Structure, function, and regulation of adrenergic receptors

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

Henderson, R. A., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., & Downing, K. H. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80271-2 · Cited by 2,982 · see citing works

A STUDY OF THE ADRENOTROPIC RECEPTORS

Ahlquist, R. P. (1948) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1948.153.3.586 · Cited by 2,908 · see citing works

Differentiation of Receptor Systems activated by Sympathomimetic Amines

Lands, A. M., ARNOLD, A., McAuliff, J. P., Ludueña, F. P., & Brown, T. G. (1967) · Nature · doi:10.1038/214597a0 · Cited by 2,061 · see citing works

MODEL SYSTEMS FOR THE STUDY OF SEVEN-TRANSMEMBRANE-SEGMENT RECEPTORS

Dohlman, H. G., Thorner, J. W., Caron, M. G., & Lefkowitz, R. J. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.003253 · Cited by 1,377 · see citing works

Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin

Dixon, R. A. F., Kobilka, B. K., Strader, D. J., Benovic, J., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., et al. (1986) · Nature · doi:10.1038/321075a0 · Cited by 1,275 · see citing works

Transcription Factor Interactions: Selectors of Positive or Negative Regulation from a Single DNA Element

Diamond, M. I., Miner, J. N., Yoshinaga, S. K., & Yamamoto, K. R. (1990) · Science · doi:10.1126/science.2119054 · Cited by 1,274 · see citing works

A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model.

Samama, P., Cotecchia, S., Costa, T., & Lefkowitz, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53442-6 · Cited by 1,256 · see citing works

β-Arrestin: a Protein that Regulates β-adrenergic Receptor Function

Lohse, M. J., Benovic, J., Codina, J., Caron, M. G., & Lefkowitz, R. J. (1990) · Science · doi:10.1126/science.2163110 · Cited by 1,222 · see citing works

Receptor-effector coupling by G proteins

Birnbaumer, L., Abramowitz, J., & Brown, A. M. (1990) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(90)90007-y · Cited by 1,121 · see citing works

Molecular Characterization of the Human β 3 -Adrenergic Receptor

Emorine, L. J., Marullo, S., BRIEND‐SUTREN, M., Patey, G., Tate, K. M., Delavier-Klutchko, C., & Strosberg, A. D. (1989) · Science · doi:10.1126/science.2570461 · Cited by 1,086 · see citing works

Cloning, Sequencing, and Expression of the Gene Coding for the Human Platelet α 2 -Adrenergic Receptor

Kobilka, B. K., Matsui, H., Kobilka, T. S., Yang‐Feng, T. L., Francke, U., Caron, M. G., Lefkowitz, R. J., & Regan, J. W. (1987) · Science · doi:10.1126/science.2823383 · Cited by 786 · see citing works

Chimeric α 2 -,β 2 -Adrenergic Receptors: Delineation of Domains Involved in Effector Coupling and Ligand Binding Specificity

Kobilka, B. K., Kobilka, T. S., Daniel, K. W., Regan, J. W., Caron, M. G., & Lefkowitz, R. J. (1988) · Science · doi:10.1126/science.2836950 · Cited by 763 · see citing works

cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor.

Kobilka, B. K., Dixon, R. A. F., Frielle, T., Dohlman, H. G., Bolanowski, M. A., Sigal, I. S., Yang-Feng, T. L., Francke, U., Caron, M. G., & Lefkowitz, R. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.1.46 · Cited by 679 · see citing works

Palmitoylation of the human β2-adrenergic receptor

O’Dowd, B. F., Hnatowich, M. R., Caron, M. G., Lefkowitz, R. J., & Bouvier, M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83271-9 · Cited by 598 · see citing works

Cloning of the cDNA for the human beta 1-adrenergic receptor.

Frielle, T., Collins, S., Daniel, K. W., Caron, M. G., Lefkowitz, R. J., & Kobilka, B. K. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.7920 · Cited by 575 · see citing works

Tissue distribution of beta 3-adrenergic receptor mRNA in man

Krief, S., Lönnqvist, F., Raimbault, S., Baude, B., Van Spronsen, A., Arner, P., Strosberg, A. D., Ricquier, D., & Emorine, L. J. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116191 · Cited by 528 · see citing works

Identification of Two Serine Residues Involved in Agonist Activation of the β-Adrenergic Receptor

Strader, C. D., Candelore, M. R., Hill, W. S., Sigal, I. S., & Dixon, R. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80035-7 · Cited by 523 · see citing works

Removal of phosphorylation sites from the β2-adrenergic receptor delays onset of agonist-promoted desensitization

Bouvier, M., Hausdorff, W. P., Blasi, A. D., O’Dowd, B. F., Kobilka, B. K., Caron, M. G., & Lefkowitz, R. J. (1988) · Nature · doi:10.1038/333370a0 · Cited by 437 · see citing works

Cloning and expression of a human kidney cDNA for an alpha 2-adrenergic receptor subtype.

Regan, J. W., Kobilka, T. S., Yang-Feng, T. L., Caron, M. G., Lefkowitz, R. J., & Kobilka, B. K. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6301 · Cited by 434 · see citing works

Molecular cloning and expression of the cDNA for a novel alpha 1-adrenergic receptor subtype.

Schwinn, D. A., Lomasney, J. W., Lorenz, W., Szklut, P., Fremeau, R. T., Yang-Feng, T. L., Caron, M. G., Lefkowitz, R. J., & Cotecchia, S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39055-6 · Cited by 418 · see citing works

Phosphorylation Sites on Two Domains of the β2-Adrenergic Receptor Are Involved in Distinct Pathways of Receptor Desensitization

Hausdorff, W. P., Bouvier, M., O’Dowd, B. F., Irons, G. P., Caron, M. G., & Lefkowitz, R. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63907-9 · Cited by 414 · see citing works

Subtypes of α 1 ‐ and α 2 ‐adrenergic receptors

Bylund, D. B. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.3.1346768 · Cited by 366 · see citing works

Adrenergic Receptors As Models For G Protein-Coupled Receptors

Kobilka, B. K. (1992) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.15.030192.000511 · Cited by 365 · see citing works

Structural features required for ligand binding to the beta‐adrenergic receptor.

Dixon, R. A., Sigal, I. S., Candelore, M. R., Register, R. B., Scattergood, W., Rands, E., & Strader, C. D. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02645.x · Cited by 354 · see citing works

G-protein-coupled receptor genes as protooncogenes: constitutively activating mutation of the alpha 1B-adrenergic receptor enhances mitogenesis and tumorigenicity.

Allen, L. F., Lefkowitz, R. J., Caron, M. G., & Cotecchia, S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11354 · Cited by 322 · see citing works

Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function.

Cotecchia, S., Exum, S. T., Caron, M. G., & Lefkowitz, R. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2896 · Cited by 308 · see citing works

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.

Lomasney, J. W., Lorenz, W., Allen, L. F., King, K., Regan, J. W., Yang‐Feng, T. L., Caron, M. G., & Lefkowitz, R. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5094 · Cited by 283 · see citing works

Two distinct pathways for cAMP-mediated down-regulation of the β2-adrenergic receptor

Bouvier, M., Collins, S., O’Dowd, B. F., Campbell, P. T., Blasi, A. D., Kobilka, B. K., MacGregor, C., Irons, G. P., Caron, M. G., & Lefkowitz, R. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84774-9 · Cited by 270 · see citing works

Identification of a Gs activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation

Okamoto, T., Murayama, Y., Hayashi, Y., Inagaki, M., Ogata, E., & Nishimoto, I. (1991) · Cell · doi:10.1016/0092-8674(91)90067-9 · Cited by 270 · see citing works

Mutations that uncouple the beta-adrenergic receptor from Gs and increase agonist affinity.

Strader, C. D., Dixon, R. A. F., Cheung, A. H., Candelore, M. R., Blake, A. D., & Sigal, I. S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49275-7 · Cited by 261 · see citing works

Purification and characterization of the beta-adrenergic receptor kinase.

Benovic, J., Mayor, F., Staniszewski, C., Lefkowitz, R. J., & Caron, M. G. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48041-6 · Cited by 248 · see citing works

The avian beta-adrenergic receptor: primary structure and membrane topology.

Yarden, Y., Rodriguez, H., Wong, S. K., Brandt, D. R., May, D. C., Burnier, J. P., Harkins, R. N., Chen, E. Y., Ramachandran, J., & Ullrich, A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.18.6795 · Cited by 248 · see citing works

Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteins

Strosberg, A. D. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15778.x · Cited by 241 · see citing works

Allele-specific activation of genetically engineered receptors.

Strader, C. D., Gaffney, T., Sugg, E. E., Candelore, M. R., Keys, R., Patchett, A. A., & Dixon, R. A. F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52392-9 · Cited by 228 · see citing works

Role of extracellular disulfide-bonded cysteines in the ligand binding function of the .beta.2-adrenergic receptor

Dohlman, H. G., Caron, M. G., DeBlasi, A., Frielle, T., & Lefkowitz, R. J. (1990) · Biochemistry · doi:10.1021/bi00461a018 · Cited by 213 · see citing works

Pharmacological characteristics of alpha 2-adrenergic receptors: comparison of pharmacologically defined subtypes with subtypes identified by molecular cloning.

Bylund, D., Blaxall, H. S., Iversen, L. J., Caron, M. G., Lefkowitz, R. J., & Lomasney, J. W. (1992) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)08833-9 · Cited by 207 · see citing works

Mutagenesis Of The Beta 2-Adrenergic Receptor: How Structure Elucidates Function

Ostrowski, J., Kjelsberg, M. A., Caron, M. G., & Lefkowitz, R. J. (1992) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.32.040192.001123 · Cited by 192 · see citing works

Agonist-modulated palmitoylation of beta 2-adrenergic receptor in Sf9 cells.

Mouillac, B., Caron, M., Bonin, H., Dennis, M., & Bouvier, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36673-6 · Cited by 175 · see citing works

The human beta 3-adrenergic receptor is resistant to short term agonist-promoted desensitization.

Nantel, F., Bonin, H., Emorine, L. J., Zilberfarb, V., Strosberg, A. D., Bouvier, M., & Marullo, S. (1993) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13419-6 · Cited by 174 · see citing works

Regulation of Adrenergic Receptor Responsiveness Through Modulation of Receptor Gene Expression

Collins, S., Caron, M. G., & Lefkowitz, R. J. (1991) · Annual Review of Physiology · doi:10.1146/annurev.ph.53.030191.002433 · Cited by 173 · see citing works

Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization.

Emorine, L. J., Marullo, S., Delavier-Klutchko, C., Kaveri, S. V., Durieu-Trautmann, O., & Strosberg, A. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.20.6995 · Cited by 172 · see citing works

Structural basis of beta-adrenergic receptor subtype specificity studied with chimeric beta 1/beta 2-adrenergic receptors.

Frielle, T., Daniel, K. W., Caron, M. G., & Lefkowitz, R. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.24.9494 · Cited by 162 · see citing works

Discrete amino acid sequences of the alpha 1-adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis.

Cotecchia, S., Ostrowski, J., Kjelsberg, M. A., Caron, M. G., & Lefkowitz, R. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45992-3 · Cited by 162 · see citing works

Affinity chromatography of the beta-adrenergic receptor.

Caron, M. G., Srinivasan, Y., Pitha, J., Kociolek, K., & Lefkowitz, R. J. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30162-x · Cited by 161 · see citing works

A Point Mutation of the α 2 -Adrenoceptor that Blocks Coupling to Potassium but not Calcium Currents

Surprenant, A., Horstman, D. A., Akbarali, H. I., & Limbird, L. E. (1992) · Science · doi:10.1126/science.1354394 · Cited by 161 · see citing works

Altered phosphorylation and desensitization patterns of a human beta 2‐adrenergic receptor lacking the palmitoylated Cys341.

Moffett, S., Mouillac, B., Bonin, H., & Bouvier, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05663.x · Cited by 161 · see citing works

Cloning of two mouse genes encoding alpha 2-adrenergic receptor subtypes and identification of a single amino acid in the mouse alpha 2-C10 homolog responsible for an interspecies variation in antagonist binding.

Link, R. E., Daunt, D. A., Barsh, G. S., Chruscinski, A. J., & Kobilka, B. K. (1992) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)08854-6 · Cited by 161 · see citing works

Genomic organization and expression of the human alpha 1B-adrenergic receptor.

Ramarao, C. S., Denker, J. A., Perez, D. M., Gaivin, R. J., Riek, R., & Graham, R. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36703-1 · Cited by 160 · see citing works

Molecular characterization of α1- and α2-adrenoceptors

Harrison, J. K., Pearson, W. R., & Lynch, K. R. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90499-i · Cited by 155 · see citing works

A point mutation in the seventh hydrophobic domain of the alpha 2 adrenergic receptor increases its affinity for a family of beta receptor antagonists

Suryanarayana, S., Daunt, D. A., von Zastrow, M., & Kobilka, B. K. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98642-4 · Cited by 145 · see citing works

Structure-Function Analysis of the -Adrenergic ReceptorPreprint

Dixon, R. A. F., Sigal, I. S., & Strader, C. D. (1988) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1988.053.01.056 · Cited by 145 · see citing works

The carboxyl terminus of the hamster β-adrenergic receptor expressed in mouse L cells is not required for receptor sequestration

Strader, C. D., Sigal, I. S., Blake, A. D., Cheung, A. H., Register, R. B., Rands, E., Zemcik, B. A., Candelore, M. R., & Dixon, R. A. F. (1987) · Cell · doi:10.1016/0092-8674(87)90623-4 · Cited by 140 · see citing works

A cAMP response element in the beta 2-adrenergic receptor gene confers transcriptional autoregulation by cAMP.

Collins, S., Altschmied, J., Herbsman, O., Caron, M. G., Mellon, P. L., & Lefkowitz, R. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30662-2 · Cited by 135 · see citing works

A Single Amino Acid Substitution in the β-Adrenergic Receptor Promotes Partial Agonist Activity from Antagonists

Strader, C. D., Candelore, M. R., Hill, W. S., Dixon, R. A. F., & Sigal, I. S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84729-4 · Cited by 133 · see citing works

Site-directed mutagenesis of human beta-adrenergic receptors: substitution of aspartic acid-130 by asparagine produces a receptor with high-affinity agonist binding that is uncoupled from adenylate cyclase.

Fraser, C. M., Chung, F., Wang, C. D., & Venter, J. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5478 · Cited by 133 · see citing works

Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors.

Lohse, M. J., Lefkowitz, R. J., Caron, M. G., & Benovic, J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3011 · Cited by 122 · see citing works

The catecholamine binding site of the beta-adrenergic receptor is formed by juxtaposed membrane-spanning domains.

Wong, S. K., Slaughter, C. A., Ruoho, A. E., & Ross, E. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68420-0 · Cited by 122 · see citing works

Beta-adrenergic agonists that down-regulate receptor mRNA up-regulate a M(r) 35,000 protein(s) that selectively binds to beta-adrenergic receptor mRNAs.

Port, J. D., Huang, L. Y., & Malbon, C. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35952-0 · Cited by 118 · see citing works

Long-term agonist exposure induces upregulation of beta 3-adrenergic receptor expression via multiple cAMP response elements.

Thomas, R. F., Holt, B. D., Schwinn, D. A., & Liggett, S. B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4490 · Cited by 117 · see citing works

Atypical beta-adrenergic receptor in 3T3-F442A adipocytes. Pharmacological and molecular relationship with the human beta 3-adrenergic receptor.

Fève, B., Emorine, L. J., Lasnier, F., Blin, N., Baude, B., Nahmias, C., Strosberg, A. D., & Pairault, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54927-9 · Cited by 116 · see citing works

Cloning, sequencing, and expression of the gene encoding the porcine alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and amiloride analogs.

Guyer, C. A., Horstman, D. A., Wilson, A. L., Clark, J. D., Cragoe, E. J., & Limbird, L. E. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44904-0 · Cited by 116 · see citing works

Involvement of tyrosine residues located in the carboxyl tail of the human beta 2-adrenergic receptor in agonist-induced down-regulation of the receptor.

Valiquette, M., Bonin, H., Hnatowich, M. R., Caron, M. G., Lefkowitz, R. J., & Bouvier, M. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5089 · Cited by 105 · see citing works

Cross-talk between tyrosine kinase and G-protein-linked receptors. Phosphorylation of beta 2-adrenergic receptors in response to insulin.

Hadcock, J. R., Port, J. D., Gelman, M. S., & Malbon, C. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35710-7 · Cited by 102 · see citing works

Isolation of adenylate cyclase-free, beta-adrenergic receptor from turkey erythrocyte membranes by affinity chromatography.

Vauquelin, G., Geynet, P., Hanoune, J., & Strosberg, A. D. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.9.3710 · Cited by 102 · see citing works

Characterization of the binding domain of the beta-adrenergic receptor with the fluorescent antagonist carazolol. Evidence for a buried ligand binding site.

Tota, M. R., & Strader, C. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44846-0 · Cited by 100 · see citing works

Evidence for essential disulfide bonds in beta1-adrenergic receptors of turkey erythrocyte membranes. Inactivation by dithiothreitol.

Vauquelin, G., Bottari, S. P., Kanarek, L., & Strosberg, A. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30032-7 · Cited by 98 · see citing works

Agonist Regulation of β-Adrenergic Receptor mRNA

Hadcock, J. R., Ros, M., & Malbon, C. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80092-8 · Cited by 88 · see citing works

The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols.

Rubenstein, R. C., Wong, S., & Ross, E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49305-2 · Cited by 88 · see citing works

Selective binding of ligands to beta 1, beta 2 or chimeric beta 1/beta 2‐adrenergic receptors involves multiple subsites.

Marullo, S., Emorine, L. J., Strosberg, A. D., & Delavier-Klutchko, C. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08264.x · Cited by 78 · see citing works

Inhibition by dexamethasone of beta 3-adrenergic receptor responsiveness in 3T3-F442A adipocytes. Evidence for a transcriptional mechanism.

Fève, B., Baude, B., Krief, S., Strosberg, A. D., Pairault, J., & Emorine, L. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49620-8 · Cited by 76 · see citing works

Molecular cloning and sequencing of a cDNA encoding a human α1A adrenergic receptor

Bruno, J. F., Whittaker, J., Song, J., & Berelowitz, M. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91740-4 · Cited by 70 · see citing works

Structural basis for functional diversity of β1-, β2- and β3-adrenergic receptors

Emorine, L. J., Fève, B., Pairault, J., BRIEND‐SUTREN, M., Marullo, S., Delavier-Klutchko, C., & Strosberg, A. D. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90188-b · Cited by 62 · see citing works

Expression of Human β1 and β2 Adrenergic Receptors in E. Coli As a New Tool for Ligand Screening

Marullo, S., Delavier-Klutchko, C., Guillet, J., Charbit, A., Strosberg, A. D., & Emorine, L. J. (1989) · Nature Biotechnology · doi:10.1038/nbt0989-923 · Cited by 58 · see citing works

Mutational analysis of ligand binding activity of beta 2 adrenergic receptor expressed in Escherichia coli.

BREYER, R. M., Strosberg, A. D., & Guillet, J. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07453.x · Cited by 41 · see citing works

Affinity Chromatography of the β‐Adrenergic Receptor from Turkey Erythrocytes

Vauquelin, G., Geynet, P., Hanoune, J., & Strosberg, A. D. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb13215.x · Cited by 40 · see citing works

Biotechnology of β-adrenergic receptors

Strosberg, A. D. (1990) · Molecular Neurobiology · doi:10.1007/bf02780342 · Cited by 38 · see citing works

The oligosaccharide moiety of the .beta.1-adrenergic receptor from turkey erythrocytes has a biantennary, N-acetyllactosamine-containing structure

CERVANTES‐OLIVIER, P., Durieu-Trautmann, O., Delavier-Klutchko, C., & Strosberg, A. D. (1985) · Biochemistry · doi:10.1021/bi00335a052 · Cited by 38 · see citing works

The β2-adrenergic receptors of human epidermoid carcinoma cells bear two different types of oligosaccharides which influence expression on the cell surface

CERVANTES‐OLIVIER, P., Delavier-Klutchko, C., Durieu-Trautmann, O., Kaveri, S. V., Desmandril, M., & Strosberg, A. D. (1988) · Biochemical Journal · doi:10.1042/bj2500133 · Cited by 31 · see citing works

In receptors coupled to GTP-binding proteins, ligand binding and G-protein activation is a multistep dynamic process.

Strosberg, A. D., Camoin, L., Blin, N., & Maigret, B. (1993) · PubMed · Cited by 21 · see citing works

Functional expression of receptors in microorganisms

Strosberg, A. D., & Marullo, S. (1992) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(92)90035-5 · Cited by 16 · see citing works

High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Kühn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,280 · see citing works

A Peptide Derived from a β2-Adrenergic Receptor Transmembrane Domain Inhibits Both Receptor Dimerization and Activation

Hébert, T. E., Moffett, S., Morello, J.-P., Loisel, T. P., Bichet, D. G., Barret, C., & Bouvier, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16384 · Cited by 775 · see citing works

Functional beta3-adrenoceptor in the human heart.

Gauthier, C., Tavernier, G., Charpentier, F., Langin, D., & Marec, H. L. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118823 · Cited by 461 · see citing works

Locating ligand-binding sites in 7tm receptors by protein engineering

Schwartz, T. W. (1994) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(94)90054-x · Cited by 274 · see citing works

The β-Adrenergic Receptors

Wallukat, G. (2002) · Herz · doi:10.1007/s00059-002-2434-z · Cited by 273 · see citing works

STRUCTURE AND FUNCTION OF THE β3-ADRENERGIC RECEPTOR

Strosberg, A. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.421 · Cited by 250 · see citing works

Psychedelics in Psychiatry: Neuroplastic, Immunomodulatory, and Neurotransmitter Mechanisms

Inserra, A., De Gregorio, D., & Gobbi, G. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000056 · Cited by 232 · see citing works

Participation of noradrenergic pathways in the expression of opiate withdrawal: biochemical and pharmacological evidence

MALDONADO, R. (1997) · Neuroscience & Biobehavioral Reviews · doi:10.1016/0149-7634(95)00061-5 · Cited by 213 · see citing works

A nervous tumor microenvironment: the impact of adrenergic stress on cancer cells, immunosuppression, and immunotherapeutic response

Eng, J. W. ‐., Kokolus, K. M., Reed, C. B., Hylander, B. L., Ma, W. W., & Repasky, E. A. (2014) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-014-1617-9 · Cited by 189 · see citing works

Hepatic stellate cell senescence in liver fibrosis: Characteristics, mechanisms and perspectives

Zhang, M., Salas, S. S., Damba, T., Borghesan, M., Demaria, M., & Moshage, H. J. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111572 · Cited by 180 · see citing works

The Effect of Diabetes on Expression of β1-,β2-, and β3-Adrenoreceptors in Rat Hearts

Dinçer, Ü. D., Bidasee, K. R., Güner, Ş., Tay, A., Ozcelikay, A. T., & ALTAN, V. M. (2001) · Diabetes · doi:10.2337/diabetes.50.2.455 · Cited by 172 · see citing works

Mechanisms of ketamine and its metabolites as antidepressants

Hess, E. M., Riggs, L. M., Michaelides, M., & Gould, T. D. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114892 · Cited by 169 · see citing works

Function and regulation of the β3-adrenoceptor

Strosberg, A. D., & Piétri‐Rouxel, F. (1996) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(96)80011-3 · Cited by 167 · see citing works

Role of adrenergic receptor signalling in neuroimmune communication

Chhatar, S., & Lal, G. (2021) · Current Research in Immunology · doi:10.1016/j.crimmu.2021.11.001 · Cited by 143 · see citing works

Monoamine Oxidase Inhibitors: A Review of Their Anti-Inflammatory Therapeutic Potential and Mechanisms of Action

Ostadkarampour, M., & Putnins, E. E. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.676239 · Cited by 133 · see citing works

Mutagenesis and the Molecular Modeling of the Rat Angiotensin II Receptor (AT1)

Yamano, Y., Ohyama, K., Kikyo, M., Sano, T., Nakagomi, Y., Inoue, Y., Nakamura, N., Morishima, I., Guo, D., Hamakubo, T., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.14024 · Cited by 119 · see citing works

Recent Advances in Structure-Based Drug Design Targeting Class A G Protein-Coupled Receptors Utilizing Crystal Structures and Computational Simulations

Lee, Y., Basith, S., & Choi, S. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01453 · Cited by 116 · see citing works

Palmitoylated Cysteine 341 Modulates Phosphorylation of the β2-Adrenergic Receptor by the cAMP-dependent Protein Kinase

Moffett, S., Adam, L., Bonin, H., Loisel, T. P., Bouvier, M., & Mouillac, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.35.21490 · Cited by 114 · see citing works

Functional autoantibodies targeting G protein-coupled receptors in rheumatic diseases

Cabral-Marques, O., & Riemekasten, G. (2017) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2017.134 · Cited by 93 · see citing works

Direct Identification of a Distinct Site of Interaction between the Carboxyl-terminal Residue of Cholecystokinin and the Type A Cholecystokinin Receptor Using Photoaffinity Labeling

Ji, Z., Hadac, E. M., Henne, R. M., Patel, S. A., Lybrand, T. P., & Miller, L. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24393 · Cited by 94 · see citing works

Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human β2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris

Weiss, H., Haase, W., Michel, H., & Reiländer, H. (1998) · Biochemical Journal · doi:10.1042/bj3301137 · Cited by 90 · see citing works

New Molecular and Structural Determinants Involved in β2-Adrenergic Receptor Desensitization and Sequestration

Jockers, R., Silva, A. D., Strosberg, A. D., Bouvier, M., & Marullo, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9355 · Cited by 90 · see citing works

Functional rescue of a constitutively desensitized β2AR through receptor dimerization

Hébert, E., LOISEL, P. T., Adam, L., Éthier, N., ONGE, S. S., & Bouvier, M. (1998) · Biochemical Journal · doi:10.1042/bj3300287 · Cited by 90 · see citing works

Gut microbial-derived phenylacetylglutamine accelerates host cellular senescence

Yang, H., Wang, T., Qian, C., Wang, H., Yu, D. S., Shi, M., Fu, M., Liu, X., Pan, M., Rong, X., et al. (2025) · Nature Aging · doi:10.1038/s43587-024-00795-w · Cited by 85 · see citing works

Cloning and functional analysis of a polymorphic variant of the ovine Mel 1a melatonin receptor

Barrett, P., Conway, S., Jockers, R., Strosberg, A. D., Lemaître, B. J., Delagrange, P., & Morgan, P. J. (1997) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(96)00179-6 · Cited by 81 · see citing works

Activity of the unique β-adrenergic Na+/H+exchanger in trout erythrocytes is controlled by a novel β3-AR subtype

Nickerson, J. G., Dugan, S. G., Drouin, G., Perry, S. F., & Moon, T. W. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00146.2003 · Cited by 78 · see citing works

Multiple signalling pathways involved in β2‐adrenoceptor‐mediated glucose uptake in rat skeletal muscle cells

Nevzorova, J., Evans, B. A., Bengtsson, T., & Summers, R. J. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706626 · Cited by 78 · see citing works

The role of autoantibodies in the syndromes of orthostatic intolerance: a systematic review

Ruzieh, M., Batizy, L. H., Dasa, O., Oostra, C., & Grubb, B. P. (2017) · Scandinavian Cardiovascular Journal · doi:10.1080/14017431.2017.1355068 · Cited by 74 · see citing works

A putative β2‐adrenoceptor from the rainbow trout (Oncorhynuchus mykiss)

Nickerson, J. G., Dugan, S. G., Drouin, G., & Moon, T. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02600.x · Cited by 74 · see citing works

The Mouse Gene for the Inducible G-Protein-Coupled Receptoredg-1

Liu, C. H., & Hla, T. (1997) · Genomics · doi:10.1006/geno.1997.4759 · Cited by 73 · see citing works

Beta-Adrenergic receptor modulation of adipocyte metabolism and growth

Mersmann, H. J. (2002) · Journal of Animal Science · doi:10.2527/animalsci2002.0021881200800es10005x · Cited by 70 · see citing works

Biased agonism at β-adrenergic receptors

Ippolito, M. J., & Benovic, J. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109905 · Cited by 68 · see citing works

STRUCTURE AND FUNCTION OF THE 3 -ADRENERGIC RECEPTOR

Strosberg, A. D. (1997) · Cited by 68 · see citing works

Cloning of the rat and human prostaglandin F2α receptors and the expression of the rat prostaglandin F2α receptor

Lake, S., Gullberg, H., Wahlqvist, J., Sjogren, A., Kinhult, A. K. K., Lind, P., Hellström‐Lindahl, E., & Stjernschantz, J. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01198-2 · Cited by 68 · see citing works

Is There a Role for PGE2 in Urinary Concentration?

Olesen, E. T. B., & Fenton, R. A. (2012) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012020217 · Cited by 67 · see citing works

α1A- and α1B-adrenergic receptors differentially modulate antidepressant-like behavior in the mouse

Doze, V. A., Handel, E. M., Jensen, K. A., Darsie, B., Luger, E., Haselton, J. R., Talbot, J. N., & Rorabaugh, B. R. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.035 · Cited by 66 · see citing works

Steric Hindrance Mutagenesis versus Alanine Scan in Mapping of Ligand Binding Sites in the Tachykinin NK1 Receptor

Holst, B., Zoffmann, S., Elling, C., Hjorth, S. A., & Schwartz, T. W. (1998) · Molecular Pharmacology · doi:10.1124/mol.53.1.166 · Cited by 65 · see citing works

Adrenergic stimulation of single rat astrocytes results in distinct temporal changes in intracellular Ca2+ and cAMP-dependent PKA responses

Horvat, A., Zorec, R., & Vardjan, N. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.01.002 · Cited by 61 · see citing works

Neurochemistry of Visual Attention

Lockhofen, D. E. L., & Mulert, C. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.643597 · Cited by 62 · see citing works

New technologies for amperometric biosensors

Boutelle, M. G., Allen, H., Hill, O., Berners, M. O. M., John, R., Dobson, P. D., & Leigh, P. J. (1996) · Journal of Molecular Recognition · doi:10.1002/(sici)1099-1352(199634/12)9:5/6 · Cited by 10 · see citing works

Identification of a Conserved Switch Residue Responsible for Selective Constitutive Activation of the β2-Adrenergic Receptor

Zuscik, M. J., Porter, J. E., Gaivin, R. J., & Perez, D. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3401 · Cited by 60 · see citing works

Both alpha 1A- and alpha 2A-adrenoreceptor subtypes stimulate voltage-operated L-type calcium channels in rat portal vein myocytes. Evidence for two distinct transduction pathways.

Macrez, N., Mironneau, J., & Morel, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43914-2 · Cited by 59 · see citing works

The Negative Inotropic Effect of β3-Adrenoceptor Stimulation in the Beating Guinea Pig Heart

Kitamura, T., Onishi, K., Dohi, K., 沖中, 務., Isaka, N., & Nakano, T. (2000) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-200005000-00016 · Cited by 58 · see citing works

An agonist-like monoclonal antibody against the human β2-adrenoceptor

Lebesgue, D., Wallukat, G., Mijares, A., Granier, C., Argibay, J. A., & Hoebeke, J. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00136-8 · Cited by 55 · see citing works

Beta 3 adrenergic receptors: molecular, histological, functional and pharmacological approaches.

Coman, O. A., Păunescu, H., Ghiţă, I., Coman, L., Bădărăru, A., & Fulga, I. (2009) · PubMed · Cited by 53 · see citing works

Functional, biochemical and molecular biological evidence for a possible β3‐adrenoceptor in human near‐term myometrium

Bardou, M., Loustalot, C., Cortijo, J., Simon, B., Naline, E., Dumas, M., Esteve, S., Croci, T., Chalon, P., Frydman, R., et al. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703491 · Cited by 53 · see citing works

Gβγ subunit combinations differentially modulate receptor and effector coupling in vivo

Robillard, L., Éthier, N., Lachance, M., & Hébert, T. E. (2000) · Cellular Signalling · doi:10.1016/s0898-6568(00)00118-2 · Cited by 52 · see citing works

Inter-Kingdom Signaling of Stress Hormones: Sensing, Transport and Modulation of Bacterial Physiology

Boukerb, A. M., Cambronel, M., Rodrigues, S., Mesguida, O., Knowlton, R., Feuilloley, M. G. J., Zommiti, M., & Connil, N. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.690942 · Cited by 46 · see citing works

Lipids shape brain function through ion channel and receptor modulations: physiological mechanisms and clinical perspectives

Incontro, S., Musella, M. L., Sammari, M., Scala, C. D., Fantini, J., & Debanne, D. (2024) · Physiological Reviews · doi:10.1152/physrev.00004.2024 · Cited by 48 · see citing works

Norepinephrine induces apoptosis in neonatal rat endothelial cells via down-regulation of Bcl-2 and activation of β-adrenergic and caspase-2 pathways

Fu, Y. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.10.014 · Cited by 46 · see citing works

Metabolic reprogramming by tobacco-specific nitrosamines (TSNAs) in cancer

Sarlak, S., Lalou, C., Amoêdo, N. D., & Rossignol, R. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.09.001 · Cited by 47 · see citing works

Neurochemistry of the Kölliker‐Fuse nucleus from a respiratory perspective

Varga, A. G., Maletz, S. N., Bateman, J. T., Reid, B. T., & Levitt, E. S. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15041 · Cited by 43 · see citing works

Antibodies for the Immunochemistry of the Human β3‐Adrenergic Receptor

Guillaume, J., Petitjean, F., Haasemann, M., Bianchi, C. F., Eshdat, Y., & Strosberg, A. D. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00761.x · Cited by 44 · see citing works

Pharmacological characteristics and species‐related variations of β3‐adrenergic receptors

Piétri‐Rouxel, F., & Strosberg, A. D. (1995) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.1995.tb00288.x · Cited by 44 · see citing works

Noradrenergic Control of Gene Expression and Long-Term Neuronal Adaptation Evoked by Learned Vocalizations in Songbirds

Velho, T., Lu, K., Ribeiro, S. T. G., Pinaud, R., Vicario, D. S., & Mello, C. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036276 · Cited by 43 · see citing works

Adrenergic Downregulation in Critical Care: Molecular Mechanisms and Therapeutic Evidence

Belletti, A., Landoni, G., Ломиворотов, В. В., Oriani, A., & Ajello, S. (2019) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2019.10.017 · Cited by 41 · see citing works

Adrenergic signalling in osteoarthritis

Sohn, R. E., Rösch, G., Junker, M., Meurer, A., Zaucke, F., & Jenei‐Lanzl, Z. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109948 · Cited by 41 · see citing works

? 2-Adrenoceptors activate dihydropyridine-sensitive calcium channels via Gi-proteins and protein kinase C in rat portal vein myocytes

Lepr�tre, N., & Mironneau, J. (1994) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00374320 · Cited by 40 · see citing works

Molecular Changes in Opioid Addiction: The Role of Adenylyl Cyclase and cAMP/PKA System

Chan, P., & Lutfy, K. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.10.005 · Cited by 38 · see citing works

α-Synuclein and Noradrenergic Modulation of Immune Cells in Parkinson’s Disease Pathogenesis

Butkovich, L. M., Houser, M. C., & Tansey, M. G. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00626 · Cited by 37 · see citing works

1,3‐Diazepine: A privileged scaffold in medicinal chemistry

Malki, Y., Martínez, J., & Masurier, N. (2021) · Medicinal Research Reviews · doi:10.1002/med.21795 · Cited by 37 · see citing works

Are so many adrenergic receptor subtypes really present in domestic animal tissues? A pharmacological perspective

Badino, P., Odore, R., & Re, G. (2004) · The Veterinary Journal · doi:10.1016/j.tvjl.2004.05.015 · Cited by 37 · see citing works

Carazolol: a potent, selective β3-adrenoceptor agonist

Méjean, A., Guillaume, J., & Strosberg, A. D. (1995) · European Journal of Pharmacology Molecular Pharmacology · doi:10.1016/0922-4106(95)90077-2 · Cited by 36 · see citing works

Molecular Cloning and Pharmacological Characterization of the Bovine beta3-adrenergic Receptor

Piétri‐Rouxel, F., Lenzen, G., Kapoor, A., Drumare, M.-F., Archimbault, P., Strosberg, A. D., & Manning, B. S. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0350i.x · Cited by 36 · see citing works

Glucose Intolerance on Phaeochromocytoma and Paraganglioma—The Current Understanding and Clinical Perspectives

Abe, I., Islam, F., & Lam, A. K.-Y. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.593780 · Cited by 35 · see citing works

Neurochemical organization of the ventral striatum’s olfactory tubercle

Cansler, H. L., Wright, K. N., Stetzik, L. A., & Wesson, D. W. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14919 · Cited by 34 · see citing works

Light-induced rapid Ca2+ response and MAPK phosphorylation in the cells heterologously expressing human OPN5

Sugiyama, T., Suzuki, H., & Takahashi, T. (2014) · Scientific Reports · doi:10.1038/srep05352 · Cited by 34 · see citing works

Functional coupling of human beta 3-adrenoceptors to the KvLQT1/minK potassium channel

Kathöfer, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003331200 · Cited by 34 · see citing works

Beta-adrenergic receptor agonists induce the release of granulocyte chemotactic protein-2, oncostatin M, and vascular endothelial growth factor from macrophages

Verhoeckx, K. C. M., Doornbos, R. P., Witkamp, R. F., van der Greef, J., & Rodenburg, R. J. (2005) · International Immunopharmacology · doi:10.1016/j.intimp.2005.05.013 · Cited by 34 · see citing works

Molecular and functional diversity of the autonomic nervous system

Wang, T., Tufenkjian, A., Ajijola, O., & Oka, Y. (2025) · Nature Reviews Neuroscience · doi:10.1038/s41583-025-00941-2 · Cited by 35 · see citing works

Modulatory effects of the basolateral amygdala α2-adrenoceptors on nicotine-induced anxiogenic-like behaviours of rats in the elevated plus maze

Bashiri, H., Rezayof, A., Sahebgharani, M., Tavangar, S. M., & Zarrindast, M. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.02.010 · Cited by 33 · see citing works

Adrenoceptor Desensitization: Current Understanding of Mechanisms

Maaliki, D. S., Jaffa, A. A., Nasser, S. A., Sahebkar, A., & Eid, A. H. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.123.000831 · Cited by 32 · see citing works

β-Blockade and increased dyslipidemia in patients bearing Glu27 variant of β2 adrenergic receptor gene

Iaccarino, G., Trimarco, V., Lanni, F., Cipolletta, E., Izzo, R., Arcucci, O., LUCA, N. D., & Renzo, G. D. (2005) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500324 · Cited by 32 · see citing works

New developments in cardiovascular adrenergic receptor pharmacology: Molecular mechanisms and clinical relevance

Smiley, R. M., Kwatra, M. M., & Schwinn, D. A. (1998) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1016/s1053-0770(98)90062-3 · Cited by 32 · see citing works

The human near‐term myometrial <i>β</i>₃‐adrenoceptor but not the <i>β</i>₂‐adrenoceptor is resistant to desensitisation after sustained agonist stimulation

Rouget, C., Breuiller‐Fouché, M., Mercier, F. J., Leroy, M. J., Loustalot, C., Naline, E., Frydman, R., Croci, T., Morcillo, E. J., Advenier, C., et al. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705616 · Cited by 31 · see citing works

Purgative components in rhubarbs: Adrenergic receptor inhibitors linked with glucose carriers

Feng, T.-S., Yuan, Z., Yang, R.-Q., Zhao, S., Fan, L., Xiao, X., Xing, D., Wang, W., Ding, Y., & Du, L. (2013) · Fitoterapia · doi:10.1016/j.fitote.2013.09.020 · Cited by 31 · see citing works

β 3 Receptors: role in cardiometabolic disorders

Bhadada, S. V., Patel, B. M., Mehta, A. A., & Goyal, R. K. (2011) · Therapeutic Advances in Endocrinology and Metabolism · doi:10.1177/2042018810390259 · Cited by 31 · see citing works

Molecular Recognition by a Short Partial Peptide of the Adrenergic Receptor: A Bottom‐Up Approach

Sekiguchi, T., Tamura, M., Oba, H., Çarçarbal, P., Lozada‐Garcia, R. R., Zehnacker, A., Grégoire, G., Ishiuchi, S., & Fujii, M. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201712976 · Cited by 31 · see citing works

Inhibitory effects of the β2‐adrenergic receptor agonist zilpaterol on the LPS‐induced production of TNF‐α in vitro and in vivo

Verhoeckx, K. C. M., Doornbos, R. P., van der Greef, J., Witkamp, R. F., & Rodenburg, R. J. (2005) · Journal of Veterinary Pharmacology and Therapeutics · doi:10.1111/j.1365-2885.2005.00691.x · Cited by 30 · see citing works

Multiscale modelling to understand the self-assembly mechanism of human β2-adrenergic receptor in lipid bilayer

Ghosh, A., Sonavane, U., & Joshi, R. (2013) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2013.11.002 · Cited by 29 · see citing works

In Search of Secreted Protein Biomarkers for the Anti-inflammatory Effect of β2-Adrenergic Receptor Agonists: Application of DIGE Technology in Combination with Multivariate and Univariate Data Analysis Tools

Verhoeckx, K. C. M., Gaspari, M., Bijlsma, S., van der Greef, J., Witkamp, R. F., Doornbos, R. P., & Rodenburg, R. J. (2005) · Journal of Proteome Research · doi:10.1021/pr050183u · Cited by 29 · see citing works

Drug discovery: Past, present and future

Kaul, P. N. (1998) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8833-2_1 · Cited by 28 · see citing works

Species Variation in Mechanisms for Modulation of Growth by Beta-Adrenergic Receptors

Mersmann, H. J. (1995) · Journal of Nutrition · doi:10.1093/jn/125.suppl_6.1777s · Cited by 28 · see citing works

Probing the Immunological Properties of the Extracellular Domains of the Human β1-Adrenoceptor

Mobini, R., Magnusson, Y., Wallukat, G., Viguier, M. A., Hjalmarson, Å. C., & Hoebeke, J. (1999) · Journal of Autoimmunity · doi:10.1006/jaut.1999.0310 · Cited by 28 · see citing works

Role of G Protein-Coupled Receptors in Microglial Activation: Implication in Parkinson’s Disease

Gu, C., Chen, Y., Chen, Y., Liu, C., Zhu, Z., & Wang, M. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.768156 · Cited by 26 · see citing works

In Vitro and in Vivo Pharmacological Characterization of Ethyl-4-{trans-4-[((2 S)-2-hydroxy-3-{4-hydroxy-3[(methylsulfonyl)amino]-phenoxy}propyl) Amino]cyclohexyl}benzoate Hydrochloride (SAR150640), a New Potent and Selective Human β3-Adrenoceptor Agonist for the Treatment of Preterm Labor

Croci, T., Cecchi, R., Marini, P., Rouget, C., Viviani, N., Germain, G., Guagnini, F., Fradin, Y., Descamps, L., Pascal, M., et al. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.119123 · Cited by 26 · see citing works

Molecular and functional characteristics of β3-adrenoceptors in late pregnant mouse uterus: A comparison with β2-adrenoceptors

Parida, S., Singh, T. U., Prakash, V. R., & Mishra, S. K. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.11.048 · Cited by 25 · see citing works

Human ?3-adrenoreceptors couple to KvLQT1/MinK potassium channels in Xenopus oocytes via protein kinase C phosphorylation of the KvLQT1 protein

Kath�fer, S., R�ckl, K., Zhang, W., Thomas, D., Katus, H. A., Kiehn, J., Kreye, V. A. W., Schoels, W., & Karle, C. A. (2003) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-003-0772-x · Cited by 25 · see citing works

Structure, Function, and Regulation of the Three β‐Adrenergic Receptors

Strosberg, A. D. (1995) · Obesity Research · doi:10.1002/j.1550-8528.1995.tb00219.x · Cited by 24 · see citing works

Functional Coupling of Human β3-Adrenoreceptors to the KvLQT1/MinK Potassium Channel

Kathöfer, S., Zhang, W., Karle, C. A., Thomas, D., Schoels, W., & Kiehn, J. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61438-9 · Cited by 23 · see citing works

THE CONNECTION BETWEEN DIFFERENT NEUROTRANSMITTERS INVOLVED IN COGNITIVE PROCESSES

Handra, C. M. (2019) · FARMACIA · doi:10.31925/farmacia.2019.2.1 · Cited by 22 · see citing works

Targeting beta-adrenergic receptor pathways in melanoma: how stress modulates oncogenic immunity

Switzer, B., Puzanov, I. J., Gandhi, S., & Repasky, E. A. (2023) · Melanoma Research · doi:10.1097/cmr.0000000000000943 · Cited by 22 · see citing works

Gas phase ultraviolet and infrared spectroscopy on a partial peptide of β 2 -adrenoceptor SIVSF-NH 2 by a laser desorption supersonic jet technique

Ishiuchi, S., Yamada, K., Oba, H., Wako, H., & Fujii, M. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp04196e · Cited by 22 · see citing works

α-1 Adrenergic receptor antagonist doxazosin reverses hepatic stellate cells activation via induction of senescence

Salas, S. S., Arroyave-Ospina, J. C., Zhang, M., Damba, T., Buist‐Homan, M., Muñoz‐Ortega, M. H., Ventura‐Juárez, J., & Moshage, H. J. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111617 · Cited by 22 · see citing works

The role of catecholamines in modulating responses to stress: Sex‐specific patterns, implications, and therapeutic potential for post‐traumatic stress disorder and opiate withdrawal

Ross, J. A., & Bockstaele, E. J. V. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14714 · Cited by 19 · see citing works

β2-Adrenergic receptor activation on donor cells ameliorates acute GvHD

Mohammadpour, H., Sarow, J. L., MacDonald, C. R., Chen, G. L., Qiu, J., Sharma, U. C., Cao, X., Herr, M. M., Hahn, T., Blazar, B. R., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.137788 · Cited by 21 · see citing works

Identification of β-adrenoceptor subtypes in bovine ovarian and myometrial cell membranes

Re, G., Badino, P., Novelli, A., Canese, M. G., & Girardi, C. (1995) · British Veterinary Journal · doi:10.1016/s0007-1935(05)80028-4 · Cited by 21 · see citing works

Sustained chemogenetic activation of locus coeruleus norepinephrine neurons promotes dopaminergic neuron survival in synucleinopathy

Jovanović, P., Wang, Y., Vit, J., Novinbakht, E., Morones, N., Hogg, E. J., Tagliati, M., & Riera, C. E. (2022) · PLoS ONE · doi:10.1371/journal.pone.0263074 · Cited by 21 · see citing works

ADRA2B deletion variant and enhanced cognitive processing of emotional information: A meta-analytical review

Xie, W., Cappiello, M., Meng, M., Rosenthal, R., & Zhang, W. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.05.010 · Cited by 20 · see citing works

Stimulation of the ADRB3 Adrenergic Receptor Induces Relaxation of Human Placental Arteries: Influence of Preeclampsia1

Rouget, C., Barthez, O., Goirand, F., Leroy, M., Breuiller-Fouché, M., Rakotoniaina, Z., Guérard, P., Morcillo, E. J., Advenier, C., Sagot, P., et al. (2005) · Biology of Reproduction · doi:10.1095/biolreprod.105.043695 · Cited by 20 · see citing works

Structure and Function of Alpha-Adrenergic Receptors

Insel, P. A. (1989) · The American Journal of Medicine · doi:10.1016/0002-9343(89)90108-3 · Cited by 34 · see citing works

Structural determinants involved in the activation and regulation of G protein-coupled receptors: lessons from the alpha1-adrenegic receptor subtypes

Cotecchia, S., Stanasila, L., Diviani, D., Björklöf, K., Rossier, O., & Fanelli, F. (2004) · Biology of the Cell · doi:10.1016/j.biolcel.2004.03.009 · Cited by 21 · see citing works

Adrenergic Receptors: Classification, ligand binding and molecular properties

Wikberg, J. E. S. (1982) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1982.tb00405.x · Cited by 30 · see citing works

Adrenergic Receptors

Bylund, D. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00334-0 · Cited by 8 · see citing works

Use of Electron Microscopy in the Detection of Adrenergic Receptors

Aoki, C. J., Rodrigues, S. M., & Kurose, H. (2003) · Humana Press eBooks · doi:10.1385/1-59259-684-3:535 · Cited by 25 · see citing works