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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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Journal ArticleDOI

Molecular biology of adrenergic receptors.

Robert J. Lefkowitz, +8 more
- 01 Jan 1988 - 
Book ChapterDOI

Molecular mechanisms of beta-adrenergic receptor desensitization.

David R. Sibley, +3 more
- 01 Jan 1987 - 
TL;DR: Several protein kinases seem to be capable of promoting phosphorylation of the receptors including the cAMP-dependent kinase and protein kinase C, and heterologous desensitization seems to be associated with functional modifications at the level of nucleotide regulatory proteins (Ns and Ni).
Journal Article

Desensitization of beta-adrenergic stimulated adenylate cyclase in turkey erythrocytes.

Brian B. Hoffman, +2 more
- 01 Oct 1979 - 
TL;DR: The data are consistent with the hypothesis that there is a lesion distal to the beta-adrenergic receptor, possibly involving the nucleotide site or the catalytic subunit of adenylate cyclase, causing the desensitization in the isoproterenol treated cells.
Journal Article

(3H)-Propranolol binding sites in myocardial membranes: nonidentity with beta adrenergic receptors.

Dorothy E. Vatner, +1 more
- 01 May 1974 - 
TL;DR: It is concluded that the [3H]propranolol binding sites studied here are unrelated to the myocardial beta adrenergic receptors and may be involved in mediating the more general membrane or local anesthetic effects of proPRanolol.
Journal ArticleDOI

Dephosphorylation of the beta 2-adrenergic receptor and rhodopsin by latent phosphatase 2.

Shiaw-Der Yang, +5 more
- 25 Jun 1988 - 
TL;DR: Study of the ability of four highly purified well characterized protein phosphatases to dephosphorylate preparations of rhodopsin or beta 2-adrenergic receptor which had been highly phosphorylated by beta-adenergic receptor kinase suggests a potential role for the latent phosphatase 2 as a specific receptor phosphat enzyme.