptors (Q36394958) (← links)
- Expression of glycine-activated diheteromeric NR1/NR3 receptors in human embryonic kidney 293 cells Is NR1 splice variant-dependent (Q37444406) (← links)
- Epilepsy-associated GRIN2A mutations reduce NMDA receptor trafficking and agonist potency - molecular profiling and functional rescue (Q38752558) (← links)
- AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition (Q41015790) (← links)
- Single-channel analysis of an NMDA receptor possessing a mutation in the region of the glutamate binding site (Q42632898) (← links)
- Single-channel analysis of a point mutation of a conserved serine residue in the S2 ligand-binding domain of the NR2A NMDA receptor subunit (Q42686138) (← links)
- Modulation of glycine potency in rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes (Q46930527) (← links)
- NMDA Receptors in the Central Nervous System (Q48029905) (← links)
- Structural features in the glycine-binding sites of the GluN1 and GluN3A subunits regulate the surface delivery of NMDA receptors (Q92833028) (← links)