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.
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
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?
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.
“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]
Theoretical and experimental results do not offer clear conclusions about the vibrational theory of neurotransmission for adenosine, serotonin, and histamine receptors and their related ligands.
“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]
GPCRs are a major drug target associated with one third of all pharmaceuticals.
“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.
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 · 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
Self-citationBallesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001 · cited 1× · see citing works
“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× · see citing works
“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 · see citing works
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 · see citing works
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
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 1,345 · 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
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× · see citing works
“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× · see citing works
“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 1,067 · see citing works
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× · see citing works
“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× · see citing works
“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 · see citing works
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 · see citing works
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 903 · see citing works
Projection structure of rhodopsin
Schertler, G. F. X., Villa, C., & Henderson, R. A. (1993) · Nature · doi:10.1038/362770a0 · Cited by 766 · cited 1× · see citing works
“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 · see citing works
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× · see citing works
“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 · see citing works
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× · see citing works
“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× · see citing works
“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 · see citing works
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× · see citing works
“For β 2 AR, mutation of these residues increases constitutive activit”
Self-citationRegulation 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× · see citing works
“Similarly, the process of GPCR desensitization involves multiple pathways, including receptor phosphorylation events, arrestin-mediated internalization into endosomes, receptor recycling and lysosomal degradatio”
A 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 598 · cited 1× · see citing works
“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”
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 · see citing works
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 542 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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
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× · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
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 364 · cited 1× · see citing works
“Many GPCRs can stimulate multiple signalling systems, and specific ligands can have different relative efficacies to different pathway”
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 · see citing works
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 · 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
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 · see citing works
Self-citationGPCRDB information system for G protein-coupled receptors
Horn, F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg103 · Cited by 326 · see citing works
Faham, S., & Bowie, J. U. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5295 · Cited by 325 · see citing works
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
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 288 · see citing works
Self-citationSwaminath, 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 · see citing works
Self-citationBond, R. A., & IJzerman, A. P. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.12.007 · Cited by 251 · cited 1× · see citing works
“This observation is compatible with the findings that ligand-activated GPCRs generally have higher basal activity than rhodopsi”
Recent 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 · see citing works
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 · see citing works
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 · see citing works
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× · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
Desensitization of G protein-coupled receptors.
Freedman, N. J., & Lefkowitz, R. J. (1996) · PubMed · Cited by 190 · see citing works
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× · see citing works
“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 · see citing works
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× · see citing works
“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 · see citing works
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× · see citing works
“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 · see citing works
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 · see citing works
Self-citationPardo, L., Deupí, X., Dölker, N., López-Rodríguez, M. L., & Campillo, M. (2006) · ChemBioChem · doi:10.1002/cbic.200600429 · Cited by 121 · cited 1× · see citing works
“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 105 · cited 1× · see citing works
“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 · see citing works
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 · see citing works
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× · see citing works
“, 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× · see citing works
“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× · see citing works
“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× · see citing works
“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 · see citing works
Flagged first, then by citations
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 · 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 1,682 · see citing works
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 1,502 · see citing works
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 · see citing works
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 · see citing works
Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms
Ernst, O. P., Lodowski, D. T., Elstner, M., Hegemann, P., Brown, L. S., & Kandori, H. (2013) · Chemical Reviews · doi:10.1021/cr4003769 · Cited by 1,140 · see citing works
Structural basis of Wnt recognition by Frizzled
Janda, C. Y., Waghray, D., Levin, A. M., Thomas, C., & Garcia, K. (2012) · Science · doi:10.1126/science.1222879 · Cited by 880 · 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
Neuropeptide Transmission in Brain Circuits
van den Pol, A. N. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.014 · Cited by 810 · see citing works
Smoothened Mutation Confers Resistance to a Hedgehog Pathway Inhibitor in Medulloblastoma
Yauch, R. L., Dijkgraaf, G. J. P., Alicke, B., Januario, T., Ahn, C. P., Holcomb, T., Pujara, K., Stinson, J., Callahan, C. A., Tang, T. T.-L., et al. (2009) · Science · doi:10.1126/science.1179386 · Cited by 841 · see citing works
GPCR Dynamics: Structures in Motion
Latorraca, N. R., Venkatakrishnan, A., & Dror, R. O. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00177 · Cited by 843 · 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
Self-citationPaur, H., Wright, P., Sikkel, M. B., Tranter, M. H., Mansfield, C. A., O’Gara, P., Stuckey, D. J., Nikolaev, V. O., Diakonov, I. A., Pannell, L., et al. (2012) · Circulation · doi:10.1161/circulationaha.112.111591 · Cited by 770 · 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
Self-citationPathway and mechanism of drug binding to G-protein-coupled receptors
Dror, R. O., Pan, A. C., Arlow, D. H., Borhani, D. W., Maragakis, P., Shan, Y., Xu, H., & Shaw, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104614108 · Cited by 737 · 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
Common activation mechanism of class A GPCRs
Zhou, Q., Yang, D.-H., Wu, M., Guo, Y., Guo, W.-J., Zhong, L., Cai, X.-Q., Dai, A., Jang, W., Shakhnovich, E., et al. (2019) · eLife · doi:10.7554/elife.50279 · Cited by 491 · 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
Design and Applications of Water-Soluble Coordination Cages
Percástegui, E. G., Ronson, T. K., & Nitschke, J. R. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00672 · Cited by 592 · see citing works
The emerging mutational landscape of G proteins and G-protein-coupled receptors in cancer
O’Hayre, M., Vázquez‐Prado, J., Kufareva, I., Stawiski, E. W., Handel, T. M., Seshagiri, S., & Gutkind, J. S. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3521 · Cited by 559 · see citing works
Structure and functional expression of the cloned rat neurotensin receptor
Tanaka, K., Masu, M., & Nakanishi, S. (1990) · Neuron · doi:10.1016/0896-6273(90)90137-5 · Cited by 537 · see citing works
The Melanocortin-4 Receptor: Physiology, Pharmacology, and Pathophysiology
Tao, Y.-X. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0037 · Cited by 531 · see citing works
Visualization of arrestin recruitment by a G-protein-coupled receptor
Shukla, A. K., Westfield, G., Xiao, K., Reis, R. I., Huang, L.-Y., Tripathi‐Shukla, P., Qian, J. X., Li, S., Blanc, A., Oleskie, A. N., et al. (2014) · Nature · doi:10.1038/nature13430 · Cited by 510 · see citing works
Self-citationG 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
Molecular control of δ-opioid receptor signalling
Fenalti, G., Giguère, P. M., Katritch, V., Huang, X., Thompson, A. A., Cherezov, V., Roth, B. L., & Stevens, R. C. (2014) · Nature · doi:10.1038/nature12944 · Cited by 501 · see citing works
Regulation, signaling, and physiological functions of G-Proteins
Syrovatkina, V., Alegre, K. O., Dey, R., & Huang, X.-Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.002 · Cited by 498 · see citing works
Patching, S. G. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.028 · Cited by 465 · see citing works
Chae, P. S., Rasmussen, S. G. F., Rana, R. R., Gotfryd, K., Chandra, R., Goren, M. A., Kruse, A. C., Nurva, S., Loland, C. J., Pierre, Y., et al. (2010) · Nature Methods · doi:10.1038/nmeth.1526 · Cited by 460 · see citing works
Self-citationStructure of the chemokine receptor CXCR1 in phospholipid bilayers
Park, S. H., Das, B. B., Casagrande, F., Tian, Y., Nothnagel, H. J., Chu, M., Kiefer, H., Maier, K., Angelis, A. A. D., Marassi, F. M., et al. (2012) · Nature · doi:10.1038/nature11580 · Cited by 459 · see citing works
Cell-cell communication: New insights and clinical implications
Su, J., Song, Y., Zhu, Z., Huang, X., Fan, J., Qiao, J., & Mao, F. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01888-z · Cited by 433 · see citing works
Structure of class B GPCR corticotropin-releasing factor receptor 1
Hollenstein, K., Kean, J., Bortolato, A., Cheng, R. K. Y., Dore, A. S., Jazayeri, A., Cooke, R. M., Weir, M., & Marshall, F. H. (2013) · Nature · doi:10.1038/nature12357 · Cited by 417 · see citing works
An Approach to Spatiotemporally Resolve Protein Interaction Networks in Living Cells
Lobingier, B. T., Hüttenhain, R., Eichel, K., Miller, K. B., Ting, A. Y., von Zastrow, M., & Krogan, N. J. (2017) · Cell · doi:10.1016/j.cell.2017.03.022 · Cited by 401 · see citing works
Structure of class C GPCR metabotropic glutamate receptor 5 transmembrane domain
Dore, A. S., Okrasa, K., Patel, J. C., Serrano‐Vega, M. J., Bennett, K. A., Cooke, R. M., Errey, J. C., Jazayeri, A., Khan, S. A., Tehan, B. G., et al. (2014) · Nature · doi:10.1038/nature13396 · Cited by 410 · see citing works
A G protein-coupled receptor at work: the rhodopsin model
Hofmann, K. P., Scheerer, P., Hildebrand, P. W., Choe, H.-W., Park, J. H., Heck, M., & Ernst, O. P. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.005 · Cited by 376 · 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
A meta-analysis of genome-wide association studies identifies multiple longevity genes
Deelen, J., Evans, D. S., Arking, D. E., Tesi, N., Nygaard, M., Liu, X., Wojczynski, M. K., Biggs, M. L., van der Spek, A., Atzmon, G., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11558-2 · Cited by 370 · see citing works
Dijkgraaf, G. J. P., Alicke, B., Weinmann, L., Januario, T., West, K. A., Modrusan, Z. D., Burdick, D., Goldsmith, R. A., Robarge, K. D., Sutherlin, D., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2876 · Cited by 365 · see citing works
The unfolding stories of GPR30, a new membrane-bound estrogen receptor
Maggiolini, M., & Picard, D. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0242 · Cited by 360 · see citing works
Tryptophan Biochemistry: Structural, Nutritional, Metabolic, and Medical Aspects in Humans
Palego, L., Betti, L., Rossi, A., & Giannaccini, G. (2016) · Journal of Amino Acids · doi:10.1155/2016/8952520 · Cited by 349 · see citing works
Drugging Membrane Protein Interactions
Yin, H. H., & Flynn, A. D. (2016) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-092115-025322 · Cited by 342 · see citing works
Understanding the Molecular Mechanisms of the Interplay Between Herbal Medicines and Gut Microbiota
Xu, J., Chen, H., & Li, S. (2017) · Medicinal Research Reviews · doi:10.1002/med.21431 · Cited by 340 · see citing works
Chemically Fueled Self‐Assembly in Biology and Chemistry
Das, K., Gabrielli, L., & Prins, L. J. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202100274 · Cited by 338 · see citing works
Mini-G proteins: Novel tools for studying GPCRs in their active conformation
Nehmé, R., Carpenter, B., Singhal, A., Strege, A., Edwards, P. C., White, C. F., Du, H., Grisshammer, R., & Tate, C. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175642 · Cited by 326 · see citing works
Ho, Y.-H., del Toro, R., Rivera-Torres, J., Rak, J., Korn, C., García-García, A., Macías, D., González-Gómez, C., del Monte, A., Wittner, M., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2019.06.007 · Cited by 315 · see citing works
“Whereas both b-ARs can activate G proteins (Rosenbaum et al., 2009), their differential cardiovascular effects have been attributed to b3-AR-dependent nitric oxide (NO) generation (Gauthier et al.”
BackgroundFribourg, M., Moreno, J. L., Holloway, T., Provasi, D., Baki, L., Mahajan, R., Park, G., Adney, S. K., Hatcher, C., Eltit, J. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.055 · Cited by 311 · see citing works
Lohse, M. J., Nuber, S., & Hoffmann, C. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004309 · Cited by 306 · 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
Li, J., Seidlitz, J., John Suckling, A., Fan, F., Ji, G., Meng, Y., Yang, S., Wang, K., Qiu, J., Chen, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21943-5 · Cited by 316 · see citing works
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 · see citing works
Hallucinogens and Serotonin 5-HT2A Receptor-Mediated Signaling Pathways
López‐Giménez, J. F., & González‐Maeso, J. (2017) · Current topics in behavioral neurosciences · doi:10.1007/7854_2017_478 · Cited by 311 · see citing works
Novel insights into G protein and G protein-coupled receptor signaling in cancer
O’Hayre, M., Degese, M. S., & Gutkind, J. S. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.01.005 · Cited by 296 · see citing works
Signal transduction by protease‐activated receptors
Soh, U. J. K., Dores, M. R., Chen, B., & Trejo, J. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00705.x · Cited by 294 · see citing works
Yan, E. C. Y., Fu, L., Wang, Z., & Liu, W. (2014) · Chemical Reviews · doi:10.1021/cr4006044 · Cited by 291 · see citing works
Structural basis for nucleotide exchange in heterotrimeric G proteins
Dror, R. O., Mildorf, T. J., Hilger, D., Manglik, A., Borhani, D. W., Arlow, D. H., Philippsen, A., Villanueva, N., Yang, Z., Lerch, M. T., et al. (2015) · Science · doi:10.1126/science.aaa5264 · Cited by 292 · see citing works
Self-citationMolecular Pathways: Targeting the CXCR4–CXCL12 Axis—Untapped Potential in the Tumor Microenvironment
Scala, S. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0914 · Cited by 292 · 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
Improved tools to study astrocytes
Yu, X., Nagai, J., & Khakh, B. S. (2020) · Nature Reviews Neuroscience · doi:10.1038/s41583-020-0264-8 · Cited by 298 · see citing works
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282 · see citing works
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures
Shimada, I., Ueda, T., Kofuku, Y., Eddy, M. T., & Wüthrich, K. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.180 · Cited by 282 · see citing works
Biologics vs. small molecules: Drug costs and patient access
Makurvet, F. D. (2020) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2020.100075 · Cited by 274 · 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
The circadian clock in cancer development and therapy
Fu, L., & Kettner, N. M. (2013) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-396971-2.00009-9 · Cited by 251 · see citing works
Regulation of immune responses by tuft cells
Schneider, C., O’Leary, C. E., & Locksley, R. M. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0176-x · Cited by 260 · see citing works
Prossnitz, E. R., & Arterburn, J. B. (2015) · Pharmacological Reviews · doi:10.1124/pr.114.009712 · Cited by 263 · see citing works
“Gurevich EV, Tesmer JJ, Mushegian A, and Gurevich VV (2012) G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacol Ther 133:40–69.”
BackgroundInfluentialChemoenzymatic Semisynthesis of Proteins
Thompson, R. E., & Muir, T. W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00450 · Cited by 245 · see citing works
Wootten, D. L., Simms, J., Miller, L. J., Christopoulos, A., & Sexton, P. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221585110 · Cited by 249 · see citing works
Dimers and beyond: The functional puzzles of class C GPCRs
Kniazeff, J., Prézeau, L., Rondard, P., Pin, J., & Goudet, C. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.01.006 · Cited by 248 · see citing works
Subcellular Organization of GPCR Signaling
Eichel, K., & von Zastrow, M. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.11.009 · Cited by 250 · see citing works
Biased Signaling of Protease-Activated Receptors
Zhao, P., Metcalf, M. D., & Bunnett, N. W. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00067 · Cited by 249 · 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
Membrane protein structure determination — The next generation
Moraes, I., Evans, G., Sánchez-Weatherby, J., Newstead, S. L., & Stewart, P. D. S. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.07.010 · Cited by 242 · see citing works
G Protein-Coupled Receptors in Taste Physiology and Pharmacology
Ahmad, R., & Dalziel, J. E. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.587664 · Cited by 241 · see citing works
“neurotransmission, metabolism, cellular differentiation, inflammation and immune responses (Lagerström and Schiöth, 2008; Rosenbaum et al., 2009; Venkatakrishnan et al., 2013; Ahmad et al., 2015).”
BackgroundInfluentialA Global Map of Lipid-Binding Proteins and Their Ligandability in Cells
Niphakis, M. J., Lum, K. M., Cognetta, A. B., Correia, B. E., Ichu, T.-A., Olucha, J., Brown, S. J., Kundu, S., Piscitelli, F., Rosen, H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.05.045 · Cited by 239 · see citing works
Lee, L. C., & Lo, K. K. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00629 · Cited by 248 · see citing works
Drug repositioning by structure-based virtual screening
Ma, D., Chan, D. S., & Leung, C. (2013) · Chemical Society Reviews · doi:10.1039/c2cs35357a · Cited by 234 · see citing works
Conducting Nanomaterial Sensor Using Natural Receptors
Kwon, O. S., Song, H. S., Park, T. H., & Jang, J. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00159 · Cited by 223 · 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
Catalytic activation of β-arrestin by GPCRs
Eichel, K., Jullié, D., Barsi‐Rhyne, B., Latorraca, N. R., Masureel, M., Sibarita, J., Dror, R. O., & von Zastrow, M. (2018) · Nature · doi:10.1038/s41586-018-0079-1 · Cited by 217 · see citing works
Role of Short Chain Fatty Acid Receptors in Intestinal Physiology and Pathophysiology
Priyadarshini, M., Kumar, K. U., Dudeja, P. K., & Layden, B. T. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170050 · Cited by 272 · see citing works
Progress in Structure Based Drug Design for G Protein-Coupled Receptors
Congreve, M., LANGMEAD, C. J., Mason, J. S., & Marshall, F. H. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200371q · Cited by 213 · see citing works
Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor
Eddy, M. T., Lee, M.-Y., Gao, Z., White, K. L., Didenko, T., Horst, R., Audet, M., Stańczak, P., McClary, K. M., Han, G. W., et al. (2017) · Cell · doi:10.1016/j.cell.2017.12.004 · Cited by 212 · see citing works
Regulation of CaV2 calcium channels by G protein coupled receptors
Zamponi, G. W., & Currie, K. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.10.004 · Cited by 207 · see citing works
Lessons from the lysozyme of phage T4
Baase, W. A., Liu, L., Tronrud, D. E., & Matthews, B. W. (2010) · Protein Science · doi:10.1002/pro.344 · Cited by 199 · see citing works
de Graaf, C., Kooistra, A. J., Vischer, H. F., Katritch, V., Kuijer, M., Shiroishi, M., Iwata, S., Shimamura, T., Stevens, R. C., de Esch, I. J. P., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2011589 · Cited by 205 · see citing works
Krishnan, A., Almén, M. S., Fredriksson, R., & Schiöth, H. B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029817 · Cited by 204 · see citing works
Heng, B. C., Aubel, D., & Fussenegger, M. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2013.08.017 · Cited by 204 · see citing works
“As the most prolific superfamily of cell-membrane proteins, with approximately 800 members, GPCRs modulate diverse cellular responses to themajority of neurotransmitters and hormones within the human body (Rosenbaum et al., 2009).”
BackgroundSelenium/tellurium containing polymer materials in nanobiotechnology
Cao, W., Wang, L., & Xu, H. (2015) · Nano Today · doi:10.1016/j.nantod.2015.11.004 · Cited by 204 · see citing works
The crown-of-thorns starfish genome as a guide for biocontrol of this coral reef pest
Hall, M. R., Kocot, K. M., Baughman, K. W., Fernández-Valverde, S. L., Gauthier, M. E. A., Hatleberg, W. L., Krishnan, A., McDougall, C., Motti, C. A., Shoguchi, E., et al. (2017) · Nature · doi:10.1038/nature22033 · Cited by 199 · see citing works
“Many of the approximately 750 COTS rhodopsin-class GPCRs—the class comprising chemoreceptors 23 —are organized in species-specific tandem arrays of unique, single exon genes, akin to putative olfactory receptors in other deuterostomes 21,22 (Fig.”
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
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
Considerations in the Development of Reversibly Binding PET Radioligands for Brain Imaging
Pike, V. W. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666160418114826 · Cited by 197 · see citing works
Membrane Cholesterol in the Function and Organization of G-Protein Coupled Receptors
Paila, Y. D., & Chattopadhyay, A. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-8622-8_16 · Cited by 195 · see citing works
de Mendoza, A., Sebé-Pedrós, A., & Ruiz‐Trillo, I. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu038 · Cited by 194 · see citing works
“6(3):606–619. doi:10.1093/gbe/evu038 Advance Access publication February 23, 2014 from developmental control, such as cell growth, migration, density sensing, or neurotransmission (Bockaert and Pin 1999; Pierce et al. 2002; Rosenbaum et al. 2009).”
BackgroundInfluentialStructure and hydration of membranes embedded with voltage-sensing domains
Krepkiy, D. V., Mihailescu, M., Freites, J. A., Schow, E. V., Worcester, D. L., Gawrisch, K., Tobias, D. J., White, S. H., & Swartz, K. J. (2009) · Nature · doi:10.1038/nature08542 · Cited by 193 · see citing works
Horzmann, K. A., & Freeman, J. L. (2016) · Toxics · doi:10.3390/toxics4030019 · Cited by 163 · see citing works
Structural biology of glycoprotein hormones and their receptors: Insights to signaling
Jiang, X., Dias, J. A., & He, X. L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.08.021 · Cited by 186 · see citing works
CHARMM-GUI Membrane Builder : Past, Current, and Future Developments and Applications
Feng, S., Park, S., Choi, Y. K., & Im, W. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c01246 · Cited by 193 · see citing works
Structural requirements of bitter taste receptor activation
Brockhoff, A., Behrens, M., Niv, M. Y., & Meyerhof, W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913862107 · Cited by 185 · see citing works
Buddingh', B. C., Elzinga, J., & van Hest, J. V. (2020) · Nature Communications · doi:10.1038/s41467-020-15482-8 · Cited by 145 · see citing works
Wu, V. H., Yeerna, H., Nohata, N., Chiou, J., Harismendy, O., Raimondi, F., Inoue, A., Russell, R. B., Tamayo, P., & Gutkind, J. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.005601 · Cited by 176 · see citing works
“This includes frequent mutations in the DRY arginine motif, which is as important for class A GPCR activation as it is responsible for the intramolecular polar contacts that keep the receptor inactive until ligand binding (81).”
Background
- 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
