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.
Papers
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Book ChapterDOI
Myocardial overexpression of adrenergic receptors and receptor kinases.
TL;DR: Surprisingly, cardiac β AR signaling in these animals has been maximal even in the absence of exogenous agonist, as assessed by the measurement of several biochemical and physiological parameters.
Book ChapterDOI
Adenylate-Cyclase-Coupled β- Adrenergic Receptors
TL;DR: This work has shown that prolonged exposure of target tissues to hormones results in a rapid rise followed by a decline in intracellular levels of cAMP, which appears to be quite a general mechanism for regulation of cellular sensitivity to hormonal stimulation.
Journal ArticleDOI
β-Arrestin-Biased Allosteric Modulator Potentiates Carvedilol-Stimulated β Adrenergic Receptor Cardioprotection.
Jialu Wang,Biswaranjan Pani,Ilhan Gokhan,Xinyu Xiong,Alem W. Kahsai,Haoran Jiang,Seungkirl Ahn,Robert J. Lefkowitz,Howard A. Rockman +8 more
TL;DR: In this article, a small molecule library screen against β2 adrenergic receptors (β2AR) identified Compound-6 (Cmpd-6) to be a positive allosteric modulator for β2ARs.
Journal ArticleDOI
Editorial: Smoking, catecholamines, and the heart.
TL;DR: Of the illnesses in which increased morbidity or mortality has been associated with cigarette smoking none are of greater public-health importance than coronary-artery disease.
Journal ArticleDOI
Photoaffinity labeling of β-adrenergic receptors in mammalian tissues
TL;DR: The results demonstrate the applicability of using para-azidobenzylcarazolol to covalently label mammalian β-adrenergic receptors and suggest that mammalian β 1 and β 2 receptor binding sites primarily reside on peptides of M r 62,000–65,000 and that smaller ligand binding fragments may arise by proteolysis.