J
Jeffrey M. Stadel
Researcher at Howard Hughes Medical Institute
Publications - 38
Citations - 3770
Jeffrey M. Stadel is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Receptor & Cyclase. The author has an hindex of 23, co-authored 38 publications receiving 3695 citations. Previous affiliations of Jeffrey M. Stadel include Duke University.
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Journal ArticleDOI
A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor.
TL;DR: In this paper, a ternary complex model was used to fit the data with high accuracy under conditions where the ligand used is either a full or a partial agonist and where the system is altered by the addition of guanine nucleotide or after treatment with group-specific reagents.
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Adenylate cyclase-coupled beta-adrenergic receptors: structure and mechanisms of activation and desensitization.
Journal ArticleDOI
Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor
Jeffrey M. Stadel,Ponnal Nambi,Robert G. L. Shorr,Diane F. Sawyer,Marc G. Caron,Robert J. Lefkowitz +5 more
TL;DR: The data show that catecholamine-induced desensitization of adenylate cyclase in turkey erythrocytes correlates with a stable modification of the beta-adrenergic receptor and is associated with agonist-promoted phosphorylation of beta-receptor peptides.
Journal ArticleDOI
Desensitization of the beta-adrenergic receptor of frog erythrocytes. Recovery and characterization of the down-regulated receptors in sequestered vesicles.
Jeffrey M. Stadel,Berta Strulovici,Ponnal Nambi,T N Lavin,M M Briggs,Marc G. Caron,Robert J. Lefkowitz +6 more
TL;DR: The results suggest that neither the nucleotide regulatory protein nor the catalytic unit of adenylate cyclase are sequestered along with the receptor into the vesicles during desensitization, as suggested in frog erythrocytes with isoproterenol.
Journal ArticleDOI
Ubiquitin fusion augments the yield of cloned gene products in Escherichia coli.
Tauseef R. Butt,Sobhanaditya Jonnalagadda,Brett P. Monia,E J Sternberg,Jonathan A. Marsh,Jeffrey M. Stadel,David J. Ecker,Stanley T. Crooke +7 more
TL;DR: An expression system has been established in Escherichia coli to increase the yield of cloned gene products, where the C terminus of ubiquitin was fused to the Nterminus of unstable or poorly expressed proteins.