Control of assembly and function of glutamate receptors by the amino-terminal domain. - Test2 - elhamkhani - TriplyDB

Control of assembly and function of glutamate receptors by the amino-terminal domain.

Control of assembly and function of glutamate receptors by the amino-terminal domain.

http://www.wikidata.org/entity/Q34310112

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Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains Novel NMDA receptor modulators: an update Glutamatergic autoencephalitides: an emerging field Functional insights from glutamate receptor ion channel structures NMDA receptor modulators: an updated patent review (2013-2014)A Metabotropic-Like Flux-Independent NMDA Receptor Regulates Ca2+ Exit from Endoplasmic Reticulum and Mitochondrial Membrane Potential in Cultured Astrocytes Crystal Structures of the Glutamate Receptor Ion Channel GluK3 and GluK5 Amino-Terminal Domains Dynamics and allosteric potential of the AMPA receptor N-terminal domain Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains Structural Determinants of Agonist Efficacy at the Glutamate Binding Site of N-Methyl-D-Aspartate Receptors Crystal structure of a heterotetrameric NMDA receptor ion channel NMDA receptor structures reveal subunit arrangement and pore architecture.Activation of NMDA receptors and the mechanism of inhibition by ifenprodil.Amino terminal domains of the NMDA receptor are organized as local heterodimers Genetically encoding a light switch in an ionotropic glutamate receptor reveals subunit-specific interfaces.AMPA receptor inhibition by synaptically released zinc Domain architecture of a calcium-permeable AMPA receptor in a ligand-free conformation.Structure and organization of heteromeric AMPA-type glutamate receptors Structural determinants and mechanism of action of a GluN2C-selective NMDA receptor positive allosteric modulator.ER to synapse trafficking of NMDA receptors Cannabinoid receptor antagonists AM251 and AM630 activate TRPA1 in sensory neurons.Mechanism for noncompetitive inhibition by novel GluN2C/D N-methyl-D-aspartate receptor subunit-selective modulators 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.Emerging structural insights into the function of ionotropic glutamate receptors.Molecular pharmacology of human NMDA receptors Drosophila Neto is essential for clustering glutamate receptors at the neuromuscular junction.Subunit-selective allosteric inhibition of glycine binding to NMDA receptors Mapping the binding of GluN2B-selective N-methyl-D-aspartate receptor negative allosteric modulators.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.Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.Chimeric Glutamate Receptor Subunits Reveal the Transmembrane Domain Is Sufficient for NMDA Receptor Pore Properties but Some Positive Allosteric Modulators Require Additional Domains.Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Molecular basis of NMDA receptor functional diversity.Regulation of long-term plasticity induction by the channel and C-terminal domains of GluN2 subunits.Structure and function of glutamate receptor amino terminal domains.The multifaceted subunit interfaces of ionotropic glutamate receptors.Molecular basis of positive allosteric modulation of GluN2B NMDA receptors by polyamines.

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P2860

Control of assembly and function of glutamate receptors by the amino-terminal domain.

http://www.wikidata.org/entity/Q34310112

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

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name

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@ast

Control of assembly and function of glutamate receptors by the amino-terminal domain.

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Control of assembly and function of glutamate receptors by the amino-terminal domain.

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type

label

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@ast

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@en

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@nl

prefLabel

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@ast

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@en

Control of assembly and function of glutamate receptors by the amino-terminal domain.

@nl

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Molecular Pharmacology

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Control of assembly and function of glutamate receptors by the amino-terminal domain

@en

P2093

Hiro Furukawa

http://www.w3.org/2001/XMLSchema#string

Stephen F Traynelis

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P2860

Predicting new molecular targets for known drugs

Functional consequences of NR2 subunit composition in single recombinant N-methyl-D-aspartate receptors

Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

Mechanism of glutamate receptor desensitization

Ionotropic glutamate-like receptor 2 binds D-serine and glycine

Crystal structure and association behaviour of the GluR2 amino-terminal domain

The N-terminal domain of GluR6-subtype glutamate receptor ion channels

Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors

Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

P304

535-549

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scholarly article

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10.1124/MOL.110.067157

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4

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78

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Kasper B. Hansen

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2010-07-21T00:00:00Z

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45365690

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20660085

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2981397

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