The fifth subunit of the (α4β2)2 β2 nicotinic ACh receptor modulates maximal ACh responses
Author:
Affiliation:
1. Department of Biological and Medical Sciences, Faculty of Health and Life Sciences; Oxford Brookes University; Oxford UK
Funder
Oxford Brookes University
Publisher
Wiley
Subject
Pharmacology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/bph.13905/fullpdf
Reference42 articles.
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3. The Concise Guide to PHARMACOLOGY 2015/16: Ligand-gated ion channels;Alexander;Br J Pharmacol,2015
4. Individual properties of the two functional agonist sites in GABAA receptors;Baumann;J Neurosci,2003
5. The additional acetylcholine binding site at the α4(+)/α4(−) interface of the (α4β2)2α4 nicotinic acetylcholine receptor contributes to desensitisation;Benallegue;Br J Pharmacol,2013
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1. Stoichiometry‐selective modulation of α4β2 nicotinic ACh receptors by divalent cations;British Journal of Pharmacology;2022-01-26
2. The Hair Cell α9α10 Nicotinic Acetylcholine Receptor: Odd Cousin in an Old Family;Frontiers in Cellular Neuroscience;2021-11-15
3. Potentiation of a neuronal nicotinic receptor via pseudo-agonist site;Cellular and Molecular Life Sciences;2019-01-01
4. Nicotinic acetylcholine receptors;British Journal of Pharmacology;2018-06
5. A tale of ligands big and small: An update on how pentameric ligand-gated ion channels interact with agonists and proteins;Current Opinion in Physiology;2018-04
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