Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum. - Wikidata - wikimedia - TriplyDB

Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.

Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.

http://www.wikidata.org/entity/Q39928822

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Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers Structure and Assembly Mechanism for Heteromeric Kainate Receptors Glutamate binding and conformational flexibility of ligand-binding domains are critical early determinants of efficient kainate receptor biogenesis.Glutamate receptor ion channels: structure, regulation, and function STIM2 regulates PKA-dependent phosphorylation and trafficking of AMPARs Minireview: 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 complex Contribution of the global subunit structure and stargazin on the maturation of AMPA receptors Hydrophobic side chain dynamics of a glutamate receptor ligand binding domain AMPA-receptor specific biogenesis complexes control synaptic transmission and intellectual ability.Calcium-sensing receptor biosynthesis includes a cotranslational conformational checkpoint and endoplasmic reticulum retention AMPA 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 receptors The 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 receptors Glutamate binding to the GluN2B subunit controls surface trafficking of N-methyl-D-aspartate (NMDA) receptors Activity-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) Receptors Structural 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 GluR2 Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.Activity-mediated AMPA receptor remodeling, driven by alternative splicing in the ligand-binding domain Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis.Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors A 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.

http://www.wikidata.org/entity/Q39928822

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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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

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The EMBO Journal

P1476

Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum

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Andrew C Penn

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Ingo H Greger

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P2860

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

Mechanism of glutamate receptor desensitization

Structure and mechanism of kainate receptor modulation by anions

Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating

Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand

The glutamate receptor ion channels

RNA editing at arg607 controls AMPA receptor exit from the endoplasmic reticulum

Control of kinetic properties of AMPA receptor channels by nuclear RNA editing

Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS

Quality control in the endoplasmic reticulum

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3056-3068

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scholarly article

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10.1038/EMBOJ.2008.222

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22

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27

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Stephen R Williams

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2008-10-16T00:00:00Z

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23385341

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18923416

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endoplasmic reticulum

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