The Molecular Basis of G Protein–Coupled Receptor Activation

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637 · 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

The Energy Landscapes and Motions of Proteins

Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250 · see citing works

Crystal structure of the β2 adrenergic receptor–Gs protein complex

Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009 · see citing works

[19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors

Ballesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001 · see citing works

The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints

Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941 · see citing works

Dynamic personalities of proteins

Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545 · see citing works

Crystal structure of the human β2 adrenergic G-protein-coupled receptor

Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935 · see citing works

Structure of a nanobody-stabilized active state of the β2 adrenoceptor

Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,663 · 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

Molecular signatures of G-protein-coupled receptors

Venkatakrishnan, A., Deupí, X., Lebon, G., Tate, C. G., Schertler, G. F. X., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,502 · see citing works

GPCR Engineering Yields High-Resolution Structural Insights into β 2 -Adrenergic Receptor Function

Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Yao, X.-J., Weis, W. I., Stevens, R. C., et al. (2007) · Science · doi:10.1126/science.1150609 · Cited by 1,339 · see citing works

Crystal structure of opsin in its G-protein-interacting conformation

Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059 · see citing works

Structural insights into µ-opioid receptor activation

Huang, W., Manglik, A., Venkatakrishnan, A., Laeremans, T., Feinberg, E. N., Sanborn, A. L., KATO, H. E., Livingston, K. E., Thorsen, T. S., Kling, R. C., et al. (2015) · Nature · doi:10.1038/nature14886 · Cited by 895 · see citing works

Activation and allosteric modulation of a muscarinic acetylcholine receptor

Kruse, A. C., Ring, A. M., Manglik, A., Hu, J., Hu, K., Eitel, K., Hübner, H., Pardon, E., Valant, C., Sexton, P. M., et al. (2013) · Nature · doi:10.1038/nature12735 · Cited by 895 · see citing works

Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation

Lebon, G., Warne, T., Edwards, P. C., Bennett, K. A., Langmead, C. J., Leslie, A. G. W., & Tate, C. G. (2011) · Nature · doi:10.1038/nature10136 · Cited by 877 · see citing works

Structure of an Agonist-Bound Human A 2A Adenosine Receptor

Xu, F., Wu, H., Katritch, V., Han, G. W., Jacobson, K. A., Gao, Z., Cherezov, V., & Stevens, R. C. (2011) · Science · doi:10.1126/science.1202793 · Cited by 816 · see citing works

Structure and dynamics of the M3 muscarinic acetylcholine receptor

Kruse, A. C., Hu, J., Pan, A. C., Arlow, D. H., Rosenbaum, D. M., Rosemond, E., Green, H. F., Liu, T., Chae, P. S., Dror, R. O., et al. (2012) · Nature · doi:10.1038/nature10867 · Cited by 812 · see citing works

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Kang, Y., Zhou, X. E., Gao, X., He, Y., Liu, W., Ishchenko, A., Barty, A., White, T. A., Yefanov, O. M., Han, G. W., et al. (2015) · Nature · doi:10.1038/nature14656 · Cited by 804 · see citing works

The Dynamic Process of β2-Adrenergic Receptor Activation

Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.008 · Cited by 797 · see citing works

Structure and function of an irreversible agonist-β2 adrenoceptor complex

Rosenbaum, D. M., Zhang, C., Lyons, J. A., Holl, R., Aragão, D., Arlow, D. H., Rasmussen, S. G. F., Choi, H., DeVree, B. T., Sunahara, R. K., et al. (2011) · Nature · doi:10.1038/nature09665 · Cited by 767 · see citing works

Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR

Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., & Kurt Wüthrich, A. (2012) · Science · doi:10.1126/science.1215802 · Cited by 697 · see citing works

Allostery and cooperativity revisited

Cui, Q., & Karplus, M. (2008) · Protein Science · doi:10.1110/ps.03259908 · Cited by 680 · see citing works

Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling

Manglik, A., Kim, T. H., Masureel, M., Altenbach, C., Yang, Z., Hilger, D., Lerch, M. T., Kobilka, T. S., Thian, F. S., Hubbell, W. L., et al. (2015) · Cell · doi:10.1016/j.cell.2015.04.043 · Cited by 667 · see citing works

Crystal structure of metarhodopsin II

Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663 · see citing works

Activation mechanism of the β 2 -adrenergic receptor

Dror, R. O., Arlow, D. H., Maragakis, P., Mildorf, T. J., Pan, A. C., Xu, H., Borhani, D. W., & Shaw, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110499108 · Cited by 625 · see citing works

Activation of the β2-Adrenergic Receptor Involves Disruption of an Ionic Lock between the Cytoplasmic Ends of Transmembrane Segments 3 and 6

Ballesteros, J. A., Jensen, A. D., Liapakis, G., Rasmussen, S. G. F., Shi, L., Gether, U., & Javitch, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103747200 · Cited by 619 · see citing works

The structural basis for agonist and partial agonist action on a β1-adrenergic receptor

Warne, T., Moukhametzianov, R., Baker, J. G., Nehmé, R., Edwards, P. C., Leslie, A. G. W., Schertler, G. F. X., & Tate, C. G. (2011) · Nature · doi:10.1038/nature09746 · Cited by 619 · see citing works

Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein

Zhang, Y., Sun, B., Feng, D., Hu, H., Chu, M. L.-H., Qu, Q., Tarrasch, J. T., Li, S., Kobilka, T. S., Kobilka, B. K., et al. (2017) · Nature · doi:10.1038/nature22394 · Cited by 582 · see citing works

Adrenaline-activated structure of β2-adrenoceptor stabilized by an engineered nanobody

Ring, A. M., Manglik, A., Kruse, A. C., Enos, M. D., Weis, W. I., García, K. C., & Kobilka, B. K. (2013) · Nature · doi:10.1038/nature12572 · Cited by 491 · see citing works

The structural basis of agonist-induced activation in constitutively active rhodopsin

Standfuss, J., Edwards, P. C., D’Antona, A. M., Fransen, M. P., Xie, G., Oprian, D. D., & Schertler, G. F. X. (2011) · Nature · doi:10.1038/nature09795 · Cited by 477 · see citing works

Phase-plate cryo-EM structure of a class B GPCR–G-protein complex

Liang, Y.-L., Khoshouei, M., Radjainia, M., Zhang, Y., Glukhova, A., Tarrasch, J. T., Thal, D. M., Furness, S. G. B., Christopoulos, G., Coudrat, T., et al. (2017) · Nature · doi:10.1038/nature22327 · Cited by 464 · see citing works

High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P., & Hubbell, W. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802515105 · Cited by 462 · see citing works

Fusion Partner Toolchest for the Stabilization and Crystallization of G Protein-Coupled Receptors

Chun, E., Thompson, A. A., Liu, W., Roth, C., Griffith, M. T., Katritch, V., Kunken, J., Xu, F., Cherezov, V., Hanson, M. A., et al. (2012) · Structure · doi:10.1016/j.str.2012.04.010 · Cited by 462 · see citing works

Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors

Zhou, X. E., He, Y., de Waal, P. W., Gao, X., Kang, Y., Eps, N. V., Yin, Y., Pal, K., Goswami, D., White, T. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.002 · Cited by 449 · see citing works

Structure of the adenosine A2A receptor bound to an engineered G protein

Carpenter, B., Nehmé, R., Warne, T., Leslie, A. G. W., & Tate, C. G. (2016) · Nature · doi:10.1038/nature18966 · Cited by 438 · see citing works

Coupling ligand structure to specific conformational switches in the β2-adrenoceptor

Yao, X.-J., Parnot, C., Deupí, X., Ratnala, V. R. P., Swaminath, G., Farrens, D., & Kobilka, B. K. (2006) · Nature Chemical Biology · doi:10.1038/nchembio801 · Cited by 353 · see citing works

Activation of the A2A adenosine G-protein-coupled receptor by conformational selection

Ye, L., Eps, N. V., Zimmer, M., Ernst, O. P., & Prosser, R. S. (2016) · Nature · doi:10.1038/nature17668 · Cited by 350 · see citing works

Single-molecule analysis of ligand efficacy in β2AR–G-protein activation

Gregorio, G. G., Masureel, M., Hilger, D., Terry, D. S., Juette, M. F., Zhao, H. C., Zhou, Z., Perez‐Aguilar, J. M., Hauge, M., Mathiasen, S., et al. (2017) · Nature · doi:10.1038/nature22354 · Cited by 348 · see citing works

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 · see citing works

Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure

Faham, S., & Bowie, J. U. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5295 · Cited by 325 · 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

Agonist-induced conformational changes in the G-protein-coupling domain of the β 2 adrenergic receptor

Ghanouni, P., Steenhuis, J. J., Farrens, D., & Kobilka, B. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101126198 · Cited by 311 · see citing works

Allosteric regulation of G protein–coupled receptor activity by phospholipids

Dawaliby, R., Trubbia, C., Delporte, C., Masureel, M., Antwerpen, P. V., Kobilka, B. K., & Govaerts, C. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1960 · Cited by 305 · see citing works

Identification of two distinct inactive conformations of the β 2 -adrenergic receptor reconciles structural and biochemical observations

Dror, R. O., Arlow, D. H., Borhani, D. W., Jensen, M. Ø., Piana, S., & Shaw, D. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811065106 · Cited by 304 · see citing works

Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region

Venkatakrishnan, A., Deupí, X., Lebon, G., Heydenreich, F. M., Flock, T., Miljuš, T., Santhanam, B., Bouvier, M., Veprintsev, D. B., Tate, C. G., et al. (2016) · Nature · doi:10.1038/nature19107 · Cited by 304 · see citing works

Structural Instability of a Constitutively Active G Protein-coupled Receptor

Gether, U., Seifert, R., Ballesteros, J. A., Sanders‐Bush, E., Weinstein, H., & Kobilka, B. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2587 · Cited by 295 · see citing works

Allosteric coupling from G protein to the agonist-binding pocket in GPCRs

DeVree, B. T., Mahoney, J. P., Vélez-Ruiz, G. A., Rasmussen, S. G. F., Kuszak, A. J., Edwald, E., Fung, J. J., Manglik, A., Masureel, M., Du, Y., et al. (2016) · Nature · doi:10.1038/nature18324 · Cited by 290 · see citing works

Structural basis for chemokine recognition and activation of a viral G protein–coupled receptor

Burg, J. S., Ingram, J. R., Venkatakrishnan, A., Jude, K. M., Dukkipati, A., Feinberg, E. N., Angelini, A., Waghray, D., Dror, R. O., Ploegh, H. L., et al. (2015) · Science · doi:10.1126/science.aaa5026 · Cited by 273 · see citing works

Propagation of conformational changes during μ-opioid receptor activation

Sounier, R., Mas, C., Steyaert, J., Laeremans, T., Manglik, A., Huang, W., Kobilka, B. K., Déméné, H., & Granier, S. (2015) · Nature · doi:10.1038/nature14680 · Cited by 259 · see citing works

Nanobodies to Study G Protein–Coupled Receptor Structure and Function

Manglik, A., Kobilka, B. K., & Steyaert, J. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104710 · Cited by 257 · see citing works

Nanobody stabilization of G protein-coupled receptor conformational states

Steyaert, J., & Kobilka, B. K. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.06.011 · Cited by 234 · see citing works

Crystallizing Membrane Proteins for Structure Determination: Use of Lipidic Mesophases

Caffrey, M. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133655 · Cited by 211 · see citing works

Efficacy of the β2-adrenergic receptor is determined by conformational equilibrium in the transmembrane region

Kofuku, Y., Ueda, T., Okude, J., Shiraishi, Y., Kondo, K., Maeda, M., Tsujishita, H., & Shimada, I. (2012) · Nature Communications · doi:10.1038/ncomms2046 · Cited by 196 · see citing works

The Role of Ligands on the Equilibria Between Functional States of a G Protein-Coupled Receptor

Kim, T. H., Chung, K. Y., Manglik, A., Hansen, A. L., Dror, R. O., Mildorf, T. J., Shaw, D. E., Kobilka, B. K., & Prosser, R. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja404305k · Cited by 177 · see citing works

Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor

Isogai, S., Deupí, X., Opitz, C. F., Heydenreich, F. M., Tsai, C., Brueckner, F., Schertler, G. F. X., Veprintsev, D. B., & Grzesiek, S. (2016) · Nature · doi:10.1038/nature16577 · Cited by 177 · see citing works

Two distinct conformations of helix 6 observed in antagonist-bound structures of a β 1 -adrenergic receptor

Moukhametzianov, R., Warne, T., Edwards, P. C., Serrano‐Vega, M. J., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100185108 · Cited by 176 · see citing works

Functional Dynamics of Deuterated β2‐Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy

Kofuku, Y., Ueda, T., Okude, J., Shiraishi, Y., Kondo, K., Mizumura, T., Suzuki, S., & Shimada, I. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201406603 · Cited by 161 · see citing works

Structural and Functional Analysis of a β2-Adrenergic Receptor Complex with GRK5

Komolov, K. E., Du, Y., Duc, N. M., Betz, R. M., Rodrigues, J. P. G. L. M., Leib, R. D., Patra, D., Skiniotis, G., Adams, C. M., Dror, R. O., et al. (2017) · Cell · doi:10.1016/j.cell.2017.03.047 · Cited by 152 · see citing works

Ligand-Dependent Perturbation of the Conformational Ensemble for the GPCR β2 Adrenergic Receptor Revealed by HDX

West, G. M., Chien, E. Y. T., Katritch, V., Gatchalian, J., Chalmers, M. J., Stevens, R. C., & Griffin, P. R. (2011) · Structure · doi:10.1016/j.str.2011.08.001 · Cited by 139 · see citing works

N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor

Zou, Y., Weis, W. I., & Kobilka, B. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046039 · Cited by 131 · see citing works

Multiple conformational selection and induced fit events take place in allosteric propagation

Nussinov, R., Ma, B., & Tsai, C. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.10.002 · Cited by 130 · see citing works

Differences in Allosteric Communication Pipelines in the Inactive and Active States of a GPCR

Bhattacharya, S., & Vaidehi, N. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.015 · Cited by 121 · see citing works

Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β 2 AR

Lamichhane, R., Liu, J. J., Pljevaljčić, G., White, K. L., der Schans, E. J. C. V., Katritch, V., Stevens, R. C., Kurt Wüthrich, A., & Millar, D. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519626112 · Cited by 109 · see citing works

Role of Detergents in Conformational Exchange of a G Protein-coupled Receptor

Chung, K. Y., Kim, T. H., Manglik, A., Alvares, R. D. A., Kobilka, B. K., & Prosser, R. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.406371 · Cited by 104 · see citing works

A mutagenesis and screening strategy to generate optimally thermostabilized membrane proteins for structural studies

Magnani, F., Serrano‐Vega, M. J., Shibata, Y., Abdul-Hussein, S., Lebon, G., Miller-Gallacher, J., Singhal, A., Strege, A., Thomas, J. A., & Tate, C. G. (2016) · Nature Protocols · doi:10.1038/nprot.2016.088 · Cited by 101 · see citing works

Site-directed spin labeling EPR spectroscopy in protein research

Klare, J. P. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0155 · Cited by 100 · see citing works

β2‐Adrenergic Receptor Activation by Agonists Studied with 19F NMR Spectroscopy

Horst, R., Liu, J. J., Stevens, R. C., & Kurt Wüthrich, A. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305286 · Cited by 89 · see citing works

Concerted Interconversion between Ionic Lock Substates of the β2 Adrenergic Receptor Revealed by Microsecond Timescale Molecular Dynamics

Romo, T. D., Grossfield, A. M., & Pitman, M. C. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.09.046 · Cited by 67 · see citing works

β 2 -Adrenergic Receptor Conformational Response to Fusion Protein in the Third Intracellular Loop

Eddy, M. T., Didenko, T., Stevens, R. C., & Kurt Wüthrich, A. (2016) · Structure · doi:10.1016/j.str.2016.09.015 · Cited by 52 · see citing works

The Arginine of the DRY Motif in Transmembrane Segment III Functions as a Balancing Micro-switch in the Activation of the β2-Adrenergic Receptor

Valentin-Hansen, L., Groenen, M., Nygaard, R., Frimurer, T. M., Holliday, N. D., & Schwartz, T. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348565 · Cited by 45 · see citing works

Influence of Lipid Composition on the Structural Stability of G-Protein Coupled Receptor

Mahmood, M. I., Liu, X., Neya, S., & Hoshino, T. (2013) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c12-01059 · Cited by 32 · see citing works

FGF/FGFR signaling in health and disease

Xie, Y., Su, N., Yang, J., Tan, Q., Huang, S., Jin, M., Ni, Z., Zhang, B., Zhang, D., Luo, F., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00222-7 · Cited by 904 · see citing works

G protein-coupled receptors: structure- and function-based drug discovery

Yang, D., Zhou, Q., Labroska, V., Qin, S., Darbalaei, S., Wu, Y., Yuliantie, E., Xie, L., Tao, H., Cheng, J., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00435-w · Cited by 641 · see citing works

Common activation mechanism of class A GPCRs

Zhou, Q., Yang, D., Wu, M., Guo, Y., Guo, W., Li, Z., Cai, X., Dai, A., Jang, W., Shakhnovich, E. I., et al. (2019) · eLife · doi:10.7554/elife.50279 · Cited by 623 · see citing works

G protein-coupled receptors (GPCRs): advances in structures, mechanisms and drug discovery

Zhang, M., Chen, T., Lu, X., Lan, X., Chen, K., & Lu, S. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01803-6 · Cited by 520 · see citing works

Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor

Kim, K., Che, T., Panova, O., DiBerto, J. F., Lyu, J., Krumm, B. E., Wacker, D., Robertson, M. J., Seven, A. B., Nichols, D. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.024 · Cited by 481 · see citing works

Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS)

Drew, D., North, R. A., Nagarathinam, K., & Tanabe, M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00983 · Cited by 471 · see citing works

ProLIF: a library to encode molecular interactions as fingerprints

Bouysset, C., & Fiorucci, S. (2021) · Journal of Cheminformatics · doi:10.1186/s13321-021-00548-6 · Cited by 452 · see citing works

Impact of GPCR Structures on Drug Discovery

Congreve, M., de Graaf, C., Swain, N. A., & Tate, C. G. (2020) · Cell · doi:10.1016/j.cell.2020.03.003 · Cited by 380 · see citing works

Mechanisms of Cryptochrome-Mediated Photoresponses in Plants

Wang, Q., & Lin, C. (2020) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050718-100300 · Cited by 293 · see citing works

Protective Effects of Estrogen on Cardiovascular Disease Mediated by Oxidative Stress

Xiang, D., Liu, Y., Zhou, S.-J., Zhou, E., & Wang, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5523516 · Cited by 262 · see citing works

AlphaFold 2: Why It Works and Its Implications for Understanding the Relationships of Protein Sequence, Structure, and Function

Skolnick, J., Gao, M., Zhou, H., & Singh, S. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01114 · Cited by 251 · see citing works

Peptide-Drug Conjugates and Their Targets in Advanced Cancer Therapies

Hoppenz, P., Els‐Heindl, S., & Beck‐Sickinger, A. G. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00571 · Cited by 248 · see citing works

Molecular mechanism of biased signaling in a prototypical G protein–coupled receptor

Suomivuori, C., Latorraca, N. R., Wingler, L. M., Eismann, S., King, M. C., Kleinhenz, A. L. W., Skiba, M. A., Staus, D. P., Kruse, A. C., Lefkowitz, R. J., et al. (2020) · Science · doi:10.1126/science.aaz0326 · Cited by 243 · see citing works

G-Protein-Coupled Receptors in Astrocyte–Neuron Communication

Kofuji, P., & Araque, A. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.03.025 · Cited by 237 · see citing works

Multi‐state modeling of G‐protein coupled receptors at experimental accuracy

Heo, L., & Feig, M. (2022) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26382 · Cited by 215 · see citing works

Cannabinoids and Cannabinoid Receptors: The Story so Far

Shahbazi, F., Grandi, V., Banerjee, A., & Trant, J. F. (2020) · iScience · doi:10.1016/j.isci.2020.101301 · Cited by 234 · see citing works

Activation pathway of a G protein-coupled receptor uncovers conformational intermediates as targets for allosteric drug design

Lu, S., He, X., Yang, Z., Chai, Z., Zhou, S., Wang, J., Rehman, A. U., Ni, D., Pu, J., Sun, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25020-9 · Cited by 225 · see citing works

Pushing the frontiers: tools for monitoring neurotransmitters and neuromodulators

Wu, Z., Lin, D., & Li, Y. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00577-6 · Cited by 225 · see citing works

Emerging principles of cytokine pharmacology and therapeutics

Saxton, R. A., Glassman, C. R., & García, K. C. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00557-6 · Cited by 223 · see citing works

Novel roles of phosphoinositides in signaling, lipid transport, and disease

Hammond, G. R. V., & Burke, J. E. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.12.007 · Cited by 203 · see citing works

Receptor-associated independent cAMP nanodomains mediate spatiotemporal specificity of GPCR signaling

Anton, S. E., Kayser, C., Maiellaro, I., Nemec, K., Möller, J., Koschinski, A., Zaccolo, M., Annibale, P., Falcke, M., Lohse, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.02.011 · Cited by 186 · see citing works

Imaging neurotransmitter and neuromodulator dynamics in vivo with genetically encoded indicators

Sabatini, B. L., & Tian, L. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.036 · Cited by 203 · see citing works

Allosteric Modulator Discovery: From Serendipity to Structure-Based Design

Lu, S., He, X., Ni, D., & Zhang, J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01749 · Cited by 176 · see citing works

CXCR2 Receptor: Regulation of Expression, Signal Transduction, and Involvement in Cancer

Korbecki, J., Kupnicka, P., Chlubek, M., Gorący, J., Gutowska, I., & Baranowska‐Bosiacka, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042168 · Cited by 168 · see citing works

Structural and functional characterization of G protein–coupled receptors with deep mutational scanning

Jones, E. M., Lubock, N. B., Venkatakrishnan, A., Wang, J., Tseng, A. M., Paggi, J. M., Latorraca, N. R., Cancilla, D., Satyadi, M., Davis, J. E., et al. (2020) · eLife · doi:10.7554/elife.54895 · Cited by 168 · see citing works

Structure-Based Virtual Screening for Ligands of G Protein–Coupled Receptors: What Can Molecular Docking Do for You?

Ballante, F., Kooistra, A. J., Kampen, S., de Graaf, C., & Carlsson, J. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000246 · Cited by 160 · see citing works

Single-cell transcriptomic evidence for dense intracortical neuropeptide networks

Smith, S. J., Sümbül, U., Graybuck, L. T., Collman, F., Seshamani, S., Gala, R., Gliko, O., Elabbady, L., Miller, J. A., Bakken, T. E., et al. (2019) · eLife · doi:10.7554/elife.47889 · Cited by 156 · see citing works

Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1

Chen, Q., Plasencia, M., Li, Z., Mukherjee, S., Patra, D., Chen, C.-L., Klose, T., Yao, X.-Q., Kossiakoff, A. A., Chang, L., et al. (2021) · Nature · doi:10.1038/s41586-021-03721-x · Cited by 152 · see citing works

The tethered peptide activation mechanism of adhesion GPCRs

Barros-Álvarez, X., Nwokonko, R. M., Vizurraga, A., Matzov, D., He, F., Papasergi-Scott, M. M., Robertson, M. J., Panova, O., Yardeni, E. H., Seven, A. B., et al. (2022) · Nature · doi:10.1038/s41586-022-04575-7 · Cited by 148 · see citing works

Cryo-EM structures of GPCRs coupled to Gs, Gi and Go

García‐Nafría, J., & Tate, C. G. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.02.006 · Cited by 153 · see citing works

G-protein activation by a metabotropic glutamate receptor

Seven, A. B., Barros-Álvarez, X., de Lapeyrière, M., Papasergi-Scott, M. M., Robertson, M. J., Zhang, C.-S., Nwokonko, R. M., Gao, Y., Meyerowitz, J., Rocher, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03680-3 · Cited by 149 · see citing works

Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling

Huang, S. K., Pandey, A. N., Tran, D. P., Villanueva, N., Kitao, A., Sunahara, R. K., Sljoka, A., & Prosser, R. S. (2021) · Cell · doi:10.1016/j.cell.2021.02.041 · Cited by 148 · see citing works

G Protein‐Coupled receptors and heterotrimeric G proteins as cancer drivers

Arang, N., & Gutkind, J. S. (2020) · FEBS Letters · doi:10.1002/1873-3468.14017 · Cited by 147 · see citing works

Chemosensory signal transduction in Caenorhabditis elegans

Ferkey, D. M., Sengupta, P., & L’Étoile, N. D. (2021) · Genetics · doi:10.1093/genetics/iyab004 · Cited by 133 · see citing works

Gut microbiota-derived metabolites tune host homeostasis fate

Kim, S., Seo, S., & Kweon, M. (2024) · Seminars in Immunopathology · doi:10.1007/s00281-024-01012-x · Cited by 145 · see citing works

Structure determination of GPCRs: cryo-EM compared with X-ray crystallography

García‐Nafría, J., & Tate, C. G. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210431 · Cited by 136 · see citing works

Rhodopsin, light-sensor of vision

Hofmann, K. P., & Lamb, T. D. (2022) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2022.101116 · Cited by 126 · see citing works

AlphaFold2 versus experimental structures: evaluation on G protein-coupled receptors

He, X., You, C., Jiang, H., Jiang, Y., Xu, H. E., & Cheng, X. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00938-y · Cited by 119 · see citing works

Molecular basis of opioid receptor signaling

Che, T., & Roth, B. L. (2023) · Cell · doi:10.1016/j.cell.2023.10.029 · Cited by 123 · see citing works

Mutations in G Protein–Coupled Receptors: Mechanisms, Pathophysiology and Potential Therapeutic Approaches

Schöneberg, T., & Liebscher, I. (2020) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000011 · Cited by 127 · see citing works

The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites

Hedderich, J. B., Persechino, M., Becker, K., Heydenreich, F. M., Gutermuth, T., Bouvier, M., Bünemann, M., & Kolb, P. (2022) · Nature Communications · doi:10.1038/s41467-022-29609-6 · Cited by 116 · see citing works

Non-canonical β-adrenergic activation of ERK at endosomes

Kwon, Y., Mehta, S., Clark, M. J., Walters, G., Zhong, Y., Lee, H. N., Sunahara, R. K., & Zhang, J. (2022) · Nature · doi:10.1038/s41586-022-05343-3 · Cited by 116 · 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

Opportunities and challenges in the therapeutic activation of human energy expenditure and thermogenesis to manage obesity

Chen, K. Y., Brychta, R. J., Sater, Z. A., Cassimatis, T. M., Cero, C., Fletcher, L. A., Israni, N. S., Johnson, J. W., Lea, H. J., Linderman, J. D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007363 · Cited by 116 · see citing works

Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20

Wasilko, D. J., Johnson, Z. L., Ammirati, M. J., Che, Y., Griffor, M. C., Han, S., & Wu, H. (2020) · Nature Communications · doi:10.1038/s41467-020-16820-6 · Cited by 111 · see citing works

Structures of active-state orexin receptor 2 rationalize peptide and small-molecule agonist recognition and receptor activation

Hong, C., Byrne, N. J., Zamlynny, B., Tummala, S., Xiao, L., Shipman, J. M., Partridge, A. T., Minnick, C., Breslin, M. J., Rudd, M. T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21087-6 · Cited by 107 · see citing works

Into the Tissues: Extracellular Matrix and Its Artificial Substitutes: Cell Signalling Mechanisms

Bandzerewicz, A., & Gadomska‐Gajadhur, A. (2022) · Cells · doi:10.3390/cells11050914 · Cited by 114 · see citing works

Targeting lipid GPCRs to treat type 2 diabetes mellitus — progress and challenges

Ghislain, J. J., & Poitout, V. (2021) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-00459-w · Cited by 107 · see citing works

Autoregulation of GPCR signalling through the third intracellular loop

Sadler, F. W., Ma, N., Ritt, M., Sharma, Y. K., Vaidehi, N., & Sivaramakrishnan, S. (2023) · Nature · doi:10.1038/s41586-023-05789-z · Cited by 106 · 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

Short-Chain Fatty Acid Receptors and Cardiovascular Function

Lymperopoulos, A., Suster, M. S., & Borges, J. I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063303 · Cited by 106 · see citing works

The cancer-immune dialogue in the context of stress

Ma, Y., & Kroemer, G. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00949-8 · Cited by 110 · see citing works

When trafficking and signaling mix: How subcellular location shapes G protein‐coupled receptor activation of heterotrimeric G proteins

Lobingier, B. T., & von Zastrow, M. (2018) · Traffic · doi:10.1111/tra.12634 · Cited by 102 · see citing works

Structural and Biophysical Mechanisms of Class C G Protein-Coupled Receptor Function

Ellaithy, A., González‐Maeso, J., Logothetis, D. E., & Levitz, J. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.07.008 · Cited by 102 · see citing works

Melatonin Ameliorates Hepatic Ferroptosis in NAFLD by Inhibiting ER Stress via the MT2/cAMP/PKA/IRE1 Signaling Pathway

Guan, Q., Wang, Z., Hu, K., Cao, J., Dong, Y., & Chen, Y. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.85883 · Cited by 102 · see citing works

Receptor Tyrosine Kinase Signaling and Targeting in Glioblastoma Multiforme

Tilak, M., Holborn, J., New, L. A., Lalonde, J., & Jones, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041831 · Cited by 99 · see citing works

Bioorthogonal Reactions of Triarylphosphines and Related Analogues

Heiss, T. K., Dorn, R. S., & Prescher, J. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00014 · Cited by 102 · see citing works

Direct and indirect cholesterol effects on membrane proteins with special focus on potassium channels

Zákány, F., Kovács, T., Panyi, G., & Varga, Z. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158706 · Cited by 94 · see citing works

Molecular Insights from Conformational Ensembles via Machine Learning

Fleetwood, O., Kasimova, M. A., Westerlund, A. M., & Delemotte, L. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.12.016 · Cited by 93 · see citing works

Revealing the Activity of Trimeric G-proteins in Live Cells with a Versatile Biosensor Design

Maziarz, M., Park, J., Leyme, A., Marivin, A., Garcia-Lopez, A., Patel, P. P., & Garcia‐Marcos, M. (2020) · Cell · doi:10.1016/j.cell.2020.06.020 · Cited by 93 · see citing works

Snapshot of the cannabinoid receptor 1-arrestin complex unravels the biased signaling mechanism

Liao, Y., Zhang, H., Shen, Q., Cai, C., Ding, Y., Shen, D., Guo, J., Qin, J., Dong, Y., Zhang, Y., et al. (2023) · Cell · doi:10.1016/j.cell.2023.11.017 · Cited by 93 · see citing works

Structure of the class D GPCR Ste2 dimer coupled to two G proteins

Velazhahan, V., Ma, N., Pándy‐Szekeres, G., Kooistra, A. J., Lee, Y., Gloriam, D. E. I., Vaidehi, N., & Tate, C. G. (2020) · Nature · doi:10.1038/s41586-020-2994-1 · Cited by 91 · see citing works

Capturing a rhodopsin receptor signalling cascade across a native membrane

Chen, S., Getter, T., Salom, D., Wu, D., Quetschlich, D., Chorev, D. S., Palczewski, K., & Robinson, C. V. (2022) · Nature · doi:10.1038/s41586-022-04547-x · Cited by 91 · 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

Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor

Frei, J. N., Broadhurst, R. W., Bostock, M. J., Solt, A., Jones, A. J. Y., Gabriel, F., Tandale, A., Shrestha, B., & Nietlispach, D. (2020) · Nature Communications · doi:10.1038/s41467-020-14526-3 · Cited by 90 · see citing works

Cryo-electron microscopy analysis of small membrane proteins

Nygaard, R., Kim, J., & Mancia, F. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.009 · Cited by 90 · see citing works

Nonantimicrobial Actions of Macrolides: Overview and Perspectives for Future Development

Kricker, J. A., Page, C. P., Gardarsson, F. R., Baldursson, Ó., Guðjónsson, Þ., & Parnham, M. J. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000300 · Cited by 92 · see citing works

Identification and mechanism of G protein-biased ligands for chemokine receptor CCR1

Shao, Z., Shen, Q., Yao, B., Mao, C., Chen, L.-N., Zhang, H., Shen, D., Zhang, C., Li, W., Du, X., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00918-z · Cited by 90 · see citing works

Structure and dynamics of the CGRP receptor in apo and peptide-bound forms

Josephs, T. M., Belousoff, M. J., Liang, Y.-L., Piper, S. J., Cao, J., Garama, D. J., Leach, K., Gregory, K. J., Christopoulos, A., Hay, D. L., et al. (2021) · Science · doi:10.1126/science.abf7258 · Cited by 89 · see citing works

Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2

Zhuang, Y., Wang, L., Guo, J., Sun, D., Wang, Y., Liu, W., Xu, H. E., & Zhang, C. (2022) · Nature Communications · doi:10.1038/s41467-022-28586-0 · Cited by 88 · see citing works

Molecular mechanisms regulating Proteinase-Activated Receptors (PARs)

Chandrabalan, A., & Ramachandran, R. (2021) · The FEBS Journal · doi:10.1111/febs.15829 · Cited by 83 · 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

Orexins as Novel Therapeutic Targets in Inflammatory and Neurodegenerative Diseases

Couvineau, A., Voisin, T., Nicole, P., Gratio, V., Abad, C., & Tan, Y. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00709 · Cited by 86 · see citing works

Molecular insights into ligand recognition and activation of chemokine receptors CCR2 and CCR3

Shao, Z., Tan, Y., Shen, Q., Hou, L., Yao, B., Qin, J., Xu, P., Mao, C., Chen, L.-N., Zhang, H., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00403-4 · Cited by 86 · see citing works

Hormone- and antibody-mediated activation of the thyrotropin receptor

Duan, J., Xu, P., Luan, X., Ji, Y., He, X., Song, N., Yuan, Q., Jin, Y., Cheng, X., Jiang, H., et al. (2022) · Nature · doi:10.1038/s41586-022-05173-3 · Cited by 85 · see citing works

Structural Insights into CB1 Receptor Biased Signaling

Al-Zoubi, R. M., Morales, P., & Reggio, P. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081837 · Cited by 82 · see citing works

Energy Landscapes Reveal Agonist Control of G Protein-Coupled Receptor Activation via Microswitches

Fleetwood, O., Matricon, P. G., Carlsson, J., & Delemotte, L. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b00842 · Cited by 84 · see citing works

A conserved molecular switch in Class F receptors regulates receptor activation and pathway selection

Wright, S. C., Kozielewicz, P., Kowalski-Jahn, M., Petersen, J., Bowin, C.-F., Slodkowicz, G., Martí-Solano, M., Rodriguez, D. J., Hot, B., Okashah, N., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08630-2 · Cited by 84 · see citing works

Frizzleds as GPCRs – More Conventional Than We Thought!

Schulte, G., & Wright, S. C. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.07.001 · Cited by 82 · see citing works

Structures of atypical chemokine receptor 3 reveal the basis for its promiscuity and signaling bias

Yen, Y., Schafer, C. T., Gustavsson, M. B., Eberle, S. A., Dominik, P. K., Deneka, D., Zhang, P., Schall, T. J., Kossiakoff, A. A., Tesmer, J. J. G., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn8063 · Cited by 79 · see citing works

Translating the force—mechano-sensing GPCRs

Wilde, C., Mitgau, J., Suchý, T., Schöneberg, T., & Liebscher, I. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00465.2021 · Cited by 79 · see citing works

Retinitis Pigmentosa: Novel Therapeutic Targets and Drug Development

Wu, K. Y., Kulbay, M., Toameh, D., Xu, A. Q., Kalevar, A., & Tran, S. D. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020685 · Cited by 81 · see citing works

Ligand efficacy modulates conformational dynamics of the µ-opioid receptor

Zhao, J., Elgeti, M., O’Brien, E. S., Sár, C. P., Daibani, A. E., Heng, J., Sun, X., White, E., Che, T., Hubbell, W. L., et al. (2024) · Nature · doi:10.1038/s41586-024-07295-2 · Cited by 79 · see citing works

Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist

Isaikina, P., Tsai, C., Dietz, N., Pamula, F. K., Grahl, A., Goldie, K. N., Guixà-González, R., Branco, C., Paolini‐Bertrand, M., Calo, N., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg8685 · Cited by 78 · see citing works

Harnessing Brain Plasticity: The Therapeutic Power of Repetitive Transcranial Magnetic Stimulation (rTMS) and Theta Burst Stimulation (TBS) in Neurotransmitter Modulation, Receptor Dynamics, and Neuroimaging for Neurological Innovations

Sharbafshaaer, M., Cirillo, G., Esposito, F., Tedeschi, G., & Trojsi, F. (2024) · Biomedicines · doi:10.3390/biomedicines12112506 · Cited by 80 · see citing works

Structural Basis of the Activation of Heterotrimeric Gs-Protein by Isoproterenol-Bound β1-Adrenergic Receptor

Su, M., Zhu, L., Zhang, Y., Paknejad, N., Dey, R., Huang, J., Lee, M.-Y., Williams, D., Jordan, K. D., Eng, E. T., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.08.001 · Cited by 75 · see citing works

Molecular insights into the biased signaling mechanism of the μ-opioid receptor

Cong, X., Maurel, D., Déméné, H., Vasiliauskaité-Brooks, I., Hagelberger, J., Peysson, F., Saint‐Paul, J., Golebiowski, J., Granier, S., & Sounier, R. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.033 · Cited by 77 · 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

Neural Mechanisms in Cardiovascular Health and Disease

Ziegler, K. A., Engelhardt, S. H., Carnevale, D., McAlpine, C. S., Guzik, T. J., Dimmeler, S., & Świrski, F. K. (2025) · Circulation Research · doi:10.1161/circresaha.125.325580 · Cited by 85 · see citing works

Allosteric modulation of G protein-coupled receptor signaling

Shen, S., Zhao, C. S., Wu, C., Sun, S., Li, Z., Yan, W. X., & Shao, Z. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1137604 · Cited by 75 · see citing works

Structural and functional analyses of a GPCR-inhibited ion channel TRPM3

Zhao, C., & MacKinnon, R. (2022) · Neuron · doi:10.1016/j.neuron.2022.10.002 · Cited by 69 · see citing works

Structural basis of human ghrelin receptor signaling by ghrelin and the synthetic agonist ibutamoren

Liu, H., Sun, D., Myasnikov, A. G., Damian, M., Banères, J., Sun, J., & Zhang, C. (2021) · Nature Communications · doi:10.1038/s41467-021-26735-5 · Cited by 69 · see citing works

Structural genomics of the human dopamine receptor system

Xu, P., Huang, S., Krumm, B. E., Zhuang, Y., Mao, C., Zhang, Y., Wang, Y., Huang, X.-P., Liu, Y., He, X., et al. (2023) · Cell Research · doi:10.1038/s41422-023-00808-0 · Cited by 70 · see citing works

Conformational pathway provides unique sensitivity to a synaptic mGluR

Habrian, C. H., Levitz, J., Vyklický, V., Fu, Z., Hoagland, A., McCort‐Tranchepain, I., Acher, F., & Isacoff, E. Y. (2019) · Nature Communications · doi:10.1038/s41467-019-13407-8 · Cited by 68 · see citing works

State-selective modulation of heterotrimeric Gαs signaling with macrocyclic peptides

Dai, S. A., Hu, Q., Gao, R. B., Blythe, E. E., Touhara, K. K., Peacock, H., Zhang, Z., von Zastrow, M., Suga, H., & Shokat, K. M. (2022) · Cell · doi:10.1016/j.cell.2022.09.019 · Cited by 68 · see citing works

Receptor-Arrestin Interactions: The GPCR Perspective

Seyedabadi, M., Gharghabi, M., Gurevich, E. V., & Gurevich, V. V. (2021) · Biomolecules · doi:10.3390/biom11020218 · Cited by 68 · see citing works

Towards the Idea of Molecular Brains

Timsit, Y., & Sergeant-Perthuis, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111868 · Cited by 72 · see citing works

AlphaFold accelerated discovery of psychotropic agonists targeting the trace amine–associated receptor 1

Díaz‐Holguín, A., Saarinen, M., Vo, D. D., Sturchio, A., Branzell, N., de Vaca, I. C., Hu, H., Mitjavila-Domènech, N., Lindqvist, A., Baranczewski, P., et al. (2024) · Science Advances · doi:10.1126/sciadv.adn1524 · Cited by 67 · see citing works

Identification of ligand-specific G protein-coupled receptor states and prediction of downstream efficacy via data-driven modeling

Fleetwood, O., Carlsson, J., & Delemotte, L. (2021) · eLife · doi:10.7554/elife.60715 · Cited by 66 · see citing works

Genetically Encoded Biosensors Based on Fluorescent Proteins

Kim, H., Ju, J.-M., Lee, H. N., Chun, H., & Seong, J. (2021) · Sensors · doi:10.3390/s21030795 · Cited by 64 · see citing works

Structural Basis for G Protein–Coupled Receptor Signaling

Erlandson, S. C., McMahon, C. T., & Kruse, A. C. (2018) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070317-032931 · Cited by 126 · see citing works

Structural mechanism of G protein activation by G protein-coupled receptor

Duc, N. M., Kim, H. R., & Chung, K. Y. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.05.016 · Cited by 83 · see citing works

Active state structures of G protein-coupled receptors highlight the similarities and differences in the G protein and arrestin coupling interfaces

Carpenter, B., & Tate, C. G. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.04.010 · Cited by 73 · see citing works

G protein‐coupled receptors: a count of 1001 conformations

Vauquelin, G., & Liefde, I. V. (2005) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.2005.00319.x · Cited by 91 · see citing works

Structural Aspects of GPCR-G Protein Coupling

Chung, K. Y. (2013) · Toxicological Research · doi:10.5487/tr.2013.29.3.149 · Cited by 19 · see citing works