Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors - sprookjes - yvandenbroek - TriplyDB

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

http://www.wikidata.org/entity/Q27651229

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A structural biology perspective on NMDA receptor pharmacology and function Ionotropic glutamate receptors and voltage-gated Ca²⁺ channels in long-term potentiation of spinal dorsal horn synapses and pain hypersensitivity NMDA receptor modulators: an updated patent review (2013-2014)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 Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists Crystal Structures of the Glutamate Receptor Ion Channel GluK3 and GluK5 Amino-Terminal Domains Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors Conformational Analysis of NMDA Receptor GluN1, GluN2, and GluN3 Ligand-Binding Domains Reveals Subtype-Specific Characteristics Crystal Structure and Pharmacological Characterization of a Novel N-Methyl-D-aspartate (NMDA) Receptor Antagonist at the GluN1 Glycine Binding Site Structural Insights into Competitive Antagonism in NMDA Receptors Crystal structure of a heterotetrameric NMDA receptor ion channel Glutamate receptor ion channels: structure, regulation, and function Influence of the NR3A subunit on NMDA receptor functions.Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes.D-serine regulates cerebellar LTD and motor coordination through the δ2 glutamate receptor.Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors.Structure-based discovery of antagonists for GluN3-containing N-methyl-D-aspartate receptors.Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation.An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Alcohol and NMDA receptor: current research and future direction.Classifying neuronal subclasses of the cerebellum through constellation pharmacology.Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.Molecular lock regulates binding of glycine to a primitive NMDA receptor.Molecular dynamics simulations of protein dynamics and their relevance to drug discovery.Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.Molecular basis of NMDA receptor functional diversity.Structure and function of glutamate receptor amino terminal domains.Synaptic neurotransmitter-gated receptors Ionotropic glutamate receptors: Which ones, when, and where in the mammalian neocortex.NMDA receptor signaling: death or survival?The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating.Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors.NMDA Receptors in the Central Nervous System.Development of PET and SPECT probes for glutamate receptors.Unmasking GluN1/GluN3A excitatory glycine NMDA receptors

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P2860

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

http://www.wikidata.org/entity/Q27651229

description

2008 nî lūn-bûn

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2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

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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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name

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

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Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

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Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

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type

label

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

@ast

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

@en

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

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prefLabel

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

@ast

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

@en

Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

@nl

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The EMBO Journal

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Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors

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Chris B Harrison

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

Mark L Mayer

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Peter L Freddolino

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Yongneng Yao

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P2860

Pharmacological characterization of glycine-activated currents in HEK 293 cells expressing N-methyl-D-aspartate NR1 and NR3 subunits

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

Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state

Mechanism of glutamate receptor desensitization

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes

Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core

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

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

Structure of a glutamate-receptor ligand-binding core in complex with kainate

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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2158-70

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scholarly article

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10.1038/EMBOJ.2008.140

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15

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27

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51410544

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18636091

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2516888

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