Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains
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Crystal structure and association behaviour of the GluR2 amino-terminal domainCrystal structure of the glutamate receptor GluA1 N-terminal domainSubunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromersSeparation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA ReceptorsStructure and Assembly Mechanism for Heteromeric Kainate 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 functionAssembly and ligand binding properties of the water-soluble extracellular domains of the glutamate receptor 1 subunit.Cloning and characterization of glutamate receptor subunit 4 (GLUA4) and its alternatively spliced isoforms in turtle brain.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 receptorsMolecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.Control of assembly and function of glutamate receptors by the amino-terminal domain.A steroid modulatory domain on NR2B controls N-methyl-D-aspartate receptor proton sensitivityThe biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.The molecular pharmacology and cell biology of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptorsTwo-stage AMPA receptor trafficking in classical conditioning and selective role for glutamate receptor subunit 4 (tGluA4) flop splice variant.Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Glutamate receptors and endoplasmic reticulum quality control: looking beneath the surface.Intracellular machinery for the transport of AMPA receptorsFunctioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning.Activity-Regulated Cytoskeleton-Associated Protein Controls AMPAR Endocytosis through a Direct Interaction with Clathrin-Adaptor Protein 2.On the hypes and falls in neuroprotection: targeting the NMDA receptor.Postsynaptic glutamate receptor delta family contributes to presynaptic terminal differentiation and establishment of synaptic transmissionThe glutamate receptor subunit delta2 is capable of gating its intrinsic ion channel as revealed by ligand binding domain transplantationGluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors.Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2.Roles of the N-terminal domain on the function and quaternary structure of the ionotropic glutamate receptor.Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors.Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by gamma-secretase.A novel anterograde trafficking signal present in the N-terminal extracellular domain of ionotropic glutamate receptors.Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.Channel opening and gating mechanism in AMPA-subtype glutamate receptors.Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptorsMutation in hotfoot-4J mice results in retention of delta2 glutamate receptors in ER.Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2.Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.
P2860
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P2860
Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Subtype-specific assembly of a ...... ed by their n-terminal domains
@ast
Subtype-specific assembly of a ...... ed by their n-terminal domains
@en
Subtype-specific assembly of a ...... ed by their n-terminal domains
@nl
type
label
Subtype-specific assembly of a ...... ed by their n-terminal domains
@ast
Subtype-specific assembly of a ...... ed by their n-terminal domains
@en
Subtype-specific assembly of a ...... ed by their n-terminal domains
@nl
prefLabel
Subtype-specific assembly of a ...... ed by their n-terminal domains
@ast
Subtype-specific assembly of a ...... ed by their n-terminal domains
@en
Subtype-specific assembly of a ...... ed by their n-terminal domains
@nl
P3181
P356
P1476
Subtype-specific assembly of a ...... ed by their n-terminal domains
@en
P2093
P304
P3181
P356
10.1074/JBC.274.24.16907
P407
P577
1999-06-11T00:00:00Z