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pro vyhledávání: '"Margaret Seidenberg"'
Autor:
Rabindra V. Shivnaraine, Brendan Kelly, Gwendolynne Elmslie, Xi-Ping Huang, Yue John Dong, Margaret Seidenberg, James W. Wells, John Ellis
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract Many G protein-coupled receptors (GPCRs) are therapeutic targets, with most drugs acting at the orthosteric site. Some GPCRs also possess allosteric sites, which have become a focus of drug discovery. In the M2 muscarinic receptor, allosteri
Externí odkaz:
https://doaj.org/article/68b8f45abdf448c890100bc734c1f038
Publikováno v:
Biochemistry. 51:4518-4540
Muscarinic cholinergic receptors contain two topographically distinct sites: an orthosteric site that binds agonists and regulates signaling, and an allosteric site that binds modulators such as gallamine and alcuronium (1). The orthosteric site is l
Publikováno v:
Molecular Pharmacology. 56:1245-1253
Gallamine allosterically modulates the binding of classical muscarinic ligands with a potency order of M(2)M(1),M(4)M(3), M(5). We have suggested previously that the M(2)/M(5) and M(2)/M(3) selectivities are attributable to an epitope in the sixth tr
Autor:
Margaret Seidenberg, John Ellis
Publikováno v:
Molecular pharmacology. 58(6)
A series of ligands that allosterically modulate the binding of classical ligands to muscarinic receptors was evaluated at wild-type and chimeric receptors. All of the ligands studied had highest affinity toward the M(2) subtype and lowest affinity t
Autor:
Margaret Seidenberg, John Ellis
Publikováno v:
Pharmacology. 61(2)
The structural basis for the selectivity of the antagonist UH-AH 37 at human muscarinic acetylcholine receptors was investigated by expressing mutant receptors in COS-7 cells. Previous studies have demonstrated that the interaction between UH-AH 37 a
Autor:
Margaret Seidenberg, John Ellis
Publikováno v:
European Journal of Pharmacology. 144:39-44
The quaternary antagonist gallamine discriminates subpopulations of muscarinic receptors in the forebrain and brainstem of the rat and also modulates the binding of other muscarinic ligands via an allosteric mechanism in both brain regions. The calci