The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
The structure and function of G-protein-coupled receptors
Open accessAbstract
G-protein-coupled receptors (GPCRs) mediate most of our physiological responses to hormones, neurotransmitters and environmental stimulants, and so have great potential as therapeutic targets for a broad spectrum of diseases. They are also fascinating molecules from the perspective of membrane-protein structure and biology. Great progress has been made over the past three decades in understanding diverse GPCRs, from pharmacology to functional characterization in vivo. Recent high-resolution structural studies have provided insights into the molecular mechanisms of GPCR activation and constitutive activity.
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?
In the citing paper
“GPR20 belongs to the family of the G-protein-coupled receptors, which participate in intracellular second messenger systems triggered by different hormones and neurotransmitters, and amyloid β.53, 54, 55”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [54]
In the citing paper
“Both theoretical and experimental results do not offer any clear conclusions with respect to the vibrational theory of neurotransmission for adenosine, serotonin and histamine receptors and their related ligands.”
From Quantum effects in the brain: A review (2020) · cites this paper as [115]
In the citing paper
“Understanding the mechanism or mechanisms of ligand-GPCR interaction is particularly important due to the fact that GPCRs are a major drug target associated with one third of all pharmaceuticals 103,115 .”
From Quantum effects in the brain: A review (2020) · cites this paper as [115]
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
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
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
Self-citationBallesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001 · cited 1×
“48 (human β 2 AR, with Ballesteros/Weinstein numberin”
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 · cited 1×
“GPCRs in vertebrates are commonly divided into five families on the basis of their sequence and structural similarity”
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
Self-citationThe 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist
Jaakola, V., Griffith, M. T., Hanson, M. A., Cherezov, V., Chien, E. Y. T., Lane, J. R., IJzerman, A. P., & Stevens, R. C. (2008) · Science · doi:10.1126/science.1164772 · Cited by 1,786
Léan, A. D., Stadel, J. M., & Lefkowitz, R. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79672-9 · Cited by 1,606
Structure of a β1-adrenergic G-protein-coupled receptor
Warne, T., Serrano‐Vega, M. J., Baker, J. G., Moukhametzianov, R., Edwards, P. C., Henderson, R. A., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2008) · Nature · doi:10.1038/nature07101 · Cited by 1,377
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 1,335
Self-citationCloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
Dixon, R. A. F., Kobilka, B. K., Strader, D. J., Benovic, J., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., et al. (1986) · Nature · doi:10.1038/321075a0 · Cited by 1,275 · cited 1×
“The clustering of these residues in the cytoplasmic half of the transmembrane bundle reflects the basic conservation of mechanism across GPCRs, a remarkable structural affirmation of a hypothesis made more than 20 years ag”
Self-citationRequirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
Farrens, D., Altenbach, C., Yang, K., Hubbell, W. L., & Khorana, H. G. (1996) · Science · doi:10.1126/science.274.5288.768 · Cited by 1,179 · cited 1×
“This rigid-body movement is consistent with previous biophysical studies of both rhodopsi”
GPCRdb: an information system for G protein-coupled receptors
Ísberg, V., Mordalski, S., Munk, C., Rataj, K., Harpsøe, K., Hauser, A. S., Vroling, B., Bojarski, A. J., Vriend, G., & Gloriam, D. E. I. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1178 · Cited by 1,079
Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders
Jeffrey Conn, P., Christopoulos, A., & Lindsley, C. W. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2760 · Cited by 1,063 · cited 1×
“This high conservation in the ligand-binding pocket is also observed in other subfamilies of GPCRs (such as dopamine, serotonin and histamine), and probably explains some of the difficulty in obtaining potent subtype-selective compounds in pharmaceutical discovery program”
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 · cited 1×
“The recent structures of opsin provide clues to the transmembrane helix rearrangements that can be expected as a result of agonist bindin”
The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure
Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049
Hanson, M. A., Cherezov, V., Griffith, M. T., Roth, C., Jaakola, V., Chien, E. Y. T., Velasquez, J., Kühn, P., & Stevens, R. C. (2008) · Structure · doi:10.1016/j.str.2008.05.001 · Cited by 935
Crystal structure of the ligand-free G-protein-coupled receptor opsin
Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 908
Projection structure of rhodopsin
Schertler, G. F. X., Villa, C., & Henderson, R. A. (1993) · Nature · doi:10.1038/362770a0 · Cited by 766 · cited 1×
“The inactive states of four GPCRs The first insights into the structure of GPCRs came from two-dimensional crystals of rhodopsi”
β-Arrestin-dependent, G Protein-independent ERK1/2 Activation by the β2 Adrenergic Receptor
Shenoy, S. K., Drake, M. T., Nelson, C. D., Houtz, D. A., Xiao, K., Madabushi, S., Reiter, É., Premont, R. T., Lichtarge, O., & Lefkowitz, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506576200 · Cited by 758
Dark adaptation and the retinoid cycle of vision
Lamb, T. D., & Pugh, E. N. (2004) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2004.03.001 · Cited by 725 · cited 1×
“After photobleaching, rod photoreceptors exhibit residual activity that is presumed to result from basal activity of the unliganded state of rhodopsi”
Structure of Bovine Rhodopsin in a Trigonal Crystal Form
Li, J., Edwards, P. C., Burghammer, M. C., Villa, C., & Schertler, G. F. X. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.090 · Cited by 724
Conformational complexity of G-protein-coupled receptors
Kobilka, B. K., & Deupí, X. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.003 · Cited by 694 · cited 1×
“Rather, they are more like molecular rheostats, able to sample a continuum of conformations with relatively closely spaced energie”
Self-citationRoles of G‐protein‐coupled receptor dimerization
Terrillon, S., & Bouvier, M. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400052 · Cited by 684 · cited 1×
“These activities are further complicated by factors such as GPCR oligomerizatio”
Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography
Okada, T., Fujiyoshi, Y., Silow, M., Navarro, J., Landau, E. M., & Shichida, Y. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082666399 · Cited by 662
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 · cited 1×
“For β 2 AR, mutation of these residues increases constitutive activit”
Self-citationA unique mechanism of β-blocker action: Carvedilol stimulates β-arrestin signaling
Wisler, J. W., DeWire, S. M., Whalen, E. J., Violin, J. D., Drake, M. T., Ahn, S., Shenoy, S. K., & Lefkowitz, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707936104 · Cited by 612 · cited 1×
“In the extreme case, even opposite activities for different signalling pathways are observed: for β 2 AR, agonists for the arrestin/MAP kinase pathway are also inverse agonists for the classical Gαs/cAMP/PKA pathwa”
Regulation of GPCRs by Endocytic Membrane Trafficking and Its Potential Implications
Hanyaloglu, A. C., & von Zastrow, M. (2007) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094830 · Cited by 610 · cited 1×
“Similarly, the process of GPCR desensitization involves multiple pathways, including receptor phosphorylation events, arrestin-mediated internalization into endosomes, receptor recycling and lysosomal degradatio”
The selectivity of β‐adrenoceptor agonists at human β1‐, β2‐ and β3‐adrenoceptors
Baker, J. G. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00754.x · Cited by 591
The selectivity of β ‐adrenoceptor antagonists at the human β 1, β 2 and β 3 adrenoceptors
Baker, J. G. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706048 · Cited by 559
Strader, C. D., Sigal, I. S., Candelore, M. R., Rands, E., Hill, W. S., & Dixon, R. A. F. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81509-0 · Cited by 534
Identification of Two Serine Residues Involved in Agonist Activation of the β-Adrenergic Receptor
Strader, C. D., Candelore, M. R., Hill, W. S., Sigal, I. S., & Dixon, R. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80035-7 · Cited by 523
Azzi, M., Charest, P. G., Angers, S., Rousseau, G., Kohout, T. A., Bouvier, M., & Piñeyro, G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1936664100 · Cited by 522
Desensitization of G-protein-coupled Receptors
Xiao, Z., Yao, Y., Yu, L., & Devreotes, P. N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1440 · Cited by 521
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
Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
Salom, D., Lodowski, D. T., Stenkamp, R. E., Trong, I. L., Golczak, M., Jastrzebska, B., Harris, T., Ballesteros, J. A., & Palczewski, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608022103 · Cited by 442 · cited 1×
“The crystal structure of a photoactivated deprotonated intermediate of rhodopsi”
β2 Adrenergic Receptor Activation
Shi, L., Liapakis, G., Xu, R., Guarnieri, F., Ballesteros, J. A., & Javitch, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206801200 · Cited by 422
Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form
Serrano‐Vega, M. J., Magnani, F., Shibata, Y., & Tate, C. G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711253105 · Cited by 422
The evasive nature of drug efficacy: implications for drug discovery
Galandrin, S., Oligny-Longpré, G., & Bouvier, M. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.005 · Cited by 379 · cited 1×
“Many GPCRs can stimulate multiple signalling systems, and specific ligands can have different relative efficacies to different pathway”
Inverse agonist activity of beta-adrenergic antagonists.
Chidiac, P., Hébert, T. E., Valiquette, M., Dennis, M., & Bouvier, M. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10022-9 · Cited by 372
Ghanouni, P., Gryczynski, Z. K., Steenhuis, J. J., Lee, T. W., Farrens, D., Lakowicz, J. R., & Kobilka, B. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100162200 · Cited by 364
Self-citationHubbell, W. L., Altenbach, C., Hubbell, C., & Khorana, H. G. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)63010-x · Cited by 353
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
Self-citationSequential Binding of Agonists to the β2 Adrenoceptor
Swaminath, G., Xiang, Y. K., Lee, T. W., Steenhuis, J. J., Parnot, C., & Kobilka, B. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310888200 · Cited by 333
Self-citationGPCRDB information system for G protein-coupled receptors
Horn, F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg103 · Cited by 326
Faham, S., & Bowie, J. U. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5295 · Cited by 325
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
Self-citationStructure-based discovery of β 2 -adrenergic receptor ligands
Kolb, P., Rosenbaum, D. M., Irwin, J. J., Fung, J. J., Kobilka, B. K., & Shoichet, B. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812657106 · Cited by 291
Self-citationBond, R. A., & IJzerman, A. P. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.12.007 · Cited by 258 · cited 1×
“This observation is compatible with the findings that ligand-activated GPCRs generally have higher basal activity than rhodopsi”
Swaminath, G., Deupí, X., Lee, T. W., Zhu, W., Thian, F. S., Kobilka, T. S., & Kobilka, B. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502352200 · Cited by 257
Self-citationRecent Advances in Cardiac β2-Adrenergic Signal Transduction
Xiao, R., Cheng, H., Zhou, Y., Kuschel, M., & Lakatta, E. G. (1999) · Circulation Research · doi:10.1161/01.res.85.11.1092 · Cited by 244
Negative antagonists promote an inactive conformation of the beta 2-adrenergic receptor.
Samama, P., Pei, G., Costa, T., Cotecchia, S., & Lefkowitz, R. J. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10009-6 · Cited by 236
Crystal Structure of a Thermally Stable Rhodopsin Mutant
Standfuss, J., Xie, G., Edwards, P. C., Burghammer, M. C., Oprian, D. D., & Schertler, G. F. X. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.007 · Cited by 225
Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation
Ahuja, S., Horn̆ák, V., Yan, E. C. Y., Syrett, N., Goncalves, J. A., Hirshfeld, A., Ziliox, M., Sakmar, T. P., Sheves, M., Reeves, P. J., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1549 · Cited by 213 · cited 1×
“Recent solid-state nuclear magnetic resonance (NMR) studies provide evidence for conformational changes that disrupt a hydrogen-bond network between ECL2 and the extracellular ends of TM4, TM5 and TM6 in metarhodopsin II before the dissociation of retinal and the formation of opsi”
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
Rasmussen, S. G. F., Jensen, A. D., Liapakis, G., Ghanouni, P., Javitch, J. A., & Gether, U. (1999) · Molecular Pharmacology · doi:10.1124/mol.56.1.175 · Cited by 205
Self-citationOkada, T., Trong, I. L., Fox, B. A., Behnke, C. A., Stenkamp, R. E., & Palczewski, K. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4209 · Cited by 194
Desensitization of G protein-coupled receptors.
Freedman, N. J., & Lefkowitz, R. J. (1996) · PubMed · Cited by 190
Liapakis, G., Ballesteros, J. A., Papachristou, S., Chan, W. C., Chen, X., & Javitch, J. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002092200 · Cited by 181 · cited 1×
“One hypothesis is that the upper region of TM5, which contains several catechol-binding serine”
Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296
Cohen, G. B., Oprian, D. D., & Robinson, P. R. (1992) · Biochemistry · doi:10.1021/bi00165a008 · Cited by 170
Vogel, R., Mahalingam, M., Lüdeke, S., Huber, T., Siebert, F., & Sakmar, T. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.022 · Cited by 164 · cited 1×
“Conserved among all family A GPCRs, these amino acids form a network of polar interactions that bridges the two transmembrane helices, stabilizing the inactive-state conformatio”
Barak, L. S., Ménard, L., Ferguson, S. S. G., Colapietro, A.-M., & Caron, M. G. (1995) · Biochemistry · doi:10.1021/bi00047a003 · Cited by 156
Sequence of late molecular events in the activation of rhodopsin
Knierim, B., Hofmann, K. P., Ernst, O. P., & Hubbell, W. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710393104 · Cited by 135 · cited 1×
“Indeed, the possibility of a deprotonated intermediate of rhodopsin in an inactive conformation was directly demonstrated by kinetic electron paramagnetic resonance (EPR) measurement”
Caveolae and Lipid Rafts: G Protein‐Coupled Receptor Signaling Microdomains in Cardiac Myocytes
Insel, P. A., Head, B. P., Ostrom, R. S., Patel, H. H., Swaney, J. S., Tang, C., & Roth, D. M. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1341.015 · Cited by 132
A monoclonal antibody for G protein–coupled receptor crystallography
Day, P. W., Rasmussen, S. G. F., Parnot, C., Fung, J. J., Masood, A., Kobilka, T. S., Yao, X.-J., Choi, H., Weis, W. I., Rohrer, D. K., et al. (2007) · Nature Methods · doi:10.1038/nmeth1112 · Cited by 125
Self-citationPardo, L., Deupí, X., Dölker, N., López-Rodríguez, M. L., & Campillo, M. (2006) · ChemBioChem · doi:10.1002/cbic.200600429 · Cited by 120 · cited 1×
“Although this 'water pocket' network is presumed to stabilize the inactive state, the relative ease of breaking these weakly favourable solvent-mediated interactions probably allows for rapid toggling to the active state when an agonist bind”
Conformations of the Active and Inactive States of Opsin
Vogel, R., & Siebert, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105423200 · Cited by 108 · cited 1×
“On the basis of biochemical and infrared spectroscopic characterization, opsin at low pH is thought to be stabilized in an active state that resembles metarhodopsin I”
Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
Krebs, A., Villa, C., Edwards, P. C., & Schertler, G. F. X. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2070 · Cited by 97
Crystallization of bacteriorhodopsin from bicelle formulations at room temperature
Faham, S., Boulting, G. L., Massey, E. A., Yohannan, S., Yang, D. D., & Bowie, J. U. (2005) · Protein Science · doi:10.1110/ps.041167605 · Cited by 90
Werner, K., Richter, C. P., Klein‐Seetharaman, J., & Schwalbe, H. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9205-3 · Cited by 75 · cited 1×
“, respectively; however, the application of other methods, such as NMR spectroscopy, promises to greatly expand our knowledge of GPCR dynamic”
Adrenergic Receptors in the Heart
Hoffman, B. B., & Lefkowitz, R. J. (1982) · Annual Review of Physiology · doi:10.1146/annurev.ph.44.030182.002355 · Cited by 68 · cited 1×
“Recent advances in cardiac beta(2)-adrenergic signal transduction.”
Homology Modeling of G-Protein-Coupled Receptors and Implications in Drug Design
Patny, A., Desai, P. V., & Avery, M. A. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706777442002 · Cited by 67 · cited 1×
“Until recently, pictures of three-dimensional drug–receptor interactions could only be provided through speculative homology models based on rhodopsi”
Jiang, Q., Lee, B. X., Glashofer, M., van Rhee, A. M., & Jacobson, K. A. (1997) · Journal of Medicinal Chemistry · doi:10.1021/jm970084v · Cited by 66 · cited 1×
“Mutations at this precise region of TM3, analogous to an essential position for agonist-binding in β 2 AR and β 1 AR, have been shown to decrease agonist affinity to the A 2A recepto”
Sugimoto, Y., Fujisawa, R., Tanimura, R., Lattion, A.-L., Cotecchia, S., Tsujimoto, G., Nagao, T., & Kurose, H. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.301.1.51 · Cited by 15
Cited by
Sorted by citations
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
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 1,709
Self-citationMolecular 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 1,534
The coming of age of de novo protein design
Huang, P.-S., Boyken, S. E., & Baker, D. (2016) · Nature · doi:10.1038/nature19946 · Cited by 1,478
Fredholm, B. B., IJzerman, A. P., Jacobson, K. A., Linden, J. M., & Müller, C. E. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003285 · Cited by 1,307
Metadata
- Authors
- Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K.
- Affiliations
- Stanford Medicine (US)
- Venue
- Nature
- Published
- 2009-05
- Volume
- 459
- Issue
- 7245
- Pages
- 356-363
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3967846
- OpenAlex
- W1988097700
- Cited by
- 2,534
- References
- 73
- Citations by year
- 2026: 108 · 2025: 171 · 2024: 175 · 2023: 140 · 2022: 196 · 2021: 177 · 2020: 150 · 2019: 172 · 2018: 122 · 2017: 136 · 2016: 132 · 2015: 120 · 2014: 133 · 2013: 135 · 2012: 146
- FWCI
- 11.79
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Lundbeckfonden (R19-2008-2113)
- National Institute of General Medical Sciences (F32GM082028, R01GM083118)
- National Institute of Neurological Disorders and Stroke (R01NS28471, R01NS028471)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- G protein-coupled receptors, GPCR structure, GPCR activation, constitutive activity, membrane protein structure, therapeutic target, hormone signaling, neurotransmitter signaling
- MeSH terms
- Animals, Cytoplasm, Humans, Protein Conformation, Signal Transduction, Conserved Sequence, Receptors, G-Protein-Coupled, Opsins
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
