Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.
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Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal DomainsEmerging models of glutamate receptor ion channel structure and functionCrystal structure and association behaviour of the GluR2 amino-terminal domainCrystal Structures of the Glutamate Receptor Ion Channel GluK3 and GluK5 Amino-Terminal DomainsCrystal structure of the glutamate receptor GluA1 N-terminal domainStructure and Assembly Mechanism for Heteromeric Kainate ReceptorsGlutamate receptor ion channels: structure, regulation, and functionDomain organization and function in GluK2 subtype kainate receptors.Control of assembly and function of glutamate receptors by the amino-terminal domain.The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.Transmembrane region of N-methyl-D-aspartate receptor (NMDAR) subunit is required for receptor subunit assembly.Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Functioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning.Postsynaptic glutamate receptor delta family contributes to presynaptic terminal differentiation and establishment of synaptic transmissionAssembly and forward trafficking of NMDA receptors (Review).Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors.Subunit composition of synaptic AMPA receptors revealed by a single-cell genetic approach.Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors.Glutamate receptors at atomic resolution.Roles of the N-terminal domain on the function and quaternary structure of the ionotropic glutamate receptor.Cysteine residues 87 and 320 in the amino terminal domain of NMDA receptor GluN2A govern its homodimerization but do not influence GluN2A/GluN1 heteromeric assemblyPharmacological characterisation of S 47445, a novel positive allosteric modulator of AMPA receptorsChannel opening and gating mechanism in AMPA-subtype glutamate receptors.Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptorsInter-subunit interactions between glutamate-like receptors in ArabidopsisSubunit-specific role for the amino-terminal domain of AMPA receptors in synaptic targeting.Dorsal hippocampal brain receptor complexes linked to the protein synthesis-dependent late phase (LTP) in the rat.
P2860
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P2860
Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.
description
2005 nî lūn-bûn
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2005年学术文章
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name
Two regions in the N-terminal ...... pe-specific receptor assembly.
@en
Two regions in the N-terminal ...... pe-specific receptor assembly.
@nl
type
label
Two regions in the N-terminal ...... pe-specific receptor assembly.
@en
Two regions in the N-terminal ...... pe-specific receptor assembly.
@nl
prefLabel
Two regions in the N-terminal ...... pe-specific receptor assembly.
@en
Two regions in the N-terminal ...... pe-specific receptor assembly.
@nl
P2093
P2860
P356
P1476
Two regions in the N-terminal ...... pe-specific receptor assembly.
@en
P2093
Eitan Segev
Gai Ayalon
Sharona Elgavish
Yael Stern-Bach
P2860
P304
15053-15060
P356
10.1074/JBC.M408413200
P407
P577
2005-02-08T00:00:00Z