All Outputs (3)

GRKs as Key Modulators of Opioid Receptor Function (2020)
Journal Article
Lemel, L., Lane, J. R., & Canals, M. (2020). GRKs as Key Modulators of Opioid Receptor Function. Cells, 9(11), Article 2400. https://doi.org/10.3390/cells9112400

Understanding the link between agonist-induced phosphorylation of the mu-opioid receptor (MOR) and the associated physiological effects is critical for the development of novel analgesic drugs and is particularly important for understanding the mecha... Read More about GRKs as Key Modulators of Opioid Receptor Function.

Low intrinsic efficacy for G protein activation can explain the improved side-effect profile of new opioid agonists (2020)
Journal Article
Gillis, A., Gondin, A. B., Kliewer, A., Sanchez, J., Lim, H. D., Alamein, C., Manandhar, P., Santiago, M., Fritzwanker, S., Schmidel, F., Katte, T. A., Reekie, T., Grimsey, N. L., Kassiou, M., Kellam, B., Krasel, C., Halls, M. L., Connor, M., Lane, J. R., Schulz, S., …Canals, M. (2020). Low intrinsic efficacy for G protein activation can explain the improved side-effect profile of new opioid agonists. Science Signaling, 13(625), Article eaaz3140. https://doi.org/10.1126/scisignal.aaz3140

Biased agonism at G protein–coupled receptors describes the phenomenon whereby some drugs can activate some downstream signaling activities to the relative exclusion of others. Descriptions of biased agonism focusing on the differential engagement of... Read More about Low intrinsic efficacy for G protein activation can explain the improved side-effect profile of new opioid agonists.

Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism (2020)
Journal Article
Lane, J. R., Abramyan, A. M., Adhikari, P., Keen, A. C., Lee, K.-H., Sanchez, J., Verma, R. K., Lim, H. D., Yano, H., Javitch, J. A., & Shi, L. (2020). Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism. eLife, 9, Article e52189. https://doi.org/10.7554/elife.52189

By analyzing and simulating inactive conformations of the highly-homologous dopamine D2 and D3 receptors (D2R and D3R), we find that eticlopride binds D2R in a pose very similar to that in the D3R/eticlopride structure but incompatible with the D2R/r... Read More about Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism.