Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.
about
Anti-NMDA-receptor encephalitis: case series and analysis of the effects of antibodiesGlutamatergic autoencephalitides: an emerging fieldMechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding coreSeparation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA ReceptorsFormation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly.Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domainGlutamate receptor ion channels: structure, regulation, and functionAmino terminal domains of the NMDA receptor are organized as local heterodimersA naturally occurring null variant of the NMDA type glutamate receptor NR3B subunit is a risk factor of schizophrenia.Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+ block.Stargazin is an AMPA receptor auxiliary subunitMolecular mechanisms involved in the side effects of fatty acid amide hydrolase inhibitors: a structural phenomics approach to proteome-wide cellular off-target deconvolution and disease association.Control of assembly and function of glutamate receptors by the amino-terminal domain.Subunit arrangement and function in NMDA receptors.ER to synapse trafficking of NMDA receptorsProteins interactions implicated in AMPA receptor trafficking: a clear destination and an improving route map.Transmembrane region of N-methyl-D-aspartate receptor (NMDAR) subunit is required for receptor subunit assembly.Comparison of diagnostic accuracy of microscopy and flow cytometry in evaluating N-methyl-D-aspartate receptor antibodies in serum using a live cell-based assay.Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.Key amino acid residues within the third membrane domains of NR1 and NR2 subunits contribute to the regulation of the surface delivery of N-methyl-D-aspartate receptors.Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.Glutamate receptors and endoplasmic reticulum quality control: looking beneath the surface.Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-D-aspartate receptor.Functioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning.On the hypes and falls in neuroprotection: targeting the NMDA receptor.Assembly and forward trafficking of NMDA receptors (Review).Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptorAmino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors.Oligodendrocyte N-methyl-D-aspartate receptor signaling: insights into its functions.The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors.N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor.A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit.Subunit assembly of N-methyl-d-aspartate receptors analyzed by fluorescence resonance energy transfer.Roles of the N-terminal domain on the function and quaternary structure of the ionotropic glutamate receptor.Arginine 260 of the amino-terminal domain of NR1 subunit is critical for tissue-type plasminogen activator-mediated enhancement of N-methyl-D-aspartate receptor signaling.Export from the endoplasmic reticulum of assembled N-methyl-d-aspartic acid receptors is controlled by a motif in the c terminus of the NR2 subunit.
P2860
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P2860
Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Identification of molecular de ...... -methyl-D-aspartate receptors.
@en
type
label
Identification of molecular de ...... -methyl-D-aspartate receptors.
@en
prefLabel
Identification of molecular de ...... -methyl-D-aspartate receptors.
@en
P2093
P2860
P356
P1476
Identification of molecular de ...... -methyl-D-aspartate receptors.
@en
P2093
Grimwood S
Le Bourdelles B
McIlhinney RA
P2860
P304
18795-18803
P356
10.1074/JBC.M101382200
P407
P577
2001-03-06T00:00:00Z