Community guidelines for GPCR ligand bias: IUPHAR review 32

Trends in GPCR drug discovery: new agents, targets and indications

Hauser, A. S., Attwood, M. M., Rask‐Andersen, M., Schiöth, H. B., & Gloriam, D. E. I. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.178 · Cited by 2,609 · see citing works

A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor.

Léan, A. D., Stadel, J. M., & Lefkowitz, R. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79672-9 · Cited by 1,619 · see citing works

G Protein-Coupled Receptors as Targets for Approved Drugs: How Many Targets and How Many Drugs?

Sriram, K., & Insel, P. A. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.111062 · Cited by 1,258 · see citing works

Differential signal transduction by five splice variants of the PACAP receptor

Spengler, D., Waeber, C., Pantaloni, C., Holsboer, F., Bockaert, J., Seeburg, P. H., & Journot, L. (1993) · Nature · doi:10.1038/365170a0 · Cited by 1,182 · see citing works

A MODIFICATION OF RECEPTOR THEORY

STEPHENSON, R. P. (1956) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1956.tb00006.x · Cited by 1,161 · see citing works

Functional Selectivity and Classical Concepts of Quantitative Pharmacology

Urban, J. D., Clarke, W. P., von Zastrow, M., Nichols, D. E., Kobilka, B. K., Weinstein, H., Javitch, J. A., Roth, B. L., Christopoulos, A., Sexton, P. M., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.104463 · Cited by 1,119 · see citing works

Operational models of pharmacological agonism

Black, J. W., & Leff, P. (1983) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1983.0093 · Cited by 1,111 · see citing works

Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds

Luttrell, L. M., Roudabush, F. L., Choy, E. W., Miller, W. E., Field, M. E., Pierce, K. L., & Lefkowitz, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041604898 · Cited by 832 · see citing works

Biased signalling: from simple switches to allosteric microprocessors

Smith, J. S., Lefkowitz, R. J., & Rajagopal, S. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.229 · Cited by 746 · see citing works

Signalling bias in new drug discovery: detection, quantification and therapeutic impact

Kenakin, T., & Christopoulos, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3954 · Cited by 741 · see citing works

Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling

Hollinger, S., & Hepler, J. R. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.527 · Cited by 727 · see citing works

Agonist-receptor efficacy II: agonist trafficking of receptor signals

Kenakin, T. (1995) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)89032-x · Cited by 664 · see citing works

Illuminating G-Protein-Coupling Selectivity of GPCRs

Inoue, A., Raimondi, F., Kadji, F. M. N., Singh, G., Kishi, T., Uwamizu, A., Ono, Y., Shinjo, Y., Ishida, S., Arang, N., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.044 · Cited by 634 · see citing works

β-arrestin- but not G protein-mediated signaling by the “decoy” receptor CXCR7

Rajagopal, S., Kim, J., Ahn, S., Craig, S., Lam, C. M., Gerard, N. P., Gerard, C. J., & Lefkowitz, R. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912852107 · Cited by 602 · see citing works

GPCR-G Protein-β-Arrestin Super-Complex Mediates Sustained G Protein Signaling

Thomsen, A. R. B., Plouffe, B., Cahill, T. J., Shukla, A. K., Tarrasch, J. T., Dosey, A. M., Kahsai, A. W., Strachan, R. T., Pani, B., Mahoney, J. P., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.004 · Cited by 563 · see citing works

How Ligands Illuminate GPCR Molecular Pharmacology

Wacker, D., Stevens, R. C., & Roth, B. L. (2017) · Cell · doi:10.1016/j.cell.2017.07.009 · Cited by 560 · cited 1× · see citing works

“TRUPATH, an Open-Source Biosensor Platform for Interrogating the GPCR Transducerome”

Olsen, R., DiBerto, J., English, J., Glaudin, A. M., Krumm, B., Slocum, S. T., Che, T., Gavin, A. C., McCorvy, J., Roth, B., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0535-8 · Cited by 536 · see citing works

β-Arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors

Azzi, M., Charest, P. G., Angers, S., Rousseau, G., Kohout, T. A., Bouvier, M., & Piñeyro, G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1936664100 · Cited by 522 · see citing works

Therapeutic potential of β-arrestin- and G protein-biased agonists

Whalen, E. J., Rajagopal, S., & Lefkowitz, R. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.11.004 · Cited by 513 · see citing works

Heterotrimeric G‐proteins: a short history

Milligan, G., & Kostenis, E. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706405 · Cited by 494 · see citing works

THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: G protein‐coupled receptors

Alexander, S. P. H., Christopoulos, A., Davenport, A. P., Kelly, E., Mathie, A. A., Peters, J. A., Veale, E. L., Armstrong, J. F., Faccenda, E., Harding, S. D., et al. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15538 · Cited by 485 · see citing works

Probing the activation-promoted structural rearrangements in preassembled receptor–G protein complexes

Galès, C., Durm, J. J. J. V., Schaak, S., Pontier, S. M., Percherancier, Y., Audet, M., Paris, H., & Bouvier, M. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1134 · Cited by 461 · 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

The G protein-coupled receptor kinase (GRK) interactome: Role of GRKs in GPCR regulation and signaling

Ribas, C., Penela, P., Murga, C., Salcedo, A., García‐Hoz, C., Jurado-Pueyo, M., Aymerich, I., & Mayor, F. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.019 · Cited by 409 · see citing works

Regulators of G-Protein signalling as new central nervous system drug targets

Neubig, R. R., & Siderovski, D. P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd747 · Cited by 403 · see citing works

Quantifying Ligand Bias at Seven-Transmembrane Receptors

Rajagopal, S., Ahn, S., Rominger, D. H., Gowen-MacDonald, W., Lam, C. M., DeWire, S. M., Violin, J. D., & Lefkowitz, R. J. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.072801 · Cited by 391 · see citing works

THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Enzymes

Alexander, S. P. H., Fabbro, D., Kelly, E., Mathie, A. A., Peters, J. A., Veale, E. L., Armstrong, J. F., Faccenda, E., Harding, S. D., Pawson, A. J., et al. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15542 · Cited by 388 · see citing works

Update on the pharmacology of calcitonin/CGRP family of peptides: IUPHAR Review 25

Hay, D. L., Garelja, M. L., Poyner, D. R., & Walker, C. S. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14075 · Cited by 375 · see citing works

The evasive nature of drug efficacy: implications for drug discovery

Galandrin, S., Oligny-Longpré, G., & Bouvier, M. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.005 · Cited by 364 · see citing works

Allosteric GPCR modulators: taking advantage of permissive receptor pharmacology

Leach, K., Sexton, P. M., & Christopoulos, A. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.004 · Cited by 362 · see citing works

Lack of beta-arrestin signaling in the absence of active G proteins

Grundmann, M., Merten, N., Malfacini, D., Inoue, A., Preis, P., Simon, K., Rüttiger, N., Ziegler, N., Benkel, T., Schmitt, N., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02661-3 · Cited by 361 · see citing works

GPCRdb in 2021: integrating GPCR sequence, structure and function

Kooistra, A. J., Mordalski, S., Pándy-Szekeres, G., Esguerra, M., Mamyrbekov, A., Munk, C., Keserű, G. M., & Gloriam, D. E. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1080 · Cited by 351 · see citing works

Monitoring G protein-coupled receptor and β-arrestin trafficking in live cells using enhanced bystander BRET

Namkung, Y., Gouill, C. L., Lukashova, V., Kobayashi, H., Hogue, M., Khoury, E., Song, M., Bouvier, M., & Laporte, S. A. (2016) · Nature Communications · doi:10.1038/ncomms12178 · Cited by 349 · see citing works

The role of kinetic context in apparent biased agonism at GPCRs

Herenbrink, C. K., Sykes, D. A., Donthamsetti, P., Canals, M., Coudrat, T., Shonberg, J., Scammells, P. J., Capuano, B., Sexton, P. M., Charlton, S. J., et al. (2016) · Nature Communications · doi:10.1038/ncomms10842 · Cited by 336 · see citing works

Differential Desensitization, Receptor Phosphorylation, β-Arrestin Recruitment, and ERK1/2 Activation by the Two Endogenous Ligands for the CC Chemokine Receptor 7

Kohout, T. A., Nicholas, S., Perry, S. J., Reinhart, G. J., Junger, S., & Struthers, R. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402125200 · Cited by 333 · see citing works

An Agonist-Specific Effect of Guanine Nucleotides on Binding to the Beta Adrenergic Receptor

Maguire, M. E., ARSDALE, P. M. V., & Gilman, A. G. (1976) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10769-4 · Cited by 323 · see citing works

Selective Regulation of Gαq/11 by an RGS Domain in the G Protein-coupled Receptor Kinase, GRK2

Carman, C. V., Parent, J., Day, P. W., Pronin, A. N., Sternweis, P. M., Wedegaertner, P., Gilman, A. G., Benovic, J., & Kozasa, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34483 · Cited by 321 · see citing works

Regulation of beta-adrenergic receptors by guanyl-5'-yl imidodiphosphate and other purine nucleotides.

Lefkowitz, R. J., Mullikin, D., & Caron, M. G. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33257-x · Cited by 314 · see citing works

Biased Receptor Signaling in Drug Discovery

Kenakin, T. (2019) · Pharmacological Reviews · doi:10.1124/pr.118.016790 · Cited by 302 · see citing works

Spatial encoding of cyclic AMP signaling specificity by GPCR endocytosis

Tsvetanova, N. G., & von Zastrow, M. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1665 · Cited by 283 · see citing works

THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Introduction and Other Protein Targets

Alexander, S. P. H., Kelly, E., Mathie, A. A., Peters, J. A., Veale, E. L., Armstrong, J. F., Faccenda, E., Harding, S. D., Pawson, A. J., Southan, C., et al. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15537 · Cited by 278 · see citing works

Effector membrane translocation biosensors reveal G protein and βarrestin coupling profiles of 100 therapeutically relevant GPCRs

Avet, C., Mancini, A. D., Breton, B., Gouill, C. L., Hauser, A. S., Normand, C., Kobayashi, H., Gross, F., Hogue, M., Lukasheva, V., et al. (2022) · eLife · doi:10.7554/elife.74101 · Cited by 270 · see citing works

GPCR interacting proteins (GIP)

Bockaert, J., Fagni, L., Dumuis, A., & Marin, P. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.06.004 · Cited by 262 · see citing works

Distinct profiles of functional discrimination among G proteins determine the actions of G protein–coupled receptors

Masuho, I., Ostrovskaya, O. I., Kramer, G. M., Jones, C. D., Xie, K., & Martemyanov, K. A. (2015) · Science Signaling · doi:10.1126/scisignal.aab4068 · Cited by 259 · see citing works

Neurokinin 1 receptor signaling in endosomes mediates sustained nociception and is a viable therapeutic target for prolonged pain relief

Jensen, D. D., Lieu, T., Halls, M. L., Veldhuis, N. A., Imlach, W. L., Mai, Q. N., Poole, D. P., Quach, T., Aurelio, L., Conner, J., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal3447 · Cited by 247 · see citing works

Regulation of adrenergic receptor function by phosphorylation. II. Effects of agonist occupancy on phosphorylation of alpha 1- and beta 2-adrenergic receptors by protein kinase C and the cyclic AMP-dependent protein kinase.

Bouvier, M., Leeb-Lundberg, L. M. F., Benovic, J., Caron, M. G., & Lefkowitz, R. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61475-9 · Cited by 236 · see citing works

Retromer terminates the generation of cAMP by internalized PTH receptors

Feinstein, T. N., Wehbi, V. L., Ardura, J. A., Wheeler, D., Ferrandon, S., Gardella, T. J., & Vilardaga, J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.545 · Cited by 236 · see citing works

Functional selectivity of GPCR-directed drug action through location bias

Irannejad, R., Pessino, V., Mika, D., Huang, B., Wedegaertner, P., Conti, M., & von Zastrow, M. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2389 · Cited by 232 · see citing works

Agonist-directed signaling of the serotonin 2A receptor depends on β-arrestin-2 interactions in vivo

Schmid, C. L., Raehal, K. M., & Bohn, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708862105 · Cited by 231 · see citing works

Altered Selectivity of Parathyroid Hormone (PTH) and PTH-Related Protein (PTHrP) for Distinct Conformations of the PTH/PTHrP Receptor

Dean, T., Vilardaga, J., Potts, J. T. J., & Gardella, T. J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0274 · Cited by 227 · see citing works

Differences between natural and recombinant G protein-coupled receptor systems with varying receptor/G protein stoichiometry

Kenakin, T. P. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01136-x · Cited by 226 · see citing works

β-Arrestin drives MAP kinase signalling from clathrin-coated structures after GPCR dissociation

Eichel, K., Jullié, D., & von Zastrow, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3307 · Cited by 224 · see citing works

Catalytic activation of β-arrestin by GPCRs

Eichel, K., Jullié, D., Barsi‐Rhyne, B., Latorraca, N. R., Masureel, M., Sibarita, J., Dror, R. O., & von Zastrow, M. (2018) · Nature · doi:10.1038/s41586-018-0079-1 · Cited by 217 · see citing works

Biased Allosteric Modulators: New Frontiers in GPCR Drug Discovery

Slosky, L. M., Caron, M. G., & Barak, L. S. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.12.005 · Cited by 214 · see citing works

Deciphering biased-agonism complexity reveals a new active AT1 receptor entity

Saulière, A., Bellot, M., Paris, H., Denis, C., Finana, F., Hansen, J. T., Altié, M.-F., Séguélas, M., Pathak, A., Hansen, J. L., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.961 · Cited by 208 · see citing works

Manifold roles of β-arrestins in GPCR signaling elucidated with siRNA and CRISPR/Cas9

Luttrell, L. M., Wang, J., Plouffe, B., Smith, J. S., Yamani, L., Kaur, S., Jean‐Charles, P., Gauthier, C., Lee, M., Pani, B., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aat7650 · Cited by 206 · see citing works

Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles

Hay, D. L., & Pioszak, A. A. (2015) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103120 · Cited by 191 · see citing works

Agonist and Inverse Agonist Actions of β-Blockers at the Human β2-Adrenoceptor Provide Evidence for Agonist-Directed Signaling

Baker, J. G., Hall, I. P., & Hill, S. J. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.6.1357 · Cited by 189 · see citing works

Noncanonical GPCR signaling arising from a PTH receptor–arrestin–Gβγ complex

Wehbi, V. L., Stevenson, H. P., Feinstein, T. N., Calero, G. A., Romero, G. G., & Vilardaga, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205756110 · Cited by 185 · see citing works

G protein-coupled receptor kinases: Past, present and future

Komolov, K. E., & Benovic, J. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.07.004 · Cited by 181 · see citing works

Biased signalling and proteinase‐activated receptors ( PAR s): targeting inflammatory disease

Hollenberg, M. D., Mihara, K., Polley, D., Suen, J. Y., Han, A., Fairlie, D. P., & Ramachandran, R. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12544 · Cited by 177 · see citing works

A kinetic view of GPCR allostery and biased agonism

Lane, J. R., May, L. T., Parton, R. G., Sexton, P. M., & Christopoulos, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2431 · Cited by 166 · see citing works

A Global Map of G Protein Signaling Regulation by RGS Proteins

Masuho, I., Santhanam, B., Muntean, B. S., Skamangas, N. K., Chavali, S., Tesmer, J. J. G., Babu, M. M., & Martemyanov, K. A. (2020) · Cell · doi:10.1016/j.cell.2020.08.052 · Cited by 162 · see citing works

The IUPHAR/BPS guide to PHARMACOLOGY in 2022: curating pharmacology for COVID-19, malaria and antibacterials

Harding, S. D., Armstrong, J. F., Faccenda, E., Southan, C., Alexander, S. P. H., Davenport, A. P., Pawson, A. J., Spedding, M., Davies, J. A., & NC-IUPHAR (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1010 · Cited by 149 · see citing works

Functional selectivity profiling of the angiotensin II type 1 receptor using pathway-wide BRET signaling sensors

Namkung, Y., Gouill, C. L., Kumar, S., Cao, Y., Teixeira, L. B., Lukasheva, V., Giubilaro, J., Simões, S. C., Longpré, J., Devost, D., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aat1631 · Cited by 148 · see citing works

Multiple mechanisms of serotonergic signal transduction

Roth, B. L., & Chuang, D.-M. (1987) · Life Sciences · doi:10.1016/0024-3205(87)90621-7 · Cited by 146 · see citing works

Identification of Novel Functionally Selective κ-Opioid Receptor Scaffolds

White, K. L., Scopton, A. P., Rives, M., Bikbulatov, R. V., Polepally, P. R., Brown, P. J., Kenakin, T., Javitch, J. A., Zjawiony, J. K., & Roth, B. L. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.089649 · Cited by 142 · see citing works

Emerging Functional Divergence of β-Arrestin Isoforms in GPCR Function

Srivastava, A., Gupta, B., Gupta, C., & Shukla, A. K. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.001 · Cited by 135 · see citing works

Mechanism of Phosphorylation-Recognition by Visual Arrestin and the Transition of Arrestin into a High Affinity Binding State

Gurevich, V. V., & Benovic, J. (1997) · Molecular Pharmacology · doi:10.1124/mol.51.1.161 · Cited by 132 · see citing works

The atypical chemokine receptor ACKR3/CXCR7 is a broad-spectrum scavenger for opioid peptides

Meyrath, M., Szpakowska, M., Zeiner, J., Massotte, L., Merz, M. P., Benkel, T., Simon, K., Ohnmacht, J., Turner, J. D., Krüger, R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16664-0 · Cited by 130 · see citing works

Molecular Mechanisms of Go Signaling

Jiang, M., & Bajpayee, N. S. (2009) · Neurosignals · doi:10.1159/000186688 · Cited by 129 · see citing works

Biased signaling by endogenous opioid peptides

Gomes, I., Sierra, S., Lueptow, L. M., Gupta, A., Gouty, S., Margolis, E. B., Cox, B. M., & Devi, L. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000712117 · Cited by 127 · see citing works

Biased ligands at opioid receptors: Current status and future directions

Che, T., Dwivedi‐Agnihotri, H., Shukla, A. K., & Roth, B. L. (2021) · Science Signaling · doi:10.1126/scisignal.aav0320 · Cited by 125 · see citing works

β-Arrestin 2-Dependent Angiotensin II Type 1A Receptor-Mediated Pathway of Chemotaxis

Hunton, D. L., Barnes, W. G., Kim, J., Ren, X.-R., Violin, J. D., Reiter, É., Milligan, G., Patel, D. D., & Lefkowitz, R. J. (2005) · Molecular Pharmacology · doi:10.1124/mol.104.006270 · Cited by 123 · see citing works

Theoretical effects of single and multiple transducer receptor coupling proteins on estimates of the relative potency of agonists.

Kenakin, T., & Morgan, P. H. (1989) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10934-6 · Cited by 121 · see citing works

Noncanonical scaffolding of G αi and β-arrestin by G protein–coupled receptors

Smith, J. S., Pack, T. F., Inoue, A., Lee, C. Y., Zheng, K., Choi, I., Eiger, D. S., Warman, A., Xiong, X., Ma, Z., et al. (2021) · Science · doi:10.1126/science.aay1833 · Cited by 117 · see citing works

G Protein-coupled Receptor Kinase GRK2 Is a Phospholipid-dependent Enzyme That Can Be Conditionally Activated by G Protein βγ Subunits

DebBurman, S. K., Ptasienski, J. A., Benovic, J., & Hosey, M. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22552 · Cited by 112 · see citing works

Monitoring G Protein Activation in Cells with BRET

Masuho, I., Martemyanov, K. A., & Lambert, N. A. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2914-6_8 · Cited by 107 · see citing works

Intrinsic bias at non-canonical, β-arrestin-coupled seven transmembrane receptors

Pandey, S., Kumari, P., Baidya, M., Kise, R., Cao, Y., Dwivedi‐Agnihotri, H., Banerjee, R., Li, X. X., Cui, C. S., Lee, J. D., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.007 · Cited by 105 · see citing works

On the analysis of ligand-directed signaling at G protein-coupled receptors

Ehlert, F. J. (2008) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-008-0260-4 · Cited by 94 · see citing works

Agonist-induced modulation of inverse agonist efficacy at the beta 2-adrenergic receptor.

Chidiac, P., Nouet, S., & Bouvier, M. (1996) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09338-1 · Cited by 93 · see citing works

Gz signaling: emerging divergence from Gi signaling

Ho, M. K. C., & Wong, Y. H. (2001) · Oncogene · doi:10.1038/sj.onc.1204190 · Cited by 91 · see citing works

α2A-Adrenergic Receptor Stimulated Calcium Release Is Transduced by Gi-Associated Gβγ-Mediated Activation of Phospholipase C

Dorn, G. W., Oswald, K. J., McCluskey, T. S., Kuhel, D. G., & Liggett, S. B. (1997) · Biochemistry · doi:10.1021/bi970080s · Cited by 87 · see citing works

THE AFFINITY AND EFFICACY OF ONIUM SALTS ON THE FROG RECTUS ABDOMINIS

Barlow, R. B., Scott, N. C., & STEPHENSON, R. P. (1967) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1967.tb01989.x · Cited by 86 · see citing works

Diversity of the Gβγ complexes defines spatial and temporal bias of GPCR signaling

Masuho, I., Skamangas, N. K., Muntean, B. S., & Martemyanov, K. A. (2021) · Cell Systems · doi:10.1016/j.cels.2021.02.001 · Cited by 86 · see citing works

Compartmentalized GPCR Signaling from Intracellular Membranes

Crilly, S. E., & Puthenveedu, M. A. (2020) · The Journal of Membrane Biology · doi:10.1007/s00232-020-00158-7 · Cited by 85 · see citing works

ERK Activation Pathways Downstream of GPCRs

Jain, R., Waturuocha, U. W., Vasudevan, L., & Saini, D. K. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.02.003 · Cited by 83 · see citing works

A Novel Method for Analyzing Extremely Biased Agonism at G Protein–Coupled Receptors

Stahl, E. L., Zhou, L., Ehlert, F. J., & Bohn, L. (2015) · Molecular Pharmacology · doi:10.1124/mol.114.096503 · Cited by 79 · see citing works

The G protein database, GproteinDb

Pándy‐Szekeres, G., Esguerra, M., Hauser, A. S., Caroli, J., Munk, C., Pilger, S., Keserű, G. M., Kooistra, A. J., & Gloriam, D. E. I. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab852 · Cited by 79 · see citing works

Stimulus-dependent Phosphorylation of G-protein-coupled Receptors by Casein Kinase 1α

Tobin, A. B., Totty, N. F., Sterlin, A. E., & Nahorski, S. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20844 · Cited by 76 · see citing works

Allosteric coupling and biased agonism in G protein‐coupled receptors

Böck, A., & Bermúdez, M. (2021) · FEBS Journal · doi:10.1111/febs.15783 · Cited by 76 · see citing works

Ligand functional selectivity and quantitative pharmacology at G protein-coupled receptors

Stallaert, W., Christopoulos, A., & Bouvier, M. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.586691 · Cited by 72 · see citing works

Systematic errors in detecting biased agonism: Analysis of current methods and development of a new model-free approach

Onaran, H. O., Ambrosio, C., Uğur, Ö., Koncz, E. M., Grò, M. C., Vezzi, V., Rajagopal, S., & Costa, T. (2017) · Scientific Reports · doi:10.1038/srep44247 · Cited by 71 · see citing works

The Effective Application of Biased Signaling to New Drug Discovery

Kenakin, T. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.099770 · Cited by 70 · see citing works

Ligand bias in receptor tyrosine kinase signaling

Karl, K., Paul, M. D., Pasquale, E. B., & Hristova, K. A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.015190 · Cited by 66 · see citing works

Conformational Sensors and Domain Swapping Reveal Structural and Functional Differences between β-Arrestin Isoforms

Ghosh, E., Dwivedi‐Agnihotri, H., Baidya, M., Srivastava, A., Kumari, P., Stępniewski, T. M., Kim, H. R., Lee, M., van Gastel, J., Chaturvedi, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.053 · Cited by 64 · see citing works

Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase

Jensen, S. B., Thodberg, S., Parween, S., Moses, M. E., Hansen, C. C., Thomsen, J., Sletfjerding, M. B., Knudsen, C., Del Giudice, R., Lund, P. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22562-w · Cited by 64 · see citing works

Rapid Desensitization of the Serotonin2C Receptor System: Effector Pathway and Agonist Dependence

Stout, B. D., Clarke, W. P., & Berg, K. A. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.302.3.957 · Cited by 61 · see citing works

GPCR-Interacting Proteins, Major Players of GPCR Function

Maurice, P., Guillaume, J., Benleulmi‐Chaachoua, A., Daulat, A. M., Kamal, M. T., & Jockers, R. (2011) · Advances in pharmacology · doi:10.1016/b978-0-12-385952-5.00001-4 · Cited by 58 · see citing works

Comprehensive analysis of heterotrimeric G-protein complex diversity and their interactions with GPCRs in solution

Hillenbrand, M., Schori, C., Schöppe, J., & Plückthun, A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417573112 · Cited by 55 · see citing works

Arrestins as rheostats of GPCR signalling

Gutkind, J. S., & Kostenis, E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0041-y · Cited by 55 · see citing works

Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ

Heidari, Z., Chrisman, I. M., Nemetchek, M. D., Novick, S. J., Blayo, A., Patton, T. M., Mendes, D. E., Diaz, P., Kamenecka, T. M., Griffin, P. R., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13768-0 · Cited by 50 · see citing works

Translating in vitro ligand bias into in vivo efficacy

Luttrell, L. M., Maudsley, S. R., & Gesty‐Palmer, D. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.05.002 · Cited by 47 · see citing works

SnapShot: β-Arrestin Functions

Ahn, S., Shenoy, S. K., Luttrell, L. M., & Lefkowitz, R. J. (2020) · Cell · doi:10.1016/j.cell.2020.07.034 · Cited by 47 · see citing works

Arrestin-mediated signaling: Is there a controversy?

Gurevich, V. V., & Gurevich, E. V. (2018) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v9.i3.25 · Cited by 45 · see citing works

Illuminating the complexity of GPCR pathway selectivity – advances in biosensor development

Wright, S. C., & Bouvier, M. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.04.006 · Cited by 43 · see citing works

Kinetic operational models of agonism for G-protein-coupled receptors

Hoare, S. R. J., Pierre, N., Moya, A. G., & Larson, B. (2018) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2018.02.014 · Cited by 35 · see citing works

Signal profiling of the β1AR reveals coupling to novel signalling pathways and distinct phenotypic responses mediated by β1AR and β2AR

Lukasheva, V., Devost, D., Gouill, C. L., Namkung, Y., Martin, R., Longpré, J., Amraei, M. G., Shinjo, Y., Hogue, M., Lagacé, M., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-65636-3 · Cited by 35 · see citing works

Functional Selectivity and Partial Efficacy at the Monoamine Transporters: A Unified Model of Allosteric Modulation and Amphetamine-Induced Substrate Release

Hasenhuetl, P. S., Bhat, S., Freissmuth, M., & Sandtner, W. (2018) · Molecular Pharmacology · doi:10.1124/mol.118.114793 · Cited by 33 · see citing works

Design of Next-Generation G Protein–Coupled Receptor Drugs: Linking Novel Pharmacology and In Vivo Animal Models

Bradley, S. J., & Tobin, A. B. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140012 · Cited by 30 · see citing works

Analysis of Agonism and Inverse Agonism in Functional Assays with Constitutive Activity: Estimation of Orthosteric Ligand Affinity Constants for Active and Inactive Receptor States

Ehlert, F. J., Suga, H., & Griffin, M. T. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.179309 · Cited by 29 · see citing works

GPCR-dependent biasing of GIRK channel signaling dynamics by RGS6 in mouse sinoatrial nodal cells

Anderson, A., Masuho, I., de Velasco, E. M. F., Nakano, A., Birnbaumer, L., Martemyanov, K. A., & Wickman, K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001270117 · Cited by 25 · see citing works

Seeking ligand bias: assessing GPCR coupling to β-arrestins for drug discovery

Bohn, L., & McDonald, P. H. (2010) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2010.06.005 · Cited by 24 · see citing works

Cannabinoid Receptor Interacting Protein 1a (CRIP1a) in Health and Disease

Oliver, E. E., Hughes, E. K., Puckett, M., Chen, R., Lowther, W. T., & Howlett, A. C. (2020) · Biomolecules · doi:10.3390/biom10121609 · Cited by 24 · see citing works

Effector membrane translocation biosensors reveal G protein and βarrestin coupling profiles of 100 therapeutically relevant GPCRsPreprint

Avet, C., Mancini, A. D., Breton, B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.20.052027 · Cited by 24 · see citing works

The European Research Network on Signal Transduction (ERNEST): Toward a Multidimensional Holistic Understanding of G Protein-Coupled Receptor Signaling

Sommer, M. E., Selent, J., Carlsson, J., de Graaf, C., Gloriam, D. E. I., Keserű, G. M., Kosloff, M., Mordalski, S., Rizk, A., ROSENKILDE, M. M., et al. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00024 · Cited by 21 · see citing works

Conceptual and experimental issues in biased agonism

Onaran, H. O., & Costa, T. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109955 · Cited by 20 · see citing works

Location and Cell-Type-Specific Bias of Metabotropic Glutamate Receptor, mGlu5, Negative Allosteric Modulators

Jong, Y.-J. I., Harmon, S. K., & O’Malley, K. L. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00415 · Cited by 17 · see citing works

Approaches to Assess Functional Selectivity in GPCRs: Evaluating G Protein Signaling in an Endogenous Environment

Bohn, L., Zhou, L., & Ho, J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2914-6_12 · Cited by 15 · see citing works

The Measurement of Receptor Signaling Bias

Kenakin, T. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2914-6_11 · Cited by 13 · see citing works

Quantitating Ligand Bias Using the Competitive Model of Ligand Activity

Stahl, E. L., Ehlert, F. J., & Bohn, L. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9158-7_15 · Cited by 10 · see citing works

Assays for detecting arrestin interaction with GPCRs

Perry, N. A., Asher, W. B., Pedersen, M. H., & Javitch, J. A. (2021) · Methods in cell biology · doi:10.1016/bs.mcb.2021.06.007 · Cited by 6 · see citing works

GPCR drug discovery: new agents, targets and indications

Lorente, J. S., Sokolov, A. V., Ferguson, G., Schiöth, H. B., Hauser, A. S., & Gloriam, D. E. I. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01139-y · Cited by 274 · see citing works

GPCRdb in 2023: state-specific structure models using AlphaFold2 and new ligand resources

Pándy‐Szekeres, G., Caroli, J., Mamyrbekov, A., Kermani, A. A., Keserű, G. M., Kooistra, A. J., & Gloriam, D. E. I. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1013 · Cited by 205 · see citing works

Identification of 5-HT2A receptor signaling pathways associated with psychedelic potential

Wallach, J. V., Cao, A. B., Calkins, M. M., Heim, A. J., Lanham, J. K., Bonniwell, E. M., Hennessey, J. J., Bock, H. A., Anderson, E. I., Sherwood, A. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-44016-1 · Cited by 187 · see citing works

G Protein-Coupled Receptors: A Century of Research and Discovery

Liu, S., Anderson, P. J., Rajagopal, S., Lefkowitz, R. J., & Rockman, H. A. (2024) · Circulation Research · doi:10.1161/circresaha.124.323067 · Cited by 183 · see citing works

Common coupling map advances GPCR-G protein selectivity

Hauser, A. S., Avet, C., Normand, C., Mancini, A. D., Inoue, A., Bouvier, M., & Gloriam, D. E. I. (2022) · eLife · doi:10.7554/elife.74107 · Cited by 138 · see citing works

Homodimerization of CB2 cannabinoid receptor triggered by a bivalent ligand enhances cellular signaling

Navarro, G., Gómez‐Autet, M., Morales, P., Rebassa, J. B., del Torrent, C. L., Jagerovic, N., Pardo, L., & Franco, R. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107363 · Cited by 115 · see citing works

Biased Agonism: Lessons from Studies of Opioid Receptor Agonists

Kelly, E., Conibear, A. E., & Henderson, G. (2022) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052120-091058 · Cited by 102 · see citing works

Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery

Conflitti, P., Lyman, E. R., Sansom, M. S. P., Hildebrand, P. W., Gutiérrez‐de‐Terán, H., Carloni, P., Ansell, T. B., Yuan, S., Barth, P., Robinson, A. S., et al. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01083-3 · Cited by 97 · see citing works

The molecular pharmacology of glucagon agonists in diabetes and obesity

Novikoff, A., & Müller, T. D. (2023) · Peptides · doi:10.1016/j.peptides.2023.171003 · Cited by 82 · see citing works

5-HT2A receptors: Pharmacology and functional selectivity

Cummins, B. R., Billac, G. B., Nichols, D. E., & Nichols, C. D. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100059 · Cited by 79 · see citing works

The polypharmacology of psychedelics reveals multiple targets for potential therapeutics

Jain, M. K., Gumpper, R. H., Slocum, S. T., Schmitz, G. P., Madsen, J. S., Tummino, T. A., Suomivuori, C., Huang, X.-P., Shub, L., DiBerto, J. F., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.06.012 · Cited by 66 · see citing works

Conserved class B GPCR activation by a biased intracellular agonist

Zhao, L., Qian, H., Yuan, Q., Gu, Y., He, X., Shan, H., Li, J., Wang, K., Li, Y., Hu, W., et al. (2023) · Nature · doi:10.1038/s41586-023-06467-w · Cited by 64 · see citing works

Allosteric modulation of GPCRs: From structural insights to in silico drug discovery

Persechino, M., Hedderich, J. B., Kolb, P., & Hilger, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108242 · Cited by 55 · see citing works

Mu-Opioid Receptor Selective Superagonists Produce Prolonged Respiratory Depression

Malcolm, N. J., Palkovic, B., Sprague, D. J., Calkins, M. M., Lanham, J. K., Halberstadt, A. L., Stucke, A. G., & McCorvy, J. D. (2023) · iScience · doi:10.1016/j.isci.2023.107121 · Cited by 53 · see citing works

Biased allosteric activation of ketone body receptor HCAR2 suppresses inflammation

Zhao, C. S., Wang, H., Liu, Y., Cheng, L., Wang, B., Tian, X., Fu, H., Wu, C., Li, Z., Shen, C., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.030 · Cited by 52 · see citing works

Elucidating the Interactome of G Protein-Coupled Receptors and Receptor Activity-Modifying Proteins

Kotliar, I. B., Lorenzen, E., Schwenk, J. M., Hay, D. L., & Sakmar, T. P. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000180 · Cited by 46 · see citing works

The formyl peptide receptors FPR1 and FPR2 as targets for inflammatory disorders: recent advances in the development of small-molecule agonists

Yi, X., Tran, E., Odiba, J. O., Qin, C. X., Ritchie, R. H., & Baell, J. B. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115989 · Cited by 45 · see citing works

Key aspects of modern GPCR drug discovery

Addis, P., Bali, U., Baron, F., Campbell, A. P., Harborne, S. P. D., Jagger, L., Milne, G., Pearce, M. J., Rosethorne, E. M., Satchell, R., et al. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.08.007 · Cited by 44 · see citing works

IUPHAR themed review: Opioid efficacy, bias, and selectivity

Ramos‐Gonzalez, N., Paul, B., & Majumdar, S. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106961 · Cited by 43 · see citing works

Fine-tuning GPCR-mediated neuromodulation by biasing signaling through different G protein subunits

Park, J., Luebbers, A., Dao, M. T., Semeano, A. T. S., Nguyen, A. M., Papakonstantinou, M. P., Broselid, S., Yano, H., Martemyanov, K. A., & Garcia‐Marcos, M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.006 · Cited by 39 · see citing works

A community Biased Signaling Atlas

Caroli, J., Mamyrbekov, A., Harpsøe, K., Gardizi, S., Dörries, L., Ghosh, E., Hauser, A. S., Kooistra, A. J., & Gloriam, D. E. I. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01292-8 · Cited by 38 · see citing works

GproteinDb in 2024: new G protein-GPCR couplings, AlphaFold2-multimer models and interface interactions

Pándy‐Szekeres, G., Herrera, L. P. T., Caroli, J., Kermani, A. A., Kulkarni, Y., Keserű, G. M., & Gloriam, D. E. I. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1089 · Cited by 36 · see citing works

G protein-specific mechanisms in the serotonin 5-HT2A receptor regulate psychosis-related effects and memory deficits

Kossatz, E., Dı́ez-Alarcia, R., Gaitonde, S. A., Ramon‐Duaso, C., Stępniewski, T. M., Aranda-García, D., Arrate, I. M., Blondel-Tepaz, É., Saen‐oon, S., Soliva, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48196-2 · Cited by 39 · see citing works

Ligand-induced conformational changes in the β1-adrenergic receptor revealed by hydrogen-deuterium exchange mass spectrometry

Toporowska, J., Kapoor, P., Musgaard, M., Gherbi, K., Sengmany, K., Qu, F., Soave, M., Yen, H., Hansen, K., Jazayeri, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53161-0 · Cited by 36 · see citing works

Design, Synthesis, and Biological Activity of New CB2 Receptor Ligands: from Orthosteric and Allosteric Modulators to Dualsteric/Bitopic Ligands

Gado, F., Ferrisi, R., Polini, B., Mohamed, K. A., Ricardi, C., Lucarini, E., Carpi, S., Domenichini, F., Stevenson, L., Rapposelli, S., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00582 · Cited by 35 · see citing works

Highly biased agonism for GPCR ligands via nanobody tethering

Sachdev, S., Creemer, B. A., Gardella, T. J., & Cheloha, R. W. (2024) · Nature Communications · doi:10.1038/s41467-024-49068-5 · Cited by 32 · see citing works

Structure-based identification of a G protein–biased allosteric modulator of cannabinoid receptor CB1

Shen, S., Wu, C., Lin, G., Yang, X., Zhou, Y., Zhao, C. S., Miao, Z., Tian, X., Wang, K., Yang, Z., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321532121 · Cited by 34 · see citing works

A structural mechanism of nuclear receptor biased agonism

Nemetchek, M. D., Chrisman, I. M., Rayl, M. L., Voss, A. H., & Hughes, T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2215333119 · Cited by 36 · see citing works

GRK specificity and Gβγ dependency determines the potential of a GPCR for arrestin-biased agonism

Matthees, E. S. F., Filor, J. C., Jaiswal, N., Reichel, M., Youssef, N., D’Uonnolo, G., Szpakowska, M., Drube, J., König, G. M., Kostenis, E., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06490-1 · Cited by 31 · see citing works

Pharmacologically targeting intracellular allosteric sites of GPCRs for drug discovery

Zhang, M., Lan, X., Li, X., & Lu, S. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103803 · Cited by 29 · see citing works

Carfentanil is a β‐arrestin‐biased agonist at the μ opioid receptor

Ramos‐Gonzalez, N., Groom, S., Sutcliffe, K. J., Bancroft, S., Bailey, C. P., Sessions, R. B., Henderson, G., & Kelly, E. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16084 · Cited by 27 · see citing works

Visible‐Light Photoswitchable Benzimidazole Azo‐Arenes as β‐Arrestin2‐Biased Selective Cannabinoid 2 Receptor Agonists

Steinmüller, S. A. M., Fender, J., Deventer, M. H., Tutov, A., Lorenz, K., Stove, C. P., Hislop, J. N., & Decker, M. W. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202306176 · Cited by 30 · see citing works

Structure–Activity Assessment and In-Depth Analysis of Biased Agonism in a Set of Phenylalkylamine 5-HT2A Receptor Agonists

Pottie, E., Poulie, C. B. M., Simon, Í. A., Harpsøe, K., D’Andrea, L., Komarov, I. V., Gloriam, D. E. I., Jensen, A. A., Kristensen, J. L., & Stove, C. P. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00267 · Cited by 27 · see citing works

GPCR signaling bias: an emerging framework for opioid drug development

Kise, R., & Inoue, A. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae013 · Cited by 28 · see citing works

Towards the convergent therapeutic potential of G protein‐coupled receptors in autism spectrum disorders

Annamneedi, A., Gora, C., Dudas, A., Leray, X., Bozon, V., Crépieux, P., & Pellissier, L. P. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16216 · Cited by 29 · see citing works

Ligand selectivity hotspots in serotonin GPCRs

Simon, Í. A., Bjørn-Yoshimoto, W. E., Harpsøe, K., Iliadis, S., Svensson, B. R., Jensen, A. A., & Gloriam, D. E. I. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.09.012 · Cited by 26 · see citing works

Non-canonical G protein signaling

Nürnberg, B., Beer‐Hammer, S., Reisinger, E., & Leiss, V. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108589 · Cited by 29 · see citing works

The path to the G protein‐coupled receptor structural landscape: Major milestones and future directions

Kogut, M. M., Zara, Z., Nicoli, A., Steuer, A., Lopez‐Balastegui, M., Selent, J., Karanth, S., Koehler, M., Ciancetta, A., Abiko, L. A., et al. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17314 · Cited by 27 · see citing works

Structural basis of THC analog activity at the Cannabinoid 1 receptor

Thorsen, T. S., Kulkarni, Y., Sykes, D. A., Bøggild, A., Drace, T., Hompluem, P., Iliopoulos‐Tsoutsouvas, C., Nikas, S. P., Daver, H., Makriyannis, A., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55808-4 · Cited by 24 · see citing works

Designing allosteric modulators to change GPCR G protein subtype selectivity

Moore, M. N., Person, K. L., Robleto, V. L., Alwin, A. R., Krusemark, C. L., Foster, N., Ray, C., Inoue, A., Jackson, M. R., Sheedlo, M. J., et al. (2025) · Nature · doi:10.1038/s41586-025-09643-2 · Cited by 24 · see citing works

Proinflammatory chemokine CXCL14 activates MAS-related G protein-coupled receptor MRGPRX2 and its putative mouse ortholog MRGPRB2

Hamwi, G. A., Namasivayam, V., Bueschbell, B., Gedschold, R., Gölz, S., & Müller, C. E. (2024) · Communications Biology · doi:10.1038/s42003-023-05739-5 · Cited by 24 · see citing works

Variation in responses to incretin therapy: Modifiable and non-modifiable factors

Austin, G. O., & Tomás, A. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1170181 · Cited by 23 · see citing works

Functional consequences of spatial, temporal and ligand bias of G protein-coupled receptors

Tóth, A. D., Turu, G., & Hunyady, L. (2024) · Nature Reviews Nephrology · doi:10.1038/s41581-024-00869-3 · Cited by 21 · see citing works

Specific pharmacological and Gi/o protein responses of some native GPCRs in neurons

Xu, C., Zhou, Y., Liu, Y., Li, L., Liu, P., Wang, X., Xu, Z., Pin, J., Rondard, P., & Liu, J. (2024) · Nature Communications · doi:10.1038/s41467-024-46177-z · Cited by 21 · see citing works

Targeting cryptic allosteric sites of G protein-coupled receptors as a novel strategy for biased drug discovery

Qiao, X., Li, X., Zhang, M., Liu, N., Wu, Y., Lu, S., & Chen, T. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2024.107574 · Cited by 21 · see citing works

Slow dissociation kinetics of fentanyls and nitazenes correlates with reduced sensitivity to naloxone reversal at the μ‐opioid receptor

Alhosan, N., Cavallo, D., Santiago, M., Kelly, E., & Henderson, G. (2025) · British Journal of Pharmacology · doi:10.1111/bph.17376 · Cited by 23 · see citing works

Systematic assessment of chemokine ligand bias at the human chemokine receptor CXCR2 indicates G protein bias over β-arrestin recruitment and receptor internalization

Boon, K., Vanalken, N., Szpakowska, M., Chevigné, A., Schols, D., & Loy, T. V. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01460-2 · Cited by 20 · see citing works

Progress on the development of Class A GPCR‐biased ligands

Morales, P., Scharf, M. M., Bermúdez, M., Egyed, A., Franco, R., Hansen, O. K., Jagerovic, N., Jakubík, J., Keserű, G. M., Kiss, D. J., et al. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17301 · Cited by 20 · see citing works

OpenMMDL - Simplifying the Complex: Building, Simulating, and Analyzing Protein–Ligand Systems in OpenMM

Talagayev, V., Chen, Y., Doering, N. P., Obendorf, L., Denzinger, K., Puls, K., Lam, K., Liu, S., Wolf, C. A., Noonan, T., et al. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c02158 · Cited by 20 · see citing works

Bias translation: The final frontier?

Kenakin, T. (2024) · British Journal of Pharmacology · doi:10.1111/bph.16335 · Cited by 19 · see citing works

Quantification of ligand and mutation-induced bias in EGFR phosphorylation in direct response to ligand binding

Wirth, D., Özdemir, E., & Hristova, K. A. (2023) · Nature Communications · doi:10.1038/s41467-023-42926-8 · Cited by 18 · see citing works

Investigating selectivity and bias for G protein subtypes and β-arrestins by synthetic cannabinoid receptor agonists at the cannabinoid CB1 receptor

Ehrlich, B., Patel, M., Sparkes, E., Banister, S. D., Finlay, D. B., & Glass, M. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116052 · Cited by 18 · see citing works

Ligand-Induced Biased Activation of GPCRs: Recent Advances and New Directions from In Silico Approaches

Hashem, S., Dougha, A., & Tufféry, P. (2025) · Molecules · doi:10.3390/molecules30051047 · Cited by 18 · see citing works

Elucidating the harm potential of brorphine analogues as new synthetic opioids: Synthesis, in vitro, and in vivo characterization

Vandeputte, M. M., Bilel, S., Tirri, M., Corli, G., Bassi, M., Layle, N. K., Fantinati, A., Walther, D., Iula, D. M., Baumann, M. H., et al. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.110113 · Cited by 19 · see citing works

Biased GPCR Signaling: Possible Mechanisms and Therapeutic Applications

Fan, L., & Wang, S. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00827 · Cited by 17 · see citing works

Quantification of signal amplification for receptors: the Kd/EC50 ratio of full agonists as a gain parameter

Buchwald, P. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1541872 · Cited by 16 · see citing works

Evidence that 5‐HT 2A receptor signalling efficacy and not biased agonism differentiates serotonergic psychedelic from non‐psychedelic drugs

Ippolito, A., Vasudevan, S. R., Hurley, S., Gilmour, G., Westhorpe, F. G., Churchill, G. C., & Sharp, T. (2025) · British Journal of Pharmacology · doi:10.1111/bph.70109 · Cited by 17 · see citing works

Virtual library docking for cannabinoid-1 receptor agonists with reduced side effects

Tummino, T. A., Iliopoulos‐Tsoutsouvas, C., Braz, J. M., O’Brien, E. S., Stein, R. M., Craik, V., Tran, N. K., Ganapathy, S., Liu, F., Shiimura, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57136-7 · Cited by 25 · see citing works

Discovery and Development of First-in-Class ACKR3/CXCR7 Superagonists for Platelet Degranulation Modulation

Bayrak, A., Mohr, F., Kolb, K., Szpakowska, M., Shevchenko, E., Dicenta, V., Rohlfing, A., Kudolo, M., Pantsar, T., Günther, M., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01198 · Cited by 13 · see citing works

G protein–coupled receptor endocytosis generates spatiotemporal bias in β-arrestin signaling

Tóth, A. D., Szalai, B., Kovács, O. T., Garger, D., Prokop, S., Soltész‐Katona, E., Balla, A., Inoue, A., Várnai, P., Turu, G., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adi0934 · Cited by 15 · see citing works

Quantitative and Qualitative Differences in the Activation of a Fibroblast Growth Factor Receptor by Different FGF Ligands

Krzyścik, M., Karl, K., Dudeja, P., Krejci, P., & Hristova, K. (2024) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2024.07.002 · Cited by 14 · see citing works

Selective Signal Capture from Multidimensional GPCR Outputs with Biased Agonists: Progress Towards Novel Drug Development

Kim, D., Tokmakova, A., Woo, J. A., An, S. S., Goddard, W. A., & Liggett, S. B. (2022) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-022-00592-4 · Cited by 14 · see citing works

Membrane Heteroreceptor Complexes as Second-Order Protein Modulators: A Novel Integrative Mechanism through Allosteric Receptor–Receptor Interactions

Mirchandani‐Duque, M., Choucri, M., Hernández-Mondragón, J. C., Crespo‐Ramírez, M., Pérez-Olives, C., Ferraro, L., Franco, R., de la Mora, M. P., Fuxé, K., & Borroto‐Escuela, D. O. (2024) · Membranes · doi:10.3390/membranes14050096 · Cited by 14 · see citing works

Fish-hunting cone snail disrupts prey’s glucose homeostasis with weaponized mimetics of somatostatin and insulin

Yeung, H. Y., Ramiro, I. B. L., Andersen, D. B., Koch, T. L., Hamilton, A., Bjørn-Yoshimoto, W. E., Espino, S. S., Vakhrushev, S. Y., Pedersen, K. B., de Haan, N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50470-2 · Cited by 13 · see citing works

Taste GPCRs and their ligands

Dubovski, N., Fierro, F., Margulis, E., Shoshan-Galeczki, Y. B., Peri, L., & Niv, M. Y. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.06.008 · Cited by 12 · see citing works

A Balancing Act: Learning from the Past to Build a Future-Focused Opioid Strategy

Gooding, S. W., & Whistler, J. L. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-042022-015914 · Cited by 12 · see citing works

Content analysis of Reddit posts about coadministration of selective serotonin reuptake inhibitors and psilocybin mushrooms

Sakai, K., Bradley, E., Zamaria, J. A., Agin-Liebes, G., Kelley, D. P., Fish, A., Martini, V., Ferris, M. C., Morton, E. E., Michalak, E. E., et al. (2024) · Psychopharmacology · doi:10.1007/s00213-024-06585-x · Cited by 13 · see citing works

G protein-coupled receptor (GPCR) pharmacogenomics

Thompson, M. D., Reiner‐Link, D., Berghella, A., Rana, B. K., Rovati, G. E., Capra, V., Gorvin, C. M., & Hauser, A. S. (2024) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2024.2358304 · Cited by 12 · see citing works

Molecular Characterization and Pharmacology of Melatonin Receptors in Animals

Cecon, E., Boutin, J. A., & Jockers, R. (2023) · Receptors · doi:10.3390/receptors2020008 · Cited by 12 · see citing works

Non-equilibrium snapshots of ligand efficacy at the μ-opioid receptor

Robertson, M. J., Modak, A., Papasergi-Scott, M. M., Hu, M., Peroto, M. C., Varga, B. R., Majumdar, S., Kalathur, R., Blanchard, S. C., & Skiniotis, G. (2025) · Nature · doi:10.1038/s41586-025-10056-4 · Cited by 11 · see citing works

Identification of 5-HT 2A Receptor Signaling Pathways Responsible for Psychedelic PotentialPreprint

Wallach, J. V., Cao, A. B., Calkins, M. M., Heim, A. J., Lanham, J. K., Bonniwell, E. M., Hennessey, J. J., Bock, H. A., Anderson, E. I., Sherwood, A. M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.29.551106 · Cited by 11 · see citing works

Mind the Gap—Deciphering GPCR Pharmacology Using 3D Pharmacophores and Artificial Intelligence

(2022) · doi:10.3390/ph15111304 · Cited by 15 · see citing works

Comparative analysis of formyl peptide receptor 1 and formyl peptide receptor 2 reveals shared and preserved signalling profiles

Pajonczyk, D., Sternschulte, M. F., Soehnlein, O., Bermúdez, M., Raabe, C. A., & Rescher, U. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17334 · Cited by 11 · see citing works

Label-free biosensor assay decodes the dynamics of Toll-like receptor signaling

Holze, J., Lauber, F., Soler, S., Kostenis, E., & Weindl, G. (2024) · Nature Communications · doi:10.1038/s41467-024-53770-9 · Cited by 10 · see citing works

Exploring Bias in GPCR Signaling and its Implication in Drug Development: A One-Sided Affair

Borah, M. P., Trakroo, D., Soni, N., Kumari, P., & Baidya, M. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00676 · Cited by 10 · see citing works

Quantification of receptor binding from response data obtained at different receptor levels: a simple individual sigmoid fitting and a unified SABRE approach

Buchwald, P. (2022) · Scientific Reports · doi:10.1038/s41598-022-23588-w · Cited by 10 · see citing works

Exploiting Cell-Based Assays to Accelerate Drug Development for G Protein-Coupled Receptors

Wu, Y., Jensen, N., Rossner, M. J., & Wehr, M. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105474 · Cited by 10 · see citing works

Biased signaling in drug discovery and precision medicine

Ji, R., & Tao, Y. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108804 · Cited by 9 · see citing works

The ABCs of psychedelics: a preclinical roadmap for drug discovery

Kwan, A. C., Mantsch, J. R., & McCorvy, J. D. (2025) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2025.07.017 · Cited by 9 · see citing works

Structural basis of PTH1R–β-arrestin core engagement reveals design principles for G-protein-biased therapeutics

Zhao, L., He, Q., Yuan, Q., Zhang, M., Zhao, G.-G., Sun, J., Hu, W., Shan, H., & Xu, H. E. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01806-7 · Cited by 10 · see citing works

Pharmacology of Kappa Opioid Receptors: Novel Assays and Ligands

Sturaro, C., Malfacini, D., Argentieri, M., Djeujo, F. M., Marzola, E., Albanese, V., Ruzza, C., Guerrini, R., Calò, G., & Molinari, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.873082 · Cited by 9 · see citing works

Large library docking for cannabinoid-1 receptor agonists with reduced side effectsPreprint

Tummino, T. A., Iliopoulos‐Tsoutsouvas, C., Bráz, J. M., O’Brien, E. S., Stein, R. M., Craik, V., Tran, N. K., Ganapathy, S., Liu, F., Shiimura, Y., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.27.530254 · Cited by 9 · see citing works

Linkers in Bitopic Agonists Shape Bias Profile among Transducers for the Dopamine D2 and D3 Receptors

Semeano, A. T. S., Garland, R., Bonifazi, A., Lee, K. H., Famiglietti, J., Zhang, W., Jo, Y. J., Battiti, F. O., Shi, L., Newman, A. H., et al. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00119 · Cited by 8 · see citing works

Biased Allosteric Modulation in GPCR Drug Discovery

Zhou, J.-C., Li, M., Long, A., & Kahsai, A. W. (2025) · Handbook of experimental pharmacology · doi:10.1007/164_2025_771 · Cited by 8 · see citing works

Agonists of the Nuclear Receptor PPARγ Can Produce Biased Signaling

Rayl, M. L., Nemetchek, M. D., Voss, A. H., & Hughes, T. (2024) · Molecular Pharmacology · doi:10.1124/molpharm.124.000992 · Cited by 8 · see citing works

Investigation of adenosine A1 receptor-mediated β-arrestin 2 recruitment using a split-luciferase assay

Saecker, L., Häberlein, H., & Franken, S. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1172551 · Cited by 7 · see citing works

Quantitative assessment of ligand bias from bias plots: The bias coefficient “kappa”

Karl, K., Rajagopal, S., & Hristova, K. A. (2023) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2023.130428 · Cited by 7 · see citing works

REGA-SIGN: Development of a Novel Set of NanoBRET-Based G Protein Biosensors

Boon, K., Vanalken, N., Meyen, E., Schols, D., & Loy, T. V. (2023) · Biosensors · doi:10.3390/bios13080767 · Cited by 7 · see citing works

Orphan peptide and G protein‐coupled receptor signalling in alcohol use disorder

Anversa, R. G., Maddern, X. J., Lawrence, A. J., & Walker, L. C. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16301 · Cited by 6 · see citing works

Biased Agonism or “Biaism” for Dummies: A Commentary

Boutin, J. A., & Leprince, J. (2024) · Receptors · doi:10.3390/receptors3010002 · Cited by 7 · see citing works

An increase in the cytosolic concentration of free calcium ions activates the neutrophil NADPH-oxidase provided that the free fatty acid receptor 2 has been allosterically modulated

Lind, S., Wu, Y., Sundqvist, M., Forsman, H. F., & Dahlgren, C. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110687 · Cited by 7 · see citing works

Exploring Structural Determinants of Bias among D4 Subtype-Selective Dopamine Receptor Agonists

Graßl, F., Bock, L. R., González, Á. H.-H., Schiller, M. R., Gmeiner, P., König, J., Fromm, M. F., Hübner, H., & Heinrich, M. R. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00537 · Cited by 7 · see citing works

Development of Melanocortin 4 Receptor Agonists by Exploiting Animal-Derived Macrocyclic, Disulfide-Rich Peptide Scaffolds

Muratspahić, E., Aslanoglou, D., White, A. M., Draxler, C., Kozisek, X., Farooq, Z., Craik, D. J., McCormick, P. J., Durek, T., & Gruber, C. W. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00090 · Cited by 7 · see citing works

Visualizing agonist-induced M2 receptor activation regulated by aromatic ring dynamics

Gong, Z., Zhang, X., Liu, M., Jin, C., & Hu, Y. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2418559122 · Cited by 6 · see citing works

Carfentanil stabilizes µ opioid receptor conformations that are ultra-efficient in inhibiting cAMP, resistant to naloxone or nalmefene but sensitive to naltrexone

Endt, F., Guo, T., Steinritz, D., Amend, N., Gudermann, T. W., & Breit, A. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04048-6 · Cited by 6 · see citing works

Conformational Restriction of Designer Drugs Reveals Subtype-Selective and Biased CB2 Agonists with Neuroprotective Effects

Gioé-Gallo, C., Ortigueira, S., Prieto‐Díaz, R., Contino, M., Azuaje, J., Perrone, M. G., Riganti, C., Alberga, D., Mangiatordi, G. F., Andújar-Arias, A., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00604 · Cited by 6 · see citing works

Serotonin 5-HT2C Receptor Signaling Analysis Reveals Psychedelic Biased Agonism

Bonniwell, E. M., Alabdali, R., Hennessey, J. J., McKee, J. L., Cavalco, N. G., Lammers, J. C., Moore, E. J., Franchini, L., Orlandi, C., & McCorvy, J. D. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00647 · Cited by 6 · see citing works

Kinetic multiplex assay to assess biased signaling of clinical GPCR agonists

Bouma, J., de Koning, E. J. M., van der Horst, C., Kumar, S. S., van den Berg, B. J. W., Hoare, S. R. J., Wittwer, M., Guba, W., Rufer, A. C., Grether, U., et al. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.108021 · Cited by 6 · see citing works

Snapshots of the dynamic basis of NTSR1 G protein subtype promiscuity

Vo, A. V., Modak, A., Lu, S., Blanchard, S. C., Lambert, N. A., & Robertson, M. J. (2026) · Nature · doi:10.1038/s41586-026-10120-7 · Cited by 6 · see citing works

Biased signalling in analgesic research and development

Conibear, A. E., Bailey, C. P., & Kelly, E. (2024) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2024.102465 · Cited by 6 · see citing works

International Union of Basic and Clinical Pharmacology. Guidelines for GPCR ligand biasPreprint

Kolb, P., Kenakin, T., Alexander, S. P. H., Bermúdez, M., Bohn, L., Breinholt, C. S., Bouvier, M., Ehlert, F. J., Hill, S. J., Martemyanov, K. A., et al. (2021) · doi:10.22541/au.163253223.32597426/v1 · Cited by 1 · see citing works

International Union of Basic and Clinical Pharmacology. Recommendations for GPCR ligand biasPreprint

Kolb, P., & Gloriam, D. E. I. (2021) · doi:10.22541/au.163129851.17708337/v1 · Cited by 3 · see citing works

Practical guide for calculating and representing biased signaling by GPCR ligands: A stepwise approach

Nagi, K., & Piñeyro, G. (2015) · Methods · doi:10.1016/j.ymeth.2015.09.010 · Cited by 36 · see citing works

To Be Biased or Not to Be: A Play for G-Protein Coupled Receptors

Liolitsas, N. G., Pantazaka, E., & Papadimitriou, Ε. (2025) · International Journal of Translational Medicine · doi:10.3390/ijtm5040056

Analyzing biased responses of GPCR ligands

Benredjem, B., Dallaire, P., & Piñeyro, G. (2016) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2016.11.008 · Cited by 16 · see citing works