Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
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Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gatingStability of ligand-binding domain dimer assembly controls kainate receptor desensitizationSubunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromersStructure and Assembly Mechanism for Heteromeric Kainate ReceptorsGlutamate binding and conformational flexibility of ligand-binding domains are critical early determinants of efficient kainate receptor biogenesis.Glutamate receptor ion channels: structure, regulation, and functionSTIM2 regulates PKA-dependent phosphorylation and trafficking of AMPARsMinireview: the intimate link between calcium sensing receptor trafficking and signaling: implications for disorders of calcium homeostasis.Assembly and stoichiometry of the AMPA receptor and transmembrane AMPA receptor regulatory protein complexContribution of the global subunit structure and stargazin on the maturation of AMPA receptorsHydrophobic side chain dynamics of a glutamate receptor ligand binding domainAMPA-receptor specific biogenesis complexes control synaptic transmission and intellectual ability.Calcium-sensing receptor biosynthesis includes a cotranslational conformational checkpoint and endoplasmic reticulum retentionAMPA receptors commandeer an ancient cargo exporter for use as an auxiliary subunit for signaling.Control of assembly and function of glutamate receptors by the amino-terminal domain.The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.ER to synapse trafficking of NMDA receptorsThe expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits.Interaction of the M4 segment with other transmembrane segments is required for surface expression of mammalian α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors.Neuronal gamma-aminobutyric acid (GABA) type A receptors undergo cognate ligand chaperoning in the endoplasmic reticulum by endogenous GABA.Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-d-aspartate (NMDA) Receptors from the Endoplasmic Reticulum.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.Cornichons modify channel properties of recombinant and glial AMPA receptorsGlutamate binding to the GluN2B subunit controls surface trafficking of N-methyl-D-aspartate (NMDA) receptorsActivity-regulated RNA editing in select neuronal subfields in hippocampus.The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) ReceptorsStructural rearrangement of the intracellular domains during AMPA receptor activation.Agonist binding to the GluK5 subunit is sufficient for functional surface expression of heteromeric GluK2/GluK5 kainate receptors.Mechanistic Insight into NMDA Receptor Dysregulation by Rare Variants in the GluN2A and GluN2B Agonist Binding Domains.Behind the curtain: cellular mechanisms for allosteric modulation of calcium-sensing receptors.Assembly of AMPA receptors: mechanisms and regulation.Carrier subunit of plasma membrane transporter is required for oxidative folding of its helper subunit.Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites.Computational Investigation into the Interactions of Traditional Chinese Medicine Molecules of WenQingYin with GluR2Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.Activity-mediated AMPA receptor remodeling, driven by alternative splicing in the ligand-binding domainCognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis.Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptorsA nondesensitizing kainate receptor point mutant.Single amino acid residue in the M4 domain of GluN1 subunit regulates the surface delivery of NMDA receptors.
P2860
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P2860
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@en
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@nl
type
label
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@en
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@nl
prefLabel
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@en
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.
@nl
P2860
P356
P1433
P1476
Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum
@en
P2093
Andrew C Penn
Ingo H Greger
P2860
P304
P356
10.1038/EMBOJ.2008.222
P407
P577
2008-10-16T00:00:00Z