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Multiple binding sites in the nicotinic acetylcholine receptors: An opportunity for polypharmacolgy

Iturriaga-Vásquez P.; Alzate-Morales J.; Bermudez I.; Varas R.; Reyes-Parada M. (Academic Press, 2015)

α4β2 nicotinic receptors with high and low acetylcholine sensitivity: Pharmacology, stoichiometry, and sensitivity to long-term exposure to nicotine

Moroni, Mirko; Zwart, Ruud; Sher, Emanuele; Cassels Niven, Bruce; Bermudez, Isabel (2006)

α4 and β2 nicotinic acetylcholine receptor (nAChR) subunits expressed heterologously assemble into receptors with high (HS) and low (LS) sensitivity to acetylcholine (ACh); their relative proportions depend on the α4 to ...

alpha 4 beta 2 nicotinic receptors with high and low acetylcholine sensitivity: Pharmacology, stoichiometry, and sensitivity to long-term exposure to nicotine

Moroni, Mirko; Zwart, Ruud; Sher, Emanuele; Cassels Niven, Bruce; Bermúdez, Isabel (AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS, 2006-08)

Alpha 4 and beta 2 nicotinic acetylcholine receptor ( nAChR) subunits expressed heterologously assemble into receptors with high (HS) and low (LS) sensitivity to acetylcholine (ACh); their relative proportions depend on ...

Halogenated cytisine derivatives as agonists at human neuronal nicotinic acetylcholine receptor subtypes

Slater, Y.E.; Houlihan, L.M.; Maskell, P.D.; Exley, R.; Bermúdez, Isabel; Lukas, R.J.; Valdivia, A.C.; Cassels Niven, Bruce (Elsevier Science Ltd., 2002-12-19)

Cytisine (cy) is a potent and competitive partial agonist at α4 subunit-containing nicotinic acetylcholine (nACh) receptors while at homomeric α7-nACh receptors it behaves as a full agonist with a relatively lower potency. ...