Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism. - Wikidata - wikimedia - TriplyDB

Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism.

Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism.

http://www.wikidata.org/entity/Q44170924

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Structure, function, and modulation of GABA(A) receptors Structural studies of the actions of anesthetic drugs on the γ-aminobutyric acid type A receptor Allosteric activation mechanism of the cys-loop receptors Mapping the rho1 GABA(C) receptor agonist binding pocket. Constructing a complete model Modulation of the human ρ1 GABAA receptor by inhibitory steroids.Site-specific fluorescence reveals distinct structural changes induced in the human rho 1 GABA receptor by inhibitory neurosteroids.Structure and function of the glycine receptor and related nicotinicoid receptors.A fluorophore attached to nicotinic acetylcholine receptor beta M2 detects productive binding of agonist to the alpha delta site.Ligand- and subunit-specific conformational changes in the ligand-binding domain and the TM2-TM3 linker of {alpha}1 {beta}2 {gamma}2 GABAA receptors γ-Aminobutyric acid (GABA) signalling in plants.Pharmacology of structural changes at the GABA(A) receptor transmitter binding site.An allosteric modulator of alpha7 nicotinic receptors, N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea (PNU-120596), causes conformational changes in the extracellular ligand binding domain similar to those caused by acetylcholine.Desensitization of alpha7 nicotinic receptor is governed by coupling strength relative to gate tightness Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor The location of a closed channel gate in the GABAA receptor channel.Nitric oxide potentiation of the homomeric ρ1 GABA(C) receptor function.Modulating inhibitory ligand-gated ion channels.Competitive antagonists facilitate the recovery from desensitization of α1β2γ2 GABAA receptors expressed in Xenopus oocytes Ligand-specific conformational changes in the alpha1 glycine receptor ligand-binding domain Structural rearrangements in loop F of the GABA receptor signal ligand binding, not channel activation.Distinct structural changes in the GABAA receptor elicited by pentobarbital and GABA.Protonation controls ASIC1a activity via coordinated movements in multiple domains.Magnitude of a conformational change in the glycine receptor beta1-beta2 loop is correlated with agonist efficacy.The role of Loop F in the activation of the GABA receptor.The structural basis of function in Cys-loop receptors.Synaptic neurotransmitter-gated receptors Emerging approaches to probing ion channel structure and function.Orthosteric- versus allosteric-dependent activation of the GABAA receptor requires numerically distinct subunit level rearrangements.Mechanism of Allosteric Modulation of the Cys-loop Receptors.Mapping a molecular link between allosteric inhibition and activation of the glycine receptor.State-dependent cAMP binding to functioning HCN channels studied by patch-clamp fluorometry.Studies on the mechanisms of action of picrotoxin, quercetin and pregnanolone at the GABA rho 1 receptor.Agonist- and antagonist-induced conformational changes of loop F and their contributions to the rho1 GABA receptor function.Patch-clamp fluorometry recording of conformational rearrangements of ion channels.Mechanisms of H+ modulation of glycinergic response in rat sacral dorsal commissural neurons.Gaba receptor insecticide non-competitive antagonists may bind at allosteric modulator sites.A picrotoxin-specific conformational change in the glycine receptor M2-M3 loop.Horizontal Bilayer for Electrical and Optical Recordings.Agonist- and competitive antagonist-induced movement of loop 5 on the alpha subunit of the neuronal alpha4beta4 nicotinic acetylcholine receptor.Conformational variability of the glycine receptor M2 domain in response to activation by different agonists.

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Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism.

http://www.wikidata.org/entity/Q44170924

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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name

Site-specific fluorescence rev ...... tor activation and antagonism.

@en

Site-specific fluorescence rev ...... tor activation and antagonism.

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type

label

Site-specific fluorescence rev ...... tor activation and antagonism.

@en

Site-specific fluorescence rev ...... tor activation and antagonism.

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prefLabel

Site-specific fluorescence rev ...... tor activation and antagonism.

@en

Site-specific fluorescence rev ...... tor activation and antagonism.

@nl

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Nature Neuroscience

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Site-specific fluorescence rev ...... tor activation and antagonism.

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P2093

David S Weiss

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

Yongchang Chang

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P2860

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

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

Distinct agonist- and antagonist-binding sites on the glycine receptor

Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel.

Nicotinic receptors at the amino acid level.

Interaction of picrotoxin with GABAA receptor channel-lining residues probed in cysteine mutants.

Anxiety over GABA(A) receptor structure relieved by AChBP.

Primary structure of alpha-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence.

Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine.

Deletion of the S3-S4 linker in the Shaker potassium channel reveals two quenching groups near the outside of S4

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1163-1168

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scholarly article

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10.1038/NN926

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P433

11

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5

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2002-11-01T00:00:00Z

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12368804

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