The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Structural Features for Functional Selectivity at Serotonin Receptors
Abstract
Dissecting Serotonin Receptors: Serotonin receptors are the targets for many widely used drugs prescribed to treat ailments from depression to obesity and migraine headaches (see the Perspective by Palczewski and Kiser ). C. Wang et al. (p. 610 , published online 21 March) and Wacker et al. (p. 615 , published online 21 March) describe crystal structures of two members of the serotonin family of receptors bound to antimigraine medications or to a precursor of the hallucinogenic drug LSD. Subtle differences in the way particular ligands bind to the receptors cause substantial differences in the signals generated by the receptor and the consequent biological responses. The structures reveal how the same ligand can activate one or both of the two main serotonin receptor signaling mechanisms, depending on which particular receptor it binds.
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.
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
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
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
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.-J., Kuhn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,264
Self-citationCrystal 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
Ballesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001
OPM database and PPM web server: resources for positioning of proteins in membranes
Lomize, M. A., Pogozheva, I. D., Joo, H., Mosberg, H. I., & Lomize, A. L. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr703 · Cited by 2,126
The expanded biology of serotonin
Berger, M., Gray, J. A., & Roth, B. L. (2009) · Annual Review of Medicine · doi:10.1146/annurev.med.60.042307.110802 · Cited by 2,100
Self-citationMinor, W., Cymborowski, M., Otwinowski, Z., & Chruszcz, M. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906019949 · Cited by 2,099
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 1,718
Research works printed but not linked: 1
- G. Bricogne et al . Buster version 2.8.0 (Global Phasing Cambridge 2011).
Cited by
Roth, B. L. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.040 · Cited by 1,742
Self-citationPRESTO-Tango as an open-source resource for interrogation of the druggable human GPCRome
Kroeze, W. K., Sassano, M. F., Huang, X.-P., Lansu, K., McCorvy, J. D., Giguère, P. M., Sciaky, N., & Roth, B. L. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3014 · Cited by 755
Self-citationHow 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
Self-citationStructure 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
Self-citationMuscarinic acetylcholine receptors: novel opportunities for drug development
Kruse, A. C., Kobilka, B. K., Gautam, D., Sexton, P. M., Christopoulos, A., & Wess, J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4295 · Cited by 437
Preller, K. H., Burt, J. B., Ji, J. L., Schleifer, C. H., Adkinson, B. D., Stämpfli, P., Seifritz, E., Repovs, G., Krystal, J. H., Murray, J. D., et al. (2018) · eLife · doi:10.7554/elife.35082 · Cited by 390
Comprehensive characterization of the Published Kinase Inhibitor Set
Elkins, J. M., Fedele, V., Szklarz, M., Abdul Azeez, K. R., Salah, E., Mikolajczyk, J., Romanov, S., Sepetov, N., Huang, X.-P., Roth, B. L., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3374 · Cited by 323
Self-citationThe 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
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
G-Protein–Coupled Receptors in Heart Disease
Wang, J., Gareri, C., & Rockman, H. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.311403 · Cited by 303
Psychedelics in Psychiatry: Neuroplastic, Immunomodulatory, and Neurotransmitter Mechanisms
Inserra, A., De Gregorio, D., & Gobbi, G. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000056 · Cited by 232
Duncan, A. L., Song, W., & Sansom, M. S. P. (2020) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010919-023411 · Cited by 158
Ligand-Dependent Modulation of G Protein Conformation Alters Drug Efficacy
Furness, S. G. B., Liang, Y.-L., Nowell, C. J., Halls, M. L., Wookey, P. J., Dal Maso, E., Inoue, A., Christopoulos, A., Wootten, D., & Sexton, P. M. (2016) · Cell · doi:10.1016/j.cell.2016.09.021 · Cited by 134
Discovery of new GPCR ligands to illuminate new biology
Roth, B. L., Irwin, J. J., & Shoichet, B. K. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2490 · Cited by 94
Self-citationFonin, 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
Roth, B. L., & Kroeze, W. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.654764 · Cited by 88
Self-citationG-protein–coupled receptors are dynamic regulators of digestion and targets for digestive diseases
Canals, M., Poole, D. P., Veldhuis, N. A., Schmidt, B. L., & Bunnett, N. W. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.01.266 · Cited by 35
Vuckovic, Z., Wang, J., Pham, V., Mobbs, J. I., Belousoff, M. J., Bhattarai, A., Burger, W. A., Thompson, G., Yeasmin, M., Nawaratne, V., et al. (2023) · eLife · doi:10.7554/elife.83477 · Cited by 34
Full and partial agonism of a designed enzyme switch
Budiardjo, S. J., Licknack, T. J., Cory, M. B., Kapros, D., Roy, A., Lovell, S., Douglas, J., & Karanicolas, J. (2016) · ACS Synthetic Biology · doi:10.1021/acssynbio.6b00097 · Cited by 13
Metadata
- Authors
- Wacker, D., Wang, C., Katritch, V., Han, G. W., Huang, X.-P., Vardy, E., McCorvy, J. D., Jiang, Y., Chu, M., Siu, F. Y., Liu, W., Xu, H. E., Cherezov, V., Roth, B. L., & Stevens, R. C.
- Venue
- Science
- Published
- 2013-05-03
- Volume
- 340
- Issue
- 6132
- Pages
- 615-619
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 664
- References
- 39
- Language
- en
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.