Probing residues in the pore-forming (M2) domain of the Cys-loop receptor homologue GLIC reveals some unusual features.

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Probing residues in the pore-forming (M2) domain of the Cys-loop receptor homologue GLIC reveals some unusual features.

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Probing residues in the pore-f ...... reveals some unusual features.

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Probing residues in the pore-f ...... reveals some unusual features.

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Probing residues in the pore-f ...... reveals some unusual features.

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P1476

Probing residues in the pore-f ...... reveals some unusual features.

@en

P2093

Mona A Alqazzaz

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Sarah C R Lummis

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P2860

Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels

Structural basis for the function and inhibition of an influenza virus proton channel

Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel

X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Ligand Activation of the Prokaryotic Pentameric Ligand-Gated Ion Channel ELIC

Structural basis for ion permeation mechanism in pentameric ligand-gated ion channels

A locally closed conformation of a bacterial pentameric proton-gated ion channel

Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

P304

26-31

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scholarly article

P356

10.3109/09687688.2015.1023377

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2015-02-01T00:00:00Z

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274901918

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25865129

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