Amino terminal domains of the NMDA receptor are organized as local heterodimers
about
Functional insights from glutamate receptor ion channel structuresEmerging models of glutamate receptor ion channel structure and functionNMDA receptor structures reveal subunit arrangement and pore architecture.An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptorsGenetically encoding a light switch in an ionotropic glutamate receptor reveals subunit-specific interfaces.Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Cysteine substitution of transmembrane domain amino acids alters the ethanol inhibition of GluN1/GluN2A N-methyl-D-aspartate receptors.Building and breaking interfaces: how a receptor takes shapeArrangement of subunits in functional NMDA receptors.Ifenprodil effects on GluN2B-containing glutamate receptors.Allosteric regulation in NMDA receptors revealed by the genetically encoded photo-cross-linkers.Structure and function of glutamate receptor amino terminal domains.Influence of GluN2 subunit identity on NMDA receptor function.The multifaceted subunit interfaces of ionotropic glutamate receptors.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.Cysteine residues 87 and 320 in the amino terminal domain of NMDA receptor GluN2A govern its homodimerization but do not influence GluN2A/GluN1 heteromeric assemblyA eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptorsVisualization of structural changes accompanying activation of N-methyl-D-aspartate (NMDA) receptors using fast-scan atomic force microscopy imaging.Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: revealing the multiple conformational states associated with a channel at its electrical off state.
P2860
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P2860
Amino terminal domains of the NMDA receptor are organized as local heterodimers
description
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique PLoS ONE
@fr
artículu científicu espublizáu en 2011
@ast
im April 2011 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2011/04/22)
@sk
vědecký článek publikovaný v roce 2011
@cs
wetenschappelijk artikel (gepubliceerd op 2011/04/22)
@nl
наукова стаття, опублікована у квітні 2011
@uk
name
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@ast
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@en
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@nl
type
label
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@ast
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@en
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@nl
prefLabel
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@ast
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@en
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@nl
P2860
P3181
P1433
P1476
Amino terminal domains of the NMDA receptor are organized as local heterodimers
@en
P2093
Chia-Hsueh Lee
Eric Gouaux
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0019180
P407
P577
2011-04-22T00:00:00Z