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 mammalian beta-adrenergic receptor by cyclic AMP-dependent protein kinase. Regulation of the rate of receptor phosphorylation and dephosphorylation by agonist occupancy and effects on coupling of the receptor to the stimulatory guanine nucleotide regulatory protein.
J. L. Benovic,L J Pike,R A Cerione,C Staniszewski,T Yoshimasa,Juan Codina,M G Caron,Robert J. Lefkowitz +7 more
TL;DR: The quantitative extent of receptor phosphorylation and functional impairment are virtually identical to those previously observed when intact turkey erythrocytes were incubated with cyclic AMP.
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Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function.
TL;DR: The data indicate that the regions of the alpha 1AR that determine coupling to phosphatidylinositol metabolism are similar to those previously shown to be involved in coupling of beta 2AR to adenylate cyclase stimulation and that point mutations of a G-protein-coupled receptor can cause remarkable increases in sensitivity of biological response.
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New Roles for β-Arrestins in Cell Signaling: Not Just for Seven-Transmembrane Receptors
TL;DR: beta-arrestins are increasingly found to perform analogous functions for receptors from structurally diverse classes, including atypical 7TMRs such as frizzled and smoothened, the nicotinic cholinergic receptors, receptor tyrosine kinases, and cytokine receptors, thereby regulating a growing list of cellular processes such as chemotaxis, apoptosis, and metastasis.
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Expansion of the alpha 2-adrenergic receptor family: cloning and characterization of a human alpha 2-adrenergic receptor subtype, the gene for which is located on chromosome 2.
Jon W. Lomasney,Wulfing Lorenz,Lee F. Allen,Klim King,John W. Regan,Theresa L. Yang-Feng,Marc G. Caron,Robert J. Lefkowitz +7 more
TL;DR: The cloned human alpha 2AR is cloned by using the polymerase chain reaction with oligonucleotide primers homologous to conserved regions of the previously clonedAlpha 2ARs, the genes for which are located on human chromosomes 4 (C4) and 10 (C10) and the deduced amino acid sequence encodes a protein of 450 amino acids whose putative topology is similar to that of the family of guanine nucleotide-binding protein-c
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Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases.
TL;DR: The results indicate that rhodopsin kinase and β ARK both rely on the function of isoprenyl moieties for their translocation and activity, illustrating distinct, though related, modes of biological regulation of receptor function.