The DOI matches its Crossref record; 90 of the 91 references it cites were found in a registry or an index.
Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor
Open accessAbstract
Hallucinogens like lysergic acid diethylamide (LSD), psilocybin, and substituted N-benzyl phenylalkylamines are widely used recreationally with psilocybin being considered as a therapeutic for many neuropsychiatric disorders including depression, anxiety, and substance abuse. How psychedelics mediate their actions-both therapeutic and hallucinogenic-are not understood, although activation of the 5-HT 2A serotonin receptor (HTR2A) is key. To gain molecular insights into psychedelic actions, we determined the active-state structure of HTR2A bound to 25-CN-NBOH-a prototypical hallucinogen-in complex with an engineered Gαq heterotrimer by cryoelectron microscopy (cryo-EM). We also obtained the X-ray crystal structures of HTR2A complexed with the arrestin-biased ligand LSD or the inverse agonist methiothepin. Comparisons of these structures reveal determinants responsible for HTR2A-Gαq protein interactions as well as the conformational rearrangements involved in active-state transitions. Given the potential therapeutic actions of hallucinogens, these findings could accelerate the discovery of more selective drugs for the treatment of a variety of neuropsychiatric disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Serotonergic psychedelics act as partial agonists of the serotonin 2A receptor (5-HT2AR) in the brain [7].”
From Psilocybin-assisted therapy for severe alcohol use disorder: protocol for a double-blind, randomized, placebo-controlled, 7-month parallel-group phase II superiority trial (2024) · cites this paper as [7]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling
Guex, N., & Peitsch, M. C. (1997) · Electrophoresis · doi:10.1002/elps.1150181505 · Cited by 11,312
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Electrostatics of nanosystems: Application to microtubules and the ribosome
Baker, N., Sept, D., Joseph, S., Holst, M., & McCammon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181342398 · Cited by 7,125
Cited by
Sorted by citations
Psilocybin induces rapid and persistent growth of dendritic spines in frontal cortex in vivo
Shao, L.-X., Liao, C., Gregg, I., Davoudian, P. A., Savalia, N. K., Delagarza, K., & Kwan, A. C. (2021) · Neuron · doi:10.1016/j.neuron.2021.06.008 · Cited by 626
Psychedelics promote neuroplasticity through the activation of intracellular 5-HT2A receptors
Vargas, M. V., Dunlap, L. E., Dong, C., Carter, S. J., Tombari, R. J., Jami, S. A., Cameron, L. P., Patel, S. D., Hennessey, J. J., Saeger, H. N., et al. (2023) · Science · doi:10.1126/science.adf0435 · Cited by 519
Psychedelics reopen the social reward learning critical period
Nardou, R., Sawyer, E., Song, Y. J., Wilkinson, M., Padovan-Hernandez, Y., de Deus, J. L., Wright, N., Lama, C., Faltin, S., Goff, L. A., et al. (2023) · Nature · doi:10.1038/s41586-023-06204-3 · Cited by 358
Structure-based discovery of nonhallucinogenic psychedelic analogs
Cao, D., Yu, J., Wang, H., Luo, Z., Liu, X., He, L., Qi, J., Fan, L., Tang, L., Chen, Z., et al. (2022) · Science · doi:10.1126/science.abl8615 · Cited by 312
The neural basis of psychedelic action
Kwan, A. C., Olson, D. E., Preller, K. H., & Roth, B. L. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01177-4 · Cited by 330
Self-citationNeuroplasticity as a convergent mechanism of ketamine and classical psychedelics
Aleksandrova, L. R., & Phillips, A. G. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.08.003 · Cited by 276
Structural insights into the lipid and ligand regulation of serotonin receptors
Xu, P., Huang, S., Zhang, H., Mao, C., Zhou, X. E., Cheng, X., Simon, Í. A., Shen, D., Yen, H., Robinson, C. V., et al. (2021) · Nature · doi:10.1038/s41586-021-03376-8 · Cited by 277
Bespoke library docking for 5-HT2A receptor agonists with antidepressant activity
Kaplan, A. L., Confair, D. N., Kim, K., Barros-Álvarez, X., Rodriguiz, R. M., Ying, Y., Kweon, O. S., Che, T., McCorvy, J. D., Kamber, D. N., et al. (2022) · Nature · doi:10.1038/s41586-022-05258-z · Cited by 257
Self-citationStructure, function and pharmacology of human itch GPCRs
Cao, C., Kang, H. J., Singh, I., Chen, H., Zhang, C., Ye, W., Hayes, B. W., Liu, J., Gumpper, R. H., Bender, B. J., et al. (2021) · Nature · doi:10.1038/s41586-021-04126-6 · Cited by 234
Self-citationLu, 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 229
Pharmacological, neural, and psychological mechanisms underlying psychedelics: A critical review
van Elk, M., & Yaden, D. B. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104793 · Cited by 221
Psychedelic-inspired drug discovery using an engineered biosensor
Dong, C., Ly, C., Dunlap, L. E., Vargas, M. V., Sun, J., Hwang, I.-W., Azinfar, A., Oh, W. C., Wetsel, W. C., Olson, D. E., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.043 · Cited by 213
Structural basis of ligand recognition at the human MT1 melatonin receptor
Stauch, B., Johansson, L. C., McCorvy, J. D., Patel, N., Han, G. W., Huang, X., Gati, C., Batyuk, A., Slocum, S. T., Ishchenko, A., et al. (2019) · Nature · doi:10.1038/s41586-019-1141-3 · Cited by 211
Self-citationThe promises and perils of psychedelic pharmacology for psychiatry
McClure‐Begley, T. D., & Roth, B. L. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00421-7 · Cited by 202
Self-citationIdentification 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 193
AlphaFold2 structures guide prospective ligand discovery
Lyu, J., Kapolka, N. J., Gumpper, R. H., Alon, A., Wang, L., Jain, M. K., Barros-Álvarez, X., Sakamoto, K., Kim, Y., DiBerto, J. F., et al. (2024) · Science · doi:10.1126/science.adn6354 · Cited by 192
Self-citationCASTpFold: Computed Atlas of Surface Topography of the universe of protein Folds
Ye, B., Tian, W., Wang, B., & Liang, J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae415 · Cited by 180
Ballante, F., Kooistra, A. J., Kampen, S., de Graaf, C., & Carlsson, J. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000246 · Cited by 169
Signaling snapshots of a serotonin receptor activated by the prototypical psychedelic LSD
Cao, C., Barros-Álvarez, X., Zhang, S., Kim, K., Dämgen, M. A., Panova, O., Suomivuori, C., Fay, J. F., Zhong, X., Krumm, B. E., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.08.006 · Cited by 159
Self-citationThe 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
Self-citationHuang, S., Xu, P., Shen, D., Simon, Í. A., Mao, C., Tan, Y., Zhang, H., Harpsøe, K., Li, H., Zhang, Y., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.031 · Cited by 145
Biochemical Mechanisms Underlying Psychedelic-Induced Neuroplasticity
Olson, D. E. (2022) · Biochemistry · doi:10.1021/acs.biochem.1c00812 · Cited by 146
Unsaturated bond recognition leads to biased signal in a fatty acid receptor
Mao, C., Xiao, P., Tao, X.-N., Qin, J., He, Q., Zhang, C., Guo, S., Du, Y., Chen, L.-N., Shen, D., et al. (2023) · Science · doi:10.1126/science.add6220 · Cited by 128
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 130
Self-citationKelmendi, B., Kaye, A. P., Pittenger, C., & Kwan, A. C. (2022) · Current Biology · doi:10.1016/j.cub.2021.12.009 · Cited by 137
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 125
Ligand binding at the protein–lipid interface: strategic considerations for drug design
Payandeh, J., & Volgraf, M. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00240-2 · Cited by 121
Cryo-EM structure of the human histamine H1 receptor/Gq complex
Xia, R., Wang, N., Xu, Z., Lu, Y., Song, J. K., Zhang, A., Guo, C., & He, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-22427-2 · Cited by 117
Structures of active melanocortin-4 receptor–Gs-protein complexes with NDP-α-MSH and setmelanotide
Heyder, N., Kleinau, G., Speck, D., Schmidt, A., Paisdzior, S., Szczepek, M., Bauer, B., Koch, A., Gallandi, M., Kwiatkowski, D., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00569-8 · Cited by 110
The mechanism for ligand activation of the GPCR–G protein complex
Mafi, A., Kim, S., & Goddard, W. A. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110085119 · Cited by 103
Canalization and plasticity in psychopathology
Carhart-Harris, R. L., Chandaria, S., Erritzøe, D., Gazzaley, A. H., Girn, M., Kettner, H., Mediano, P. A. M., Nutt, D. J., Rosas, F. E., Roseman, L., et al. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109398 · Cited by 107
Ligand recognition and G-protein coupling selectivity of cholecystokinin A receptor
Liu, Q., Yang, D., Zhuang, Y., Croll, T. I., Cai, X., Dai, A., He, X., Duan, J., Yin, W., Ye, C., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00841-3 · Cited by 99
Selective G protein signaling driven by substance P–neurokinin receptor dynamics
Harris, J. A., Faust, B., Gondin, A. B., Dämgen, M. A., Suomivuori, C., Veldhuis, N. A., Cheng, Y., Dror, R. O., Thal, D. M., & Manglik, A. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00890-8 · Cited by 98
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 100
LSD-stimulated behaviors in mice require β-arrestin 2 but not β-arrestin 1
Rodriguiz, R. M., Nadkarni, V., Means, C. R., Pogorelov, V. M., Chiu, Y.-T., Roth, B. L., & Wetsel, W. C. (2021) · Scientific Reports · doi:10.1038/s41598-021-96736-3 · Cited by 96
Self-citation“Selective” serotonin 5-HT2A receptor antagonists
Casey, A. B., Cui, M., Booth, R. G., & Canal, C. E. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115028 · Cited by 94
Beyond the 5-HT2AReceptor: Classic and Nonclassic Targets in Psychedelic Drug Action
Cameron, L. P., Benetatos, J., Lewis, V., Bonniwell, E. M., Jaster, A. M., Moliner, R., Ċastrén, E., McCorvy, J. D., Palner, M., & Aguilar‐Valles, A. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1384-23.2023 · Cited by 100
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 103
Glatfelter, G. C., Pottie, E., Partilla, J. S., Sherwood, A. M., Kaylo, K. W., Pham, D. N. K., Naeem, M., Sammeta, V. R., DeBoer, S., Golen, J. A., et al. (2022) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.2c00177 · Cited by 95
Structure reveals the activation mechanism of the MC4 receptor to initiate satiation signaling
Israeli, H., Degtjarik, O., Fierro, F., Chunilal, V., Gill, A. K., Roth, N. J., Botta, J. A., Prabahar, V., Peleg, Y., Chan, L. F., et al. (2021) · Science · doi:10.1126/science.abf7958 · Cited by 96
Molecular basis for selective activation of DREADD-based chemogenetics
Zhang, S., Gumpper, R. H., Huang, X., Liu, Y., Krumm, B. E., Cao, C., Fay, J. F., & Roth, B. L. (2022) · Nature · doi:10.1038/s41586-022-05489-0 · Cited by 95
Self-citationPsychedelic perceptions: mental health service user attitudes to psilocybin therapy
Corrigan, K., Haran, M., McCandliss, C., McManus, R., Cleary, S., Trant, R., Kelly, Y., Ledden, K., Rush, G., O’Keane, V., et al. (2022) · Irish Journal of Medical Science (1971 -) · doi:10.1007/s11845-021-02668-2 · Cited by 84
Molecular mechanisms regulating Proteinase-Activated Receptors (PARs)
Chandrabalan, A., & Ramachandran, R. (2021) · The FEBS Journal · doi:10.1111/febs.15829 · Cited by 83
Mobbs, J. I., Belousoff, M. J., Harikumar, K. G., Piper, S. J., Xu, X., Furness, S. G. B., Venugopal, H., Christopoulos, A., Danev, R., Wootten, D. L., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001295 · Cited by 82
Kozłowska, U., Nichols, C. D., Wiatr, K., & Figiel, M. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15509 · Cited by 86
Structural pharmacology and therapeutic potential of 5-methoxytryptamines
Warren, A. L., Lankri, D., Cunningham, M. J., Serrano, I. C., Parise, L. F., Kruegel, A. C., Duggan, P., Zilberg, G., Capper, M. J., Havel, V., et al. (2024) · Nature · doi:10.1038/s41586-024-07403-2 · Cited by 84
Self-citationEvolving cryo-EM structural approaches for GPCR drug discovery
Zhang, X., Johnson, R. M., Drulyte, I., Yu, L., Kotecha, A., Danev, R., Wootten, D. L., Sexton, P. M., & Belousoff, M. J. (2021) · Structure · doi:10.1016/j.str.2021.04.008 · Cited by 81
Duan, W., Cao, D., Wang, S., & Cheng, J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00375 · Cited by 81
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 85
Self-citationMolecular recognition of an acyl-peptide hormone and activation of ghrelin receptor
Wang, Y., Guo, S., Zhuang, Y., Yun, Y., Xu, P., He, X., Guo, J., Yin, W., Xu, H. E., Xie, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25364-2 · Cited by 75
Structure-guided discovery of bile acid derivatives for treating liver diseases without causing itch
Yang, J. J. J., Zhao, T., Fan, J., Zou, H., Lan, G., Guo, F., Shi, Y., Ke, H., Yu, H., Yue, Z., et al. (2024) · Cell · doi:10.1016/j.cell.2024.10.001 · Cited by 75
Chen, Z., Fan, L., Wang, H., Yu, J., Lu, D., Qi, J., Nie, F., Luo, Z., Liu, Z., Cheng, J., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00971-w · Cited by 74
Neurotensin Receptor Allosterism Revealed in Complex with a Biased Allosteric Modulator
Krumm, B. E., DiBerto, J. F., Olsen, R. H. J., Kang, H. J., Slocum, S. T., Zhang, S., Strachan, R. T., Huang, X., Slosky, L. M., Pinkerton, A. B., et al. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00029 · Cited by 75
Self-citationPsychedelic therapy's transdiagnostic effects: A research domain criteria (RDoC) perspective
Kelly, J. R., Gillan, C. M., Prenderville, J., Kelly, C., Harkin, A., Clarke, G., & O'Keane, V. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.800072 · Cited by 69
Overcoming Depression with 5-HT2A Receptor Ligands
Zięba, A., Stępnicki, P., Matosiuk, D., & Kaczor, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010010 · Cited by 70
Structure, dynamics and lipid interactions of serotonin receptors: excitements and challenges
Sarkar, P., Mozumder, S., Bej, A., Mukherjee, S., Sengupta, J., & Chattopadhyay, A. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00772-8 · Cited by 68
Deep contrastive learning enables genome-wide virtual screening
Jia, Y., Gao, B., Tan, J., Zheng, J., Hong, X., Zhu, W., Tan, H., Xiao, Y., Tan, L., Cai, H., et al. (2026) · Science · doi:10.1126/science.ads9530 · Cited by 66
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 74
Self-citationA unified model of ketamine’s dissociative and psychedelic properties
Marguilho, M., Figueiredo, I., & Castro-Rodrigues, P. (2022) · Journal of Psychopharmacology · doi:10.1177/02698811221140011 · Cited by 71
Dynamic spatiotemporal determinants modulate GPCR:G protein coupling selectivity and promiscuity
Sandhu, M., Cho, A., Ma, N., Mukhaleva, E., Namkung, Y., Lee, S., Ghosh, S., Lee, J. H., Gloriam, D. E. I., Laporte, S. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34055-5 · Cited by 63
Update on GPCR-based targets for the development of novel antidepressants
Mantas, I., Saarinen, M., Xu, Q., & Svenningsson, P. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01040-1 · Cited by 61
A bitter anti-inflammatory drug binds at two distinct sites of a human bitter taste GPCR
Peri, L., Matzov, D., Huxley, D. R., Rainish, A., Fierro, F., Sapir, L., Pfeiffer, T., Waterloo, L. A. W., Hübner, H., Peleg, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54157-6 · Cited by 61
Ma, S., Chen, Y., Dai, A., Yin, W., Guo, J., Yang, D., Zhou, F., Jiang, Y., Wang, M., & Xu, H. E. (2021) · Cell Research · doi:10.1038/s41422-021-00557-y · Cited by 59
Molecular basis for kinin selectivity and activation of the human bradykinin receptors
Yin, Y.-L., Ye, C., Zhou, F., Wang, J., Yang, D., Yin, W., Wang, M., Xu, H. E., & Jiang, Y. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00645-y · Cited by 58
Molecular mechanism of agonism and inverse agonism in ghrelin receptor
Qin, J., Cai, Y., Xu, Z., Ming, Q., Ji, S.-Y., Wu, C., Zhang, H., Mao, C., Shen, D.-D., Hirata, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-27975-9 · Cited by 57
Solmi, M., Chen, C., Dauré, C., Buot, A., Ljuslin, M., Verroust, V., Mallet, L., Khazaal, Y., Rothen, S., Thorens, G., et al. (2022) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2022.09.004 · Cited by 62
The structure, function, and pharmacology of MRGPRs
Cao, C., & Roth, B. L. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.02.002 · Cited by 59
Self-citationMolecular basis of ligand recognition and activation of human V2 vasopressin receptor
Zhou, F., Ye, C., Ma, X., Yin, W., Croll, T. I., Zhou, Q., He, X., Zhang, X., Yang, D., Wang, P., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00480-2 · Cited by 58
Molecular insights into psychedelic drug action
Slocum, S. T., DiBerto, J. F., & Roth, B. L. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15540 · Cited by 59
Self-citationChen, T., Cheng, L., Ma, J., Yuan, J., Pi, C., Xiong, L., Chen, J., Liu, H., Tang, J., Zhong, Y., et al. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106837 · Cited by 59
Pottie, E., Dedecker, P., & Stove, C. P. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114251 · Cited by 55
Psychedelics as Transformative Therapeutics
Roth, B. L., & Gumpper, R. H. (2023) · American Journal of Psychiatry · doi:10.1176/appi.ajp.20230172 · Cited by 57
Self-citationMechanisms and molecular targets surrounding the potential therapeutic effects of psychedelics
Jaster, A. M., & González‐Maeso, J. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02274-x · Cited by 56
Design and structural validation of peptide–drug conjugate ligands of the kappa-opioid receptor
Muratspahić, E., Deibler, K., Han, J., Tomašević, N., Jadhav, K. B., Olivé-Marti, A.-L., Hochrainer, N., Hellinger, R., Koehbach, J., Fay, J. F., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43718-w · Cited by 55
Self-citationThom, C., Ehrenmann, J., Vacca, S., Waltenspühl, Y., Schöppe, J., Medalia, O., & Plückthun, A. (2021) · Science Advances · doi:10.1126/sciadv.abk2872 · Cited by 54
Gumpper, R. H., Fay, J. F., & Roth, B. L. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111211 · Cited by 50
Self-citationThe oxytocin signaling complex reveals a molecular switch for cation dependence
Meyerowitz, J., Robertson, M. J., Barros-Álvarez, X., Panova, O., Nwokonko, R. M., Gao, Y., & Skiniotis, G. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00728-4 · Cited by 51
Self-citationCryo-EM Structure of the β3 Adrenergic Receptor Reveals the Molecular Basis of Subtype Selectivity
Nagiri, C., Kobayashi, K., Tomita, A., Katô, M., Kobayashi, K., Yamashita, K., Nishizawa, T., Inoue, A., Shihoya, W., & Nureki, O. (2020) · Molecular Cell · doi:10.1016/j.molcel.2021.06.024 · Cited by 49
The Bright Side of Psychedelics: Latest Advances and Challenges in Neuropharmacology
Mastinu, A., Anyanwu, M., Carone, M., Abate, G., Bonini, S. A., Peron, G., Tirelli, E., Pucci, M., Ribaudo, G., Oselladore, E., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021329 · Cited by 52
Advancing preclinical models of psychiatric disorders with human brain organoid cultures
Dixon, T. A., & Muotri, A. R. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01708-2 · Cited by 49
Structural studies of serotonin receptor family
Parajulee, A., & Kim, K. (2023) · BMB Reports · doi:10.5483/bmbrep.2023-0147 · Cited by 51
Self-citationElucidating pathway-selective biased CCKBR agonism for Alzheimer’s disease treatment
Wang, J., Sha, X.-Y., Shao, Y., Zhang, Z.-H., Huang, S.-M., Lin, H., Gan, S., Zhang, N., Xia, X., Sun, Y.-N., et al. (2025) · Cell · doi:10.1016/j.cell.2025.10.034 · Cited by 49
Structural insights into angiotensin receptor signaling modulation by balanced and biased agonists
Zhang, D., Liu, Y., Zaidi, S. A., Xu, L., Zhan, Y., Chen, A., Guo, J., Huang, X., Roth, B. L., Katritch, V., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112940 · Cited by 47
Self-citationStructural basis of CXC chemokine receptor 1 ligand binding and activation
Ishimoto, N., Park, J.-H., Kawakami, K., Tajiri, M., Mizutani, K., Akashi, S., Tame, J. R. H., Inoue, A., & Park, S. (2023) · Nature Communications · doi:10.1038/s41467-023-39799-2 · Cited by 47
Allosteric modulation of ghrelin receptor signaling by lipids
Damian, M., Louet, M., Gomes, A. A. S., M’Kadmi, C., Denoyelle, S., Cantel, S., Mary, S., Bisch, P. M., Fehrentz, J., Catoire, L. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23756-y · Cited by 47
Ligand recognition and allosteric modulation of the human MRGPRX1 receptor
Liu, Y., Cao, C., Huang, X., Gumpper, R. H., Rachman, M. M., Shih, S. L., Krumm, B. E., Zhang, S., Shoichet, B. K., Fay, J. F., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01173-6 · Cited by 46
Self-citationPeng, S., Zhan, Y., Zhang, D., Ren, L., Chen, A., Chen, Z., & Zhang, H. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216230120 · Cited by 46
Kiilerich, K. F., Lorenz, J., Scharff, M. B., Speth, N., Brandt, T. G., Czurylo, J., Xiong, M., Jessen, N. S., Casado-Sainz, A., Shalgunov, V., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02280-z · Cited by 48
Structural insights into galanin receptor signaling
Jiang, W., & Zheng, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121465119 · Cited by 44
DiffBindFR: an SE(3) equivariant network for flexible protein–ligand docking
Zhu, J., Gu, Z., Pei, J., & Lai, L. (2024) · Chemical Science · doi:10.1039/d3sc06803j · Cited by 46
The structural diversity of psychedelic drug actions revealed
Gumpper, R. H., Jain, M. K., Kim, K., Sun, R., Sun, N., Xu, Z., DiBerto, J. F., Krumm, B. E., Kapolka, N. J., Kanıskan, H. Ü., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57956-7 · Cited by 45
Self-citationZhang, Y., Wang, N., Zhang, L., Zhuang, Y., Xin, Q., Gu, X., Jiang, C., & Wu, J. (2025) · MedComm · doi:10.1002/mco2.70383 · Cited by 46
Bous, J., Orcel, H., Floquet, N., Leyrat, C., Lai‐Kee‐Him, J., Gaibelet, G., Ancelin, A., Saint‐Paul, J., Trapani, S., Louet, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg5628 · Cited by 45
Cryo-EM advances in GPCR structure determination
Shihoya, W., Iwama, A., Sano, F. K., & Nureki, O. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae029 · Cited by 43
Pharmacological fingerprint of antipsychotic drugs at the serotonin 5-HT2A receptor
Gaitonde, S. A., Avet, C., Revenga, M. D. L. F., Blondel-Tepaz, É., Shahraki, A., Pastor, A. M., Talagayev, V., Robledo, P., Kolb, P., Selent, J., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02531-7 · Cited by 47
Molecular design of a therapeutic LSD analogue with reduced hallucinogenic potential
Tuck, J. R., Dunlap, L. E., Khatib, Y. A., Hatzipantelis, C. J., Novak, S. W., Rahn, R. M., Davis, A. R., Mosswood, A., Vernier, A. M. M., Fenton, E. M., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2416106122 · Cited by 48
Photoswitchable Serotonins for Optical Control of the 5‐HT2A Receptor**
Morstein, J., Romano, G. R., Hetzler, B. E., Plante, A., Haake, C., Levitz, J., & Trauner, D. H. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202117094 · Cited by 40
Assessment of the Acute Effects of 2C‐B vs. Psilocybin on Subjective Experience, Mood, and Cognition
Mallaroni, P., Mason, N. L., Reckweg, J. T., Paci, R., Ritscher, S., Toennes, S. W., Theunissen, E. L., Kuypers, K. P. C., & Ramaekers, J. G. (2023) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.2958 · Cited by 42
Stimulant and hallucinogenic novel psychoactive substances; an update
Schifano, F., Vento, A. E., Scherbaum, N., & Guirguis, A. (2023) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2023.2279192 · Cited by 39
Structural basis for the ligand recognition and signaling of free fatty acid receptors
Zhang, X., Guseinov, A.-A., Jenkins, L., Li, K., Tikhonova, I. G., Milligan, G., & Zhang, C. (2024) · Science Advances · doi:10.1126/sciadv.adj2384 · Cited by 40
Metadata
- Authors
- 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., Shoichet, B. K., Skiniotis, G., & Roth, B. L.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Stanford Medicine (US)
- University of California, San Francisco (US)
- Corresponding author
- Skiniotis, Georgios
- Roth, Bryan L.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-09
- Volume
- 182
- Issue
- 6
- Pages
- 1574-1588.e19
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7593816
- OpenAlex
- W3086773311
- Cited by
- 481
- References
- 91
- Citations by year
- 2026: 59 · 2025: 92 · 2024: 86 · 2023: 88 · 2022: 76 · 2021: 72 · 2020: 6
- FWCI
- 19.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- National Institute on Drug Abuse
- National Institute of Mental Health
- National Institutes of Health (R37DA04567, R01MH112205)
- Argonne National Laboratory (DE-AC02-06CH11357)
- National Institute of General Medical Sciences (AGM-12006)
- National Cancer Institute (ACB-12002, P30CA016086)
- Defense Advanced Research Projects Agency (HR0011-20-2-0029, R35GM122481)
- Office of Science
- U.S. Department of Defense
- National Research Foundation of Korea (2017R1A6A3A03012547)
- University of North Carolina
- U.S. Department of Energy
- Government of South Australia
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Social Sciences › Psychology › Clinical Psychology › Psychedelics and Drug Studies
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- 5-HT2A receptor, hallucinogens, LSD, psilocybin, receptor-G protein complex, methiothepin, inverse agonists, neuropsychiatric disorders
- MeSH terms
- Protein Conformation, alpha-Helical, Animals, Hallucinogens, Humans, Ligands, Lysergic Acid Diethylamide, Methiothepin, Models, Chemical, Mutation, Recombinant Proteins, Serotonin, Gene Expression, Crystallography, X-Ray, Spodoptera, Cryoelectron Microscopy, GTP-Binding Protein alpha Subunits, Gq-G11, Receptor, Serotonin, 5-HT2A, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
