The Nicotinicα5 Subunit Can Replace Either an Acetylcholine-Binding or Nonbinding Subunit in theα4β2* Neuronal Nicotinic Receptor (original) (raw)

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Journal of Biological Chemistry, 1996

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British Journal of Pharmacology, 2009

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Molecular Pharmacology, 2011

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1998

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Allosteric Potentiation from α4 C-tail A Novel α2/α4 Subtype-Selective Positive Allosteric Modulator of Nicotinic Acetylcholine Receptors Acting from the C-tail of an α Subunit

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Neuronal nicotinic receptor beta2 and beta4 subunits confer large differences in agonist binding affinity

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Heterologous Expression of Human α6β4β3α5 Nicotinic Acetylcholine Receptors: Binding Properties Consistent with Their Natural Expression Require Quaternary Subunit Assembly Including the α5 Subunit

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Structural differences determine the relative selectivity of nicotinic compounds for native α4β2*-, α6β2*-, α3β4*- and α7-nicotine acetylcholine receptors

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Neuropharmacology, 2010

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Agonist activation of 7 nicotinic acetylcholine receptors via an allosteric transmembrane site

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Critical Molecular Determinants of α7 Nicotinic Acetylcholine Receptor Allosteric Activation

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