Anesthetic-sensitive ion channel modulation is associated with a molar water solubility cut-off

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Anesthetic-sensitive ion channel modulation is associated with a molar water solubility cut-off

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scientific article published on 14 September 2018

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wetenschappelijk artikel

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наукова стаття, опублікована у вересні 2018

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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P1476

Anesthetic-sensitive ion chann ...... molar water solubility cut-off

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P2093

Trung L Pham

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P2860

Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures

Methyl, ethyl, propyl, butyl: futile but not for water, as the correlation of structure and thermodynamic signature shows in a congeneric series of thermolysin inhibitors

An isoflurane- and alcohol-insensitive mutant GABA(A) receptor alpha(1) subunit with near-normal apparent affinity for GABA: characterization in heterologous systems and production of knockin mice

Mutations M287L and Q266I in the glycine receptor α1 subunit change sensitivity to volatile anesthetics in oocytes and neurons, but not the minimal alveolar concentration in knockin mice

Multiple binding sites for the general anesthetic isoflurane identified in the nicotinic acetylcholine receptor transmembrane domain.

Anesthetic and convulsant properties of aromatic compounds and cycloalkanes: implications for mechanisms of narcosis.

Discrete change in volatile anesthetic sensitivity in mice with inactivated tandem pore potassium ion channel TRESK.

Hydrocarbon molar water solubility predicts NMDA vs. GABAA receptor modulation.

Anesthetic sites and allosteric mechanisms of action on Cys-loop ligand-gated ion channels.

Characterization of two mutations, M287L and Q266I, in the α1 glycine receptor subunit that modify sensitivity to alcohols.

P2888

s40360-018-0244-z

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scholarly article

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10.1186/S40360-018-0244-Z

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English

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P478

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Robert J Brosnan

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2018-09-14T00:00:00Z

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1106947613

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30217234

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6137927

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