Principal pathway coupling agonist binding to channel gating in nicotinic receptors (Q46799020)

25 December 2017

title

Principal pathway coupling agonist binding to channel gating in nicotinic receptors (English)

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25 December 2017

author name string

Won Yong Lee

series ordinal

1

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25 December 2017

Steven M Sine

series ordinal

2

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25 December 2017

language of work or name

English

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publication date

1 November 2005

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25 December 2017

published in

Nature

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25 December 2017

volume

438

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25 December 2017

page(s)

243-247

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25 December 2017

issue

7065

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25 December 2017

https://scigraph.springernature.com/pub.10.1038/nature04156

exact match

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cites work

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Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence

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A gating mechanism proposed from a simulation of a human alpha7 nicotinic acetylcholine receptor

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Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits.

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Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures

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Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels

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Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities

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Mapping the conformational wave of acetylcholine receptor channel gating

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Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding

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A novel hyperekplexia-causing mutation in the pre-transmembrane segment 1 of the human glycine receptor alpha1 subunit reduces membrane expression and impairs gating by agonists.

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Multiple roles of the conserved key residue arginine 209 in neuronal nicotinic receptors.

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Charged Residues in the β2 Subunit Involved in GABAA Receptor Activation

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Arginine 222 in the pre-transmembrane domain 1 of 5-HT3A receptors links agonist binding to channel gating

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The location of the gate in the acetylcholine receptor channel.

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Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles

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The nicotinic receptor ligand binding domain

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Agonist-induced conformational changes in the extracellular domain of alpha 7 nicotinic acetylcholine receptors

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A highly conserved aspartic acid residue in the signature disulfide loop of the alpha 1 subunit is a determinant of gating in the glycine receptor

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Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.

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Gating dynamics of the acetylcholine receptor extracellular domain.

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Charged amino acids of the N-terminal domain are involved in coupling binding and gating in alpha7 nicotinic receptors

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Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome

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Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating.

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Naturally occurring mutations at the acetylcholine receptor binding site independently alter ACh binding and channel gating.

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VMD: visual molecular dynamics

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Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events

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Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE04156

1 reference

25 December 2017

Dimensions Publication ID

0 references

1 reference

25 December 2017