Calcium modulation of 5-HT3 receptor binding and function. - Wikidata - wikimedia - TriplyDB

Calcium modulation of 5-HT3 receptor binding and function.

Calcium modulation of 5-HT3 receptor binding and function.

http://www.wikidata.org/entity/Q37113001

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Inhibition of the Prokaryotic Pentameric Ligand-Gated Ion Channel ELIC by Divalent Cations The structural basis of function in Cys-loop receptors.

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Calcium modulation of 5-HT3 receptor binding and function.

http://www.wikidata.org/entity/Q37113001

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 16 July 2008

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

Calcium modulation of 5-HT3 receptor binding and function.

@en

Calcium modulation of 5-HT3 receptor binding and function.

@nl

type

label

Calcium modulation of 5-HT3 receptor binding and function.

@en

Calcium modulation of 5-HT3 receptor binding and function.

@nl

prefLabel

Calcium modulation of 5-HT3 receptor binding and function.

@en

Calcium modulation of 5-HT3 receptor binding and function.

@nl

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J.NEUROPHARM.2008.07.009

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Neuropharmacology

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Calcium modulation of 5-HT3 receptor binding and function.

@en

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Andrew J Thompson

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Sarah C R Lummis

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P2860

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

Rapid and efficient site-specific mutagenesis without phenotypic selection

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

Models of the extracellular domain of the nicotinic receptors and of agonist- and Ca2+-binding sites.

Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors

A cytoplasmic region determines single-channel conductance in 5-HT3 receptors.

Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation.

Identification of calcium binding sites that regulate potentiation of a neuronal nicotinic acetylcholine receptor.

Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal alpha 7 nicotinic receptor.

Structural determinants of Ca2+ permeability and conduction in the human 5-hydroxytryptamine type 3A receptor.

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285-291

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scholarly article

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10.1016/J.NEUROPHARM.2008.07.009

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1

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56

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2008-07-16T00:00:00Z

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23145152

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18675830

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