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Michael Dennis

Researcher at Ohio State University

Publications -  12
Citations -  2477

Michael Dennis is an academic researcher from Ohio State University. The author has contributed to research in topics: Receptor & Acetylcholine receptor. The author has an hindex of 12, co-authored 12 publications receiving 2416 citations. Previous affiliations of Michael Dennis include Université de Montréal.

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Journal ArticleDOI

Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET).

TL;DR: The data demonstrate that GPCR exist as functional dimers in vivo and that BRET-based assays can be used to study both constitutive and hormone-promoted selective protein–protein interactions.
Journal Article

Inverse agonist activity of beta-adrenergic antagonists.

TL;DR: The properties revealed by the expression of the beta 2AR in Sf9 cells suggest two agonist-independent traits of G protein-linked receptors, i.e., that unliganded receptors are able to activate G proteins both in membrane preparations and in whole cells and that antagonists may mediate their effects not only by preventing the binding of agonists but also by decreasing the propensity of the receptor to assume an active state.
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Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine.

TL;DR: The membrane-bound acetylcholine receptor from Torpedo marmorata was photolabeled by the noncompetitive channel blocker [3H]chlorpromazine under equilibrium conditions in the presence of agonist.
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Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the .beta. and .delta. chains

TL;DR: Results show that homologous regions of different receptor subunits contribute to the unique high-affinity site for noncompetitive blockers, a finding consistent with the location of this site on the axis of symmetry of the receptor molecule.
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Desensitization, phosphorylation and palmitoylation of the human dopamine D1 receptor

TL;DR: The study of the baculovirus-eukaryotic cell expression system provides the first evidence that the human dopamine D1 receptor undergoes agonist-dependent desensitization, phosphorylation and palmitoylation.