Emerging models of glutamate receptor ion channel structure and function - Test2 - elhamkhani - TriplyDB

Emerging models of glutamate receptor ion channel structure and function

Emerging models of glutamate receptor ion channel structure and function

http://www.wikidata.org/entity/Q26995713

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Functional insights from glutamate receptor ion channel structures Glutamate receptor pores Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains A Conformational Intermediate in Glutamate Receptor Activation Conformational Analysis of NMDA Receptor GluN1, GluN2, and GluN3 Ligand-Binding Domains Reveals Subtype-Specific Characteristics Structural Insights into Competitive Antagonism in NMDA Receptors NMDA receptor structures reveal subunit arrangement and pore architecture.An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptors Genetically encoding a light switch in an ionotropic glutamate receptor reveals subunit-specific interfaces.The quantal component of synaptic transmission from sensory hair cells to the vestibular calyx.Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Structural mechanism of glutamate receptor activation and desensitization.Mechanism of NMDA Receptor Inhibition and Activation.Evolutionary and Expression Analysis Provides Evidence for the Plant Glutamate-like Receptors Family is Involved in Woody Growth-related Function.Prepuberal stimulation of 5-HT7-R by LP-211 in a rat model of hyper-activity and attention-deficit: permanent effects on attention, brain amino acids and synaptic markers in the fronto-striatal interface.Molecular Mechanism of Disease-Associated Mutations in the Pre-M1 Helix of NMDA Receptors and Potential Rescue Pharmacology.Structural rearrangement of the intracellular domains during AMPA receptor activation.Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles.Conduits of life's spark: a perspective on ion channel research since the birth of neuron.The role of ionotropic glutamate receptors in childhood neurodevelopmental disorders: autism spectrum disorders and fragile x syndrome.Modes of glutamate receptor gating.Glutamate receptor homologs in plants: functions and evolutionary origins.Unanticipated parallels in architecture and mechanism between ATP-gated P2X receptors and acid sensing ion channels.Glutamate receptor antibodies in neurological diseases: anti-AMPA-GluR3 antibodies, anti-NMDA-NR1 antibodies, anti-NMDA-NR2A/B antibodies, anti-mGluR1 antibodies or anti-mGluR5 antibodies are present in subpopulations of patients with either: epilep Discovery of functional antibodies targeting ion channels.Retour aux sources: defining the structural basis of glutamate receptor activation.Radial symmetry in a chimeric glutamate receptor pore.AMPA receptor-positive allosteric modulators for the treatment of schizophrenia: an overview of recent patent applications.Molecular Mechanisms of Reception and Perireception in Crustacean Chemoreception: A Comparative Review.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.A conserved mechanism for gating in an ionotropic glutamate receptor Visualization of structural changes accompanying activation of N-methyl-D-aspartate (NMDA) receptors using fast-scan atomic force microscopy imaging.Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: revealing the multiple conformational states associated with a channel at its electrical off state.Modulation of homomeric and heteromeric kainate receptors by the auxiliary subunit Neto1.Glutamate-Dependent Translational Control of Glutamine Synthetase in Bergmann Glia Cells.Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.Mutations of N-Methyl-D-Aspartate Receptor Subunits in Epilepsy.The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.Neurotransmitter Funneling Optimizes Glutamate Receptor Kinetics.Access to the odor world: olfactory receptors and their role for signal transduction in insects.

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Emerging models of glutamate receptor ion channel structure and function

http://www.wikidata.org/entity/Q26995713

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2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Emerging models of glutamate receptor ion channel structure and function

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Mark L. Mayer

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P2860

The glutamate story

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

Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone

Mechanism of glutamate receptor desensitization

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

Structural basis for partial agonist action at ionotropic glutamate receptors

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

Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization

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

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1370-80

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scholarly article

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3919042

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10.1016/J.STR.2011.08.009

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10

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19

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51718626

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22000510

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3197216

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