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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Catecholamine-induced subsensitivity of adenylate cyclase associated with loss of beta-adrenergic receptor binding sites
TL;DR: Data suggest that beta-adrenergic catecholamines are able to regulate catechlamine sensitivity of tissues in vivo, by regulating the properties of the beta- adrenergic receptor binding sites.
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Identification of beta-adrenergic receptors in human lymphocytes by (-) (3H) alprenolol binding.
TL;DR: The results demonstrate the feasibility of using direct binding methods to study beta-adrenergic receptors in a human tissue and provide an experimental approach to the study of states of altered sensitivity to catecholamines at the receptor level in man.
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Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid.
TL;DR: It is reported that the binding of G and lipid to the PH domain of the β-adrenergic receptor kinase (βARK) synergistically enhances agonist-dependent receptor phosphorylation and that both PH domain-binding ligands are required for membrane association of the kinase.
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Dopaminergic receptors in the anterior pituitary gland. Correlation of [3H]dihydroergocryptine binding with the dopaminergic control of prolactin release.
Marc G. Caron,M. Beaulieu,Vincent Raymond,B Gagné,Jacques Drouin,Robert J. Lefkowitz,Fernand Labrie +6 more
TL;DR: The ergot alkaloid, a potent dopaminergic agonist, has been used to study binding sites in bovine anterior pituitary membranes and fulfilled another criterion of specific receptor sites in that binding to the anterior pituitsary sites was saturable with an apparent dissociation constant.
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A highly conserved tyrosine residue in G protein-coupled receptors is required for agonist-mediated beta 2-adrenergic receptor sequestration.
Larry S. Barak,Mario Tiberi,Neil J. Freedman,Madan M. Kwatra,Robert J. Lefkowitz,Marc G. Caron +5 more
TL;DR: The lack of resensitization in the sequestration-defective beta 2-adrenergic receptor mutant strongly suggests that the sequestrations pathway is an important mechanism by which cells re-establish the normal responsiveness of G protein-coupled receptors following the removal of agonist.