Isoform-Specific Biased Agonism of Histamine H3 Receptor Agonists

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Isoform-specific biased agonism of histamine H3 receptor agonists

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Correction to "Isoform-Specific Biased Agonism of Histamine H3 Receptor Agonists".

The human histamine H3 receptor (hH3R) is subject to extensive gene splicing that gives rise to a large number of functional and nonfunctional isoforms. Despite the general acceptance that G protein-coupled receptors can adopt different ligand-induced conformations that give rise to biased signaling, this has not been studied for the H3R; further, it is unknown whether splice variants of the sa...

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Biased Agonism of Three Different Cannabinoid Receptor Agonists in Mouse Brain Cortex

Cannabinoid receptors are able to couple to different families of G proteins when activated by an agonist drug. It has been suggested that different intracellular responses may be activated depending on the ligand. The goal of the present study was to characterize the pattern of G protein subunit stimulation triggered by three different cannabinoid ligands, Δ9-THC, WIN55212-2, and ACEA in mouse...

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Effects of betahistine at histamine H3 receptors: mixed inverse agonism/agonism in vitro and partial inverse agonism in vivo.

We previously suggested that therapeutic effects of betahistine in vestibular disorders result from its antagonist properties at histamine H(3) receptors (H(3)Rs). However, H(3)Rs exhibit constitutive activity, and most H(3)R antagonists act as inverse agonists. Here, we have investigated the effects of betahistine at recombinant H(3)R isoforms. On inhibition of cAMP formation and [(3)H]arachid...

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Biased agonism

Seven-transmembrane receptors are commonly coupled to multiple signaling pathways in cells. The simple model describing agonists for these receptors as producing a common active state to induce uniform activation of the pathways linked to the receptor has been shown to be untenable in light of a large body of data that suggest that some agonists produce activation of some but not all available ...

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ژورنال

عنوان ژورنال: Molecular Pharmacology

سال: 2016

ISSN: 0026-895X,1521-0111

DOI: 10.1124/mol.116.106153