NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers
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Functional insights from glutamate receptor ion channel structuresOptocontrol of glutamate receptor activity by single side-chain photoisomerization.Extracellular Ca(2+) ions reduce NMDA receptor conductance and gating.Cysteine substitution of transmembrane domain amino acids alters the ethanol inhibition of GluN1/GluN2A N-methyl-D-aspartate receptors.Glycine-dependent activation of NMDA receptors.Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-d-aspartate (NMDA) Receptors from the Endoplasmic Reticulum.Probing the activation sequence of NMDA receptors with lurcher mutationsKinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors.C-terminal domains of N-methyl-D-aspartic acid receptor modulate unitary channel conductance and gatingProbing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation.Inhibition of GluN2A-containing N-methyl-D-aspartate receptors by 2-naphthoic acidAmino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.Modes of glutamate receptor gating.Structure and gating of tetrameric glutamate receptors.Retour aux sources: defining the structural basis of glutamate receptor activation.How to build the fastest receptor on earth.Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state.NMDA receptors: linking physiological output to biophysical operation.Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.Defining the structural relationship between kainate-receptor deactivation and desensitizationA Molecular Determinant of Subtype-Specific Desensitization in Ionotropic Glutamate Receptors.Asynchronous movements prior to pore opening in NMDA receptors.Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors.
P2860
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P2860
NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
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2011年论文
@zh-cn
name
NMDA receptor activation requi ...... in ligand-binding heterodimers
@en
type
label
NMDA receptor activation requi ...... in ligand-binding heterodimers
@en
prefLabel
NMDA receptor activation requi ...... in ligand-binding heterodimers
@en
P2860
P356
P1476
NMDA receptor activation requi ...... in ligand-binding heterodimers
@en
P2093
Eileen M Kasperek
William F Borschel
P2860
P2888
P356
10.1038/NCOMMS1512
P407
P577
2011-10-11T00:00:00Z