(Q34985096)

5 August 2017

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title

The structure of the M2 channel-lining segment from the nicotinic acetylcholine receptor (English)

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5 August 2017

M Montal

1

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5 August 2017

S J Opella

series ordinal

2

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5 August 2017

language of work or name

English

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publication date

1 October 2002

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Biochimica et Biophysica Acta

5 August 2017

published in

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5 August 2017

volume

1565

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5 August 2017

issue

2

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5 August 2017

page(s)

287-293

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Neural science: a century of progress and the mysteries that remain

5 August 2017

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Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

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

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Nicotinic acetylcholine receptor at 4.6 A resolution: transverse tunnels in the channel wall.

7 January 2021

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Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic.

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Mutational analysis of the charge selectivity filter of the alpha7 nicotinic acetylcholine receptor

7 January 2021

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Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit.

7 January 2021

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Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors

7 January 2021

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An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor

7 January 2021

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7 January 2021

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Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor

7 January 2021

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7 January 2021

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7 January 2021

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Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia

7 January 2021

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10.1016/S0005-2736(02)00575-8

7 January 2021

Identifiers

DOI

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5 August 2017

1 reference