R
Robert J. Lefkowitz
Researcher at Howard Hughes Medical Institute
Publications - 867
Citations - 153371
Robert J. Lefkowitz is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Receptor & G protein-coupled receptor. The author has an hindex of 214, co-authored 860 publications receiving 147995 citations. Previous affiliations of Robert J. Lefkowitz include University of Nice Sophia Antipolis & University of Stuttgart.
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Journal ArticleDOI
Functional activity and regulation of human beta 2-adrenergic receptors expressed in Xenopus oocytes.
Brian K. Kobilka,C MacGregor,Kiefer W. Daniel,Tong Sun Kobilka,Marc G. Caron,Robert J. Lefkowitz +5 more
TL;DR: The recently cloned human beta-adrenergic cDNA and several mutated forms expressed in Xenopus laevis oocytes are validated and the utility of the Xenopus oocyte system for studying functional and regulatory properties of receptors coupled to adenylate cyclase is documented, and the possibility that elements in the 5' untranslated region of the beta 2- adrenergic receptor RNA may regulate its translation in vivo is suggested.
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Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism.
Stephen B. Liggett,J Ostrowski,L. C. Chesnut,Hitoshi Kurose,John R. Raymond,Marc G. Caron,Robert J. Lefkowitz +6 more
TL;DR: Long term agonist-induced desensitization of alpha 2AAR was found to be due in part to a decrease in the amount of cellular Gi, which was not dependent on receptor third loop phosphorylation sites.
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Coupling of a mutated form of the human beta 2-adrenergic receptor to Gi and Gs. Requirement for multiple cytoplasmic domains in the coupling process.
TL;DR: It is suggested that S1,2,3 interacts with Gi as well as Gs, and that receptor:G protein coupling requires the concerted participation of multiple cytoplasmic receptor domains.
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Direct Binding Studies of Adrenergic Receptors: Biochemical, Physiologic, and Clinical Implications
TL;DR: Recently developed radioligand binding techniques permit direct investigation of the alpha- and beta-adrenergic receptors for catecholamines in a wide variety of tissues, providing fresh insights into the mechanisms by which endogenous catecholsamines and other hormones regulate the properties of the adrenergic receptors and, in turn, control tissue sensitivity to catecholic action.
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Alpha-Adrenergic Receptor Identification by [3H]Dihydroergocryptine Binding
TL;DR: The data suggest that alpha-adrenergic receptors can be directly identified and studied by [3H]dihydroergocryptine binding, and that catecholamines that are devoid of alpha- adrenergic physiological activity do not compete for the binding sites.