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
Receptor and G betagamma isoform-specific interactions with G protein-coupled receptor kinases.
Yehia Daaka,Julie A. Pitcher,Mark Richardson,Robert H. Stoffel,Janet D. Robishaw,Robert J. Lefkowitz +5 more
TL;DR: This study provides a direct demonstration of a role for G betagamma in mediating the agonist-stimulated translocation of GRK2 and GRK3 in an intact cellular system and demonstrates isoform specificity in the interaction of these components.
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Arrestin Development: Emerging Roles for β-arrestins in Developmental Signaling Pathways
TL;DR: The involvement of arrestins in many discrete developmental signaling events suggests an indispensable role for these multifaceted molecular scaffolds.
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Restoration of beta-adrenergic signaling in failing cardiac ventricular myocytes via adenoviral-mediated gene transfer.
Shahab A. Akhter,Christine A. Skaer,Alan P. Kypson,Patricia McDonald,Karsten Peppel,Donald D. Glower,Robert J. Lefkowitz,Walter J. Koch +7 more
TL;DR: It is demonstrated that defects present in this critical myocardial signaling pathway can be corrected in vitro using genetic modification and raise the possibility of novel inotropic therapies for CHF including the inhibition of betaARK1 activity in the heart.
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Gβγ Subunits Mediate Mitogen-activated Protein Kinase Activation by the Tyrosine Kinase Insulin-like Growth Factor 1 Receptor
Louis M. Luttrell,Tim van Biesen,Brian E. Hawes,Walter J. Koch,Kazushige Touhara,Robert J. Lefkowitz +5 more
TL;DR: In Rat 1 fibroblasts, stimulation of mitogen-activated protein (MAP) kinase via the IGF1 receptor and the Gi-coupled receptor for lysophosphatidic acid (LPA), but not via the EGF receptor, is sensitive both to pertussis toxin treatment and to cellular expression of a specific Gβγ subunit-binding peptide.
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The multiple membrane spanning topography of the beta 2-adrenergic receptor. Localization of the sites of binding, glycosylation, and regulatory phosphorylation by limited proteolysis.
TL;DR: A structural model of beta-AR is proposed which is similar to that elucidated for rhodopsin, and the various features delineated, including the length of the carboxypeptidase Y-sensitive region, the extracellular location of the trypsin-sensitive site, the locations of phosphorylation and glycosylation all constrain the receptor to a rhodopin-like structure with multiple membrane spanning segments.