Regulation of AMPA receptor gating by ligand binding core dimers (Q44758001)

6 December 2017

title

Regulation of AMPA receptor gating by ligand binding core dimers (English)

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6 December 2017

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Michelle S Horning

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6 December 2017

Mark L Mayer

series ordinal

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6 December 2017

language of work or name

English

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publication date

1 February 2004

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6 December 2017

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6 December 2017

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6 December 2017

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6 December 2017

page(s)

379-388

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Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis.

6 December 2017

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

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

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

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Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

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Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization.

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

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Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX

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Crystal structure and mechanism of a calcium-gated potassium channel

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Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: studies of 5-substituted willardiines and GluR2 S1S2 in the crystal

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Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate

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Structural basis for partial agonist action at ionotropic glutamate receptors

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Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD.

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

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Structure and gating mechanism of the acetylcholine receptor pore

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AMPA receptor flip/flop mutants affecting deactivation, desensitization, and modulation by cyclothiazide, aniracetam, and thiocyanate.

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Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins

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Mechanism of glutamate receptor desensitization

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Structural basis for modulation and agonist specificity of HCN pacemaker channels

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7 January 2021

10.1016/S0896-6273(04)00018-2

Identifiers

DOI

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6 December 2017

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