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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Gβγ interactions with PH domains and Ras-MAPK signaling pathways
TL;DR: The βγ-subunit complex of G proteins mediates many of the functions associated with G-protein-coupled receptor signaling and may even provide a means to link G proteins to RTK-initiated cascades.
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β-Arrestin-dependent Constitutive Internalization of the Human Chemokine Decoy Receptor D6
Emanuela Galliera,Venkatakrishna R. Jala,John O. Trent,Raffaaella Bonecchi,Paola Signorelli,Robert J. Lefkowitz,Alberto Mantovani,Massimo Locati,Bodduluri Haribabu +8 more
TL;DR: D6 may be considered a decoy receptor structurally adapted to perform chemokine scavenging, and this scavenging activity is mediated by continuous internalization and constant surface expression of the receptor, a process involving the clathrin-coated pit-dependent pathway.
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β1-Adrenergic Receptor Association with PSD-95 INHIBITION OF RECEPTOR INTERNALIZATION AND FACILITATION OF β1-ADRENERGIC RECEPTOR INTERACTION WITHN-METHYL-d-ASPARTATE RECEPTORS
Liaoyuan A. Hu,Yuting Tang,William E. Miller,Mei Cong,Anthony G. Lau,Robert J. Lefkowitz,Randy A. Hall +6 more
TL;DR: Data reveal that PSD-95 is a specificβ1AR binding partner that modulates β1AR function and facilitates physical association of the β1 AR with synaptic proteins, such as theN-methyl-d-aspartate receptors, which are known to be regulated by β1ar stimulation.
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Receptor-specific Ubiquitination of β-Arrestin Directs Assembly and Targeting of Seven-transmembrane Receptor Signalosomes
TL;DR: Shenoy et al. as discussed by the authors showed that lysines at positions 11 and 12 in β-arrestin2 are specific and required sites for its AngII-mediated sustained ubiquitination.
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Relative opioid efficacy is determined by the complements of the G protein-coupled receptor desensitization machinery.
TL;DR: A rationale is presented to explain the seemingly paradoxical relationship between beta-arrestins and microOR regulation wherein morphine-like agonists fail to promote efficient internalization and resensitization of the receptor.