Neuron
ArticlecDNA clones coding for the structural subunit of a chicken brain nicotinic acetylcholine receptor
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Production of Heteromeric Transmembrane Receptors with Defined Subunit Stoichiometry
2016, StructureCitation Excerpt :The heteromeric receptors of focus in this Preview are ligand-gated ion channels; however, it is worthwhile to note that many other membrane proteins function as heteromers including G protein-coupled receptors such as the γ-aminobutyric acid (GABA) B receptor (heterodimer of GABAB1 and GABAB2) and gamma-secretase (heterotetramer of presenilin, Pen2, nicastrin, and Aph1). The most abundant nAChR in the brain is composed of the α4 and β2 subunits Schoepfer et al. (1988) and is the target of the study by Morales-Perez et al. (2016) presented in this issue. These two subunits preferentially assemble into pentamers with two distinct stoichiometries, (α4)2(β2)3 and (α4)3(β2)2 (Carbone et al., 2009; Nelson et al., 2003), which bind to acetylcholine and nicotine with different affinities and have distinct ion selectivity and channel conductance levels (Carbone et al., 2009; Nelson et al., 2003).
Cellular events in nicotine addiction
2009, Seminars in Cell and Developmental BiologyCitation Excerpt :Receptors containing α4 and β2 subunits represent the main population of central nAChRs, and account for the majority of high affinity binding sites labeled by [3H]nicotine [44,45].
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2005, European Journal of Paediatric NeurologyNicotinic acetylcholine receptors in the nervous system
2004, Advances in Molecular and Cell BiologyCharacterization of a Rat Neuronal Nicotinic Acetylcholine Receptor α7 Promoter
2001, Journal of Biological ChemistryNew functions for nicotinic acetylcholine receptors?
1998, Behavioural Brain Research
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