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
Phosphorylation of the Type 1A Angiotensin II Receptor by G Protein-coupled Receptor Kinases and Protein Kinase C
TL;DR: A role for receptor phosphorylation by one or several GRKs in the rapid agonist-induced desensitization of the type 1A angiotensin II receptor is suggested.
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Recent developments in biased agonism.
TL;DR: Significant developments in several areas of GPCR biology include increased understanding of structural and biophysical mechanisms underlying biased agonism, improvements in characterization and quantification of ligand efficacy, as well as clinical development of these novel ligands.
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β2-Adrenergic Receptor Signaling and Desensitization Elucidated by Quantitative Modeling of Real Time cAMP Dynamics
Jonathan D. Violin,Lisa M. DiPilato,Necmettin Yildirim,Timothy C. Elston,Jin Zhang,Robert J. Lefkowitz +5 more
TL;DR: It is found that the cAMP response is restricted in duration by two distinct mechanisms in HEK-293 cells: G protein-coupled receptor kinase (GRK6)-mediated receptor phosphorylation leading to β-arrestin mediated receptor inactivation and cAMP-dependent kinase-mediated induction of cAMP metabolism by phosphodiesterases.
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Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions.
Brian K. Kobilka,T Frielle,Henrik G. Dohlman,Mark A. Bolanowski,Richard A. F. Dixon,P Keller,M G Caron,Robert J. Lefkowitz +7 more
TL;DR: A detailed characterization of its complete gene in both the human and hamster which reveals several unusual and provocative features suggest that the beta 2-adrenergic receptor may have arisen as a processed gene for another related gene.
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Constitutively active mutants of the alpha 2-adrenergic receptor.
TL;DR: The findings strengthen the idea that constitutively active adrenergic receptors mimic the "active" state of a G protein-coupled receptor adopting conformations similar to those induced by agonist when it binds to wild type receptors.