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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.

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Book ChapterDOI

Structure and Regulation of G Protein-Coupled Receptors: The β2-Adrenergic Receptor as a Model

TL;DR: This chapter discusses the major findings concerning the structure and coupling properties of G protein-coupled receptors and describes what is currently known about the pathways and mechanisms regulating trans-membrane signaling at the receptor level.
Journal ArticleDOI

[3H]WB4101--caution about its role as an alpha-adrenergic subtype selective radioligand.

TL;DR: It is found that both unlabeled and tritiated WB4101 bind with indistinguishable affinity to the alpha 1 and alpha 2 receptors in rabbit uterus, confirming thatWB4101 is alpha 1 selective in calf cerebral cortex.
Journal ArticleDOI

Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase. Structural alterations in the beta-adrenergic receptor revealed by photoaffinity labeling.

TL;DR: Data indicate that structural alterations in the beta-adrenergic receptor accompany the desensitization process in turkey erythrocytes, and this results in impaired ability of beta- adrenergic agonists to stimulate adenylate cycling in membranes prepared from these cells.
Journal ArticleDOI

Adenovirus-mediated gene transfer of the β2-adrenergic receptor to donor hearts enhances cardiac function

TL;DR: The results indicate that myocardial function of the transplanted heart can be enhanced by the adenovirus-mediated delivery of β2-ARs, and genetic manipulation may offer a novel therapeutic strategy to improve donor heart function in the post- operative setting.
Journal ArticleDOI

Conformationally selective RNA aptamers allosterically modulate the β2-adrenoceptor.

TL;DR: Using biochemical, pharmacological, and biophysical approaches, it is demonstrated that RNA aptamers that bind a prototypical GPCR, β2-adrenoceptor (β2AR), bind with nanomolar affinity at defined surfaces of the receptor, allosterically stabilizing active, inactive, and ligand-specific receptor conformations.