European Journal of Pharmacology: Molecular Pharmacology
Short communicationPositive and negative allosteric interactions on muscarinic receptors
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Cited by (41)
Biased signaling as allosteric probe dependence
2021, Cellular SignallingCitation Excerpt :Specifically, depending on the identity of the allosteric modulating ligand, the effect on the ‘guest’ ligand (ligand interacting at the other protein binding site) is linked to the allosteric effect imposed on that guest ligand. For example, the allosteric ligand for the muscarinic M2 receptor alcuroniuim produces an inhibition of binding of the radioligand [[3H]-QNB but an increase in the binding of the radioligand [3H]-atropine (Hejnova et al., 1995) [11]. Therefore the effects of allosteric ligands on the secondary interactions of receptors with other bodies are dependent on the nature of the allosteric modulators producing the change.
What ligand-gated ion channels can tell us about the allosteric regulation of G protein-coupled receptors
2013, Progress in Molecular Biology and Translational ScienceCitation Excerpt :Additional allosteric ligands having unusual effects have also been described. Alcuronium, for example, was found to increase the affinity of one antagonist [3H]NMS, but decrease that of another, QNB, as well as that of agonists.111 In functional assays, however, alcuronium has been found to have a powerful inhibitory effect on the responses to agonists, and in the case of the agonist pilocarpine, this has been shown to be caused by a reduction in efficacy.112
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