Quantifying Ligand Bias at Seven-Transmembrane Receptors

Regulation of μ-opioid receptors: desensitization, phosphorylation, internalization, and tolerance

Williams, J. T., Ingram, S. L., Henderson, G., Chavkin, C., von Zastrow, M., Schulz, S., Koch, T., Evans, C. J., & Christie, M. J. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.005942 · Cited by 802

A G Protein-Biased Ligand at the μ-Opioid Receptor Is Potently Analgesic with Reduced Gastrointestinal and Respiratory Dysfunction Compared with Morphine

DeWire, S. M., Yamashita, D. S., Rominger, D. H., Liu, G., Cowan, C. L., Graczyk, T. M., Chen, X.-T., Pitis, P. M., Gotchev, D., Yuan, C., et al. (2013) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.201616 · Cited by 647

Low intrinsic efficacy for G protein activation can explain the improved side effect profiles of new opioid agonists

Gillis, A., Gondin, A. B., Kliewer, A., Sanchez, J., Lim, H. D., Alamein, C., Manandhar, P., Santiago, M., Fritzwanker, S., Schmiedel, F., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aaz3140 · Cited by 336

Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

Staus, D. P., Strachan, R. T., Manglik, A., Pani, B., Kahsai, A. W., Kim, T. H., Wingler, L. M., Ahn, S., Chatterjee, A., Masoudi, A., et al. (2016) · Nature · doi:10.1038/nature18636 · Cited by 330

The role of kinetic context in apparent biased agonism at GPCRs

Klein Herenbrink, C., 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 328

The β-Arrestins: Multifunctional Regulators of G Protein-coupled Receptors

Smith, J. S., & Rajagopal, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.713313 · Cited by 294

Human gain-of-function MC4R variants show signaling bias and protect against obesity

Lotta, L. A., Mokrosiński, J., Mendes de Oliveira, E., Li, C., Sharp, S. J., Luan, J., Brouwers, B., Ayinampudi, V., Bowker, N., Kerrison, N., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.044 · Cited by 284

Community guidelines for GPCR ligand bias: IUPHAR review 32

Kolb, P., Kenakin, T., Alexander, S. P. H., Bermudez, M., Bohn, L. M., Breinholt, C. S., Bouvier, M., Hill, S. J., Kostenis, E., Martemyanov, K. A., et al. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15811 · Cited by 232

Molecular Mechanisms Underlying β-Adrenergic Receptor-Mediated Cross-Talk between Sympathetic Neurons and Immune Cells

Lorton, D., & Bellinger, D. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16035635 · Cited by 221

Synthesis, Chemical Characterization, and μ-Opioid Receptor Activity Assessment of the Emerging Group of “Nitazene” 2-Benzylbenzimidazole Synthetic Opioids

Vandeputte, M. M., Van Uytfanghe, K., Layle, N. K., St. Germaine, D. M., Iula, D. M., & Stove, C. P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00064 · Cited by 161

Allostery and biased agonism at class B G protein-coupled receptors

Wootten, D., Miller, L. J., Koole, C., Christopoulos, A., & Sexton, P. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00049 · Cited by 112

Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder-based proteoforms

Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91

Fine Tuning Muscarinic Acetylcholine Receptor Signaling Through Allostery and Bias

van der Westhuizen, E. T., Choy, K. H. C., Valant, C., McKenzie-Nickson, S., Bradley, S. J., Tobin, A. B., Sexton, P. M., & Christopoulos, A. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.606656 · Cited by 63

Intracellular signaling mechanisms of the melanocortin receptors: current state of the art

Rodrigues, A. R., Almeida, H., & Gouveia, A. M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1800-3 · Cited by 64

Assessment of structure-activity relationships and biased agonism at the Mu opioid receptor of novel synthetic opioids using a novel, stable bio-assay platform

Vasudevan, L., Vandeputte, M., Deventer, M., Wouters, E., Cannaert, A., & Stove, C. P. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113910 · Cited by 55

In Vitro Functional Profiling of Fentanyl and Nitazene Analogs at the μ-Opioid Receptor Reveals High Efficacy for Gi Protein Signaling

Tsai, M.-H. M., Chen, L., Baumann, M. H., Canals, M., Javitch, J. A., Lane, J. R., & Shi, L. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00750 · Cited by 27

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

Coevolution-Driven Method for Efficiently Simulating Conformational Changes in Proteins Reveals Molecular Details of Ligand Effects in the β2AR Receptor

Mitrovic, D., Chen, Y., Marciniak, A., & Delemotte, L. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c04897 · Cited by 10