Stargazin promotes closure of the AMPA receptor ligand-binding domain - Wikidata - wikimedia - TriplyDB

Stargazin promotes closure of the AMPA receptor ligand-binding domain

Stargazin promotes closure of the AMPA receptor ligand-binding domain

http://www.wikidata.org/entity/Q34566665

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Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy The Emerging Roles of the Calcineurin-Nuclear Factor of Activated T-Lymphocytes Pathway in Nervous System Functions and Diseases Role of the Ion Channel Extracellular Collar in AMPA Receptor Gating A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes.Stargazin Modulation of AMPA Receptors.Molecular lock regulates binding of glycine to a primitive NMDA receptor.Characterization of the Tetraspan Junctional Complex (4JC) superfamily.Identification of critical functional determinants of kainate receptor modulation by auxiliary protein Neto2.Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation.Channel opening and gating mechanism in AMPA-subtype glutamate receptors.Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes.The DLGAP family: neuronal expression, function and role in brain disorders.Accessories assist AMPA receptors to close pockets.The structure-energy landscape of NMDA receptor gating.Of tracking channel activity, modulating AMPA receptor function, permeating potassium ions, and the plant response to osmotic stress.Train stimulation of parallel fibre to Purkinje cell inputs reveals two populations of synaptic responses with different receptor signatures.Engineering defined membrane-embedded elements of AMPA receptor induces opposing gating modulation by cornichon 3 and stargazin.Acid-sensing ion channels are tuned to follow high-frequency stimuli.

P2860

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P2860

Stargazin promotes closure of the AMPA receptor ligand-binding domain

http://www.wikidata.org/entity/Q34566665

description

2014 nî lūn-bûn

@nan

2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@ast

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@en

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@nl

type

label

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@ast

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@en

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@nl

prefLabel

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@ast

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@en

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@nl

P1433

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P1433

The Journal of General Physiology

P1476

Stargazin promotes closure of the AMPA receptor ligand-binding domain

@en

P2093

James R Howe

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

Mei Du

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

Swarna S Ramaswamy

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

Vasanthi Jayaraman

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

P2860

Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number.

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

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

TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists

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

A Conformational Intermediate in Glutamate Receptor Activation

Conformational Analysis of NMDA Receptor GluN1, GluN2, and GluN3 Ligand-Binding Domains Reveals Subtype-Specific Characteristics

Electrophysiological properties of AMPA receptors are differentially modulated depending on the associated member of the TARP family.

Control of kinetic properties of AMPA receptor channels by nuclear RNA editing

P304

503-512

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scholarly article

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10.1085/JGP.201411287

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6

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144

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David M Maclean

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2014-12-01T00:00:00Z

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268874810

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25422502

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P932

4242809

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