Arrangement of subunits in functional NMDA receptors. - Test2 - elhamkhani - TriplyDB

Arrangement of subunits in functional NMDA receptors.

Arrangement of subunits in functional NMDA receptors.

http://www.wikidata.org/entity/Q35514700

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A structural biology perspective on NMDA receptor pharmacology and function Functional insights from glutamate receptor ion channel structures Emerging models of glutamate receptor ion channel structure and function Molecular bases of NMDA receptor subtype-dependent properties Glutamate receptor pores Crystal structure of a heterotetrameric NMDA receptor ion channel NMDA receptor structures reveal subunit arrangement and pore architecture.An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptors Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Ethanol inhibition of constitutively open N-methyl-D-aspartate receptors.Emerging structural insights into the function of ionotropic glutamate receptors.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.Interactions among positions in the third and fourth membrane-associated domains at the intersubunit interface of the N-methyl-D-aspartate receptor forming sites of alcohol action.An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Bigenomic regulation of cytochrome c oxidase in neurons and the tight coupling between neuronal activity and energy metabolism Alterations in ethanol-induced behaviors and consumption in knock-in mice expressing ethanol-resistant NMDA receptors.Functional analysis of a de novo GRIN2A missense mutation associated with early-onset epileptic encephalopathy.The multifaceted subunit interfaces of ionotropic glutamate receptors.Assembly of AMPA receptors: mechanisms and regulation.Radial symmetry in a chimeric glutamate receptor pore.Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors: Computation Meets Electrophysiology.The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.Binding of ArgTX-636 in the NMDA receptor ion channel NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers Distinct subunit contributions to the activation of M-type potassium channels by PI(4,5)P2.An evolutionary switch in ND2 enables Src kinase regulation of NMDA receptors Asynchronous movements prior to pore opening in NMDA receptors.Synaptic NMDA receptors in basolateral amygdala principal neurons are triheteromeric proteins: physiological role of GluN2B subunits.Functional Evaluation of a De Novo GRIN2A Mutation Identified in a Patient with Profound Global Developmental Delay and Refractory Epilepsy.Disruption of GRIN2B Impairs Differentiation in Human Neurons A structurally derived model of subunit-dependent NMDA receptor function

P2860

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P2860

Arrangement of subunits in functional NMDA receptors.

http://www.wikidata.org/entity/Q35514700

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

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2011年論文

@zh-tw

2011年论文

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name

Arrangement of subunits in functional NMDA receptors.

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Arrangement of subunits in functional NMDA receptors.

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Arrangement of subunits in functional NMDA receptors.

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Arrangement of subunits in functional NMDA receptors.

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Arrangement of subunits in functional NMDA receptors.

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Arrangement of subunits in functional NMDA receptors.

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JNEUROSCI.5612-10.2011

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Journal of Neuroscience

P1476

Arrangement of subunits in functional NMDA receptors.

@en

P2093

Catherine L Salussolia

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Lonnie P Wollmuth

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Michael L Prodromou

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Priya Borker

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P2860

Glutamate and neurotrophic factors in neuronal plasticity and disease

Mechanism of glutamate receptor desensitization

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

Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors

Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors

Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly.

Synaptic plasticity: multiple forms, functions, and mechanisms

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11295-11304

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scholarly article

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10.1523/JNEUROSCI.5612-10.2011

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31

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