NMDA receptors with locked glutamate-binding clefts open with high efficacy. - Wikidata - wikimedia - TriplyDB

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

http://www.wikidata.org/entity/Q36175873

about

Functional insights from glutamate receptor ion channel structures Molecular bases of NMDA receptor subtype-dependent properties Mechanism of AMPA Receptor Activation by Partial Agonists: DISULFIDE TRAPPING OF CLOSED LOBE CONFORMATIONS GluN1-specific redox effects on the kinetic mechanism of NMDA receptor activation Role of cross-cleft contacts in NMDA receptor gating Local constraints in either the GluN1 or GluN2 subunit equally impair NMDA receptor pore opening.Glycine-dependent activation of NMDA receptors.Ethanol inhibition of constitutively open N-methyl-D-aspartate receptors.Different pools of glutamate receptors mediate sensitivity to ambient glutamate in the cochlear nucleus.Conformational transitions in the glycine-bound GluN1 NMDA receptor LBD via single-molecule FRET.Probing the activation sequence of NMDA receptors with lurcher mutations Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors.Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation.Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.Modes of glutamate receptor gating.Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors: Computation Meets Electrophysiology.NMDA receptors: linking physiological output to biophysical operation.Differential effects of TM4 tryptophan mutations on inhibition of N-methyl-d-aspartate receptors by ethanol and toluene.Structural Basis for Negative Allosteric Modulation of GluN2A-Containing NMDA Receptors.A single-channel mechanism for pharmacological potentiation of GluN1/GluN2A NMDA receptors.Probing the Structural Dynamics of the NMDA Receptor Activation by Coarse-Grained Modeling.Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties.Mechanism of partial agonism in AMPA-type glutamate receptors.NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating.Allosteric Inhibitors of NMDA Receptor Functions.Mechanism and properties of positive allosteric modulation of N-methyl-d-aspartate receptors by 6-alkyl 2-naphthoic acid derivatives.

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P2860

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

http://www.wikidata.org/entity/Q36175873

description

2010 nî lūn-bûn

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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

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2010年論文

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2010年論文

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2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@ast

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@en

type

label

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@ast

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@en

prefLabel

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@ast

NMDA receptors with locked glutamate-binding clefts open with high efficacy.

@en

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JNEUROSCI.3337-10.2010

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Journal of Neuroscience

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NMDA receptors with locked glutamate-binding clefts open with high efficacy

@en

P2093

Cassandra L Kussius

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P2860

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

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

Structural basis for partial agonist action at ionotropic glutamate receptors

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

Enhanced Efficacy without Further Cleft Closure: Reevaluating Twist as a Source of Agonist Efficacy in AMPA Receptors

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

Desensitization of NMDA receptor channels is modulated by glutamate agonists.

Reaction mechanism determines NMDA receptor response to repetitive stimulation

The structure and function of glutamate receptor ion channels

Glutamate receptor gating.

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12474-12479

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scholarly article

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10.1523/JNEUROSCI.3337-10.2010

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37

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Gabriela K Popescu

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20844142

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