Cited by 2,534Receptor Mechanisms and SignalingProtein Kinase Regulation and GTPase SignalingNeuroscience and Neuropharmacology Research

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 access

Rosenbaum, Daniel M., Rasmussen, Søren G. F., Kobilka, Brian K.·2009·Nature

DOI 10.1038/nature08144PMC PMC3967846

Open this paper in CoChat — free account

Abstract

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

Crossref · 10.1038/nature08144

Cites

73 of 73 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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-citation
[19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
Ballesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001 · cited 1×
“48 (human β 2 AR, with Ballesteros/Weinstein numberin”
The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints
Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941 · 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-citation
The 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
A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor.
Léan, A. D., Stadel, J. M., & Lefkowitz, R. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79672-9 · Cited by 1,606
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-citation
Cloning 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-citation

Flagged first, then by citations

Show all 73 references

Sorted by citations

Items 401–500 of 1,002

Minireview: Toward the Establishment of a Link between Melatonin and Glucose Homeostasis: Association of Melatonin MT2Receptor Variants with Type 2 Diabetes
Karamitri, A., Renault, N., Clément, N., Guillaume, J., & Jockers, R. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1101 · Cited by 63
Molecular pathways of oestrogen receptors and β‐adrenergic receptors in cardiac cells: Recognition of their similarities, interactions and therapeutic value
Machuki, J. O., Zhang, H., Harding, S. E., & Sun, H. (2017) · Acta Physiologica · doi:10.1111/apha.12978 · Cited by 61
Structural insights into melatonin receptors
Stauch, B., Johansson, L. C., & Cherezov, V. (2019) · FEBS Journal · doi:10.1111/febs.15128 · Cited by 61
Host plant adaptation in the polyphagous whitefly, Trialeurodes vaporariorum, is associated with transcriptional plasticity and altered sensitivity to insecticides
Pym, A., Singh, K. S., Nordgren, Ã., Davies, T. G. E., Zimmer, C. T., Eliáš, J., Slater, R., & Bass, C. (2019) · BMC Genomics · doi:10.1186/s12864-019-6397-3 · Cited by 64
“G-protein-coupled receptors or GPCRs are the largest family of membrane proteins, responsible for cellular responses to hormones and neurotransmitters [58].”
Background
Can Specific Protein-Lipid Interactions Stabilize an Active State of the Beta 2 Adrenergic Receptor?
Neale, C., Herce, H. D., Pomès, R., & Garcı́a, A. E. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.08.028 · Cited by 62
Endothelial dysfunction: mechanisms and contribution to diseases
Ajoolabady, A., Praticò, D., & Ren, J. T. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01295-8 · Cited by 65
“GPCRs are integrated proteins of the plasma membrane of ECs, which can be activated by various stimuli such as hormones, neurotransmitters, and chemoattractants to transduce their message into intracellular signaling pathways in ECs [36, 37].”
A Triple Arg Motif Mediates α2 B‐Adrenergi c Receptor Interaction with Sec 24 C /D and Export
Dong, C., Nichols, C. D., Guo, J., Huang, W. Y., Lambert, N. A., & Wu, G. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01351.x · Cited by 61
Ligand-Steered Modeling and Docking: A Benchmarking Study in Class A G-Protein-Coupled Receptors
Phatak, S. S., Gatica, E. A., & Cavasotto, C. N. (2010) · Journal of Chemical Information and Modeling · doi:10.1021/ci100285f · Cited by 59
Functional properties of cell-free expressed human endothelin A and endothelin B receptors in artificial membrane environments
Proverbio, D., Roos, C., Beyermann, M., Orbán, E., Dötsch, V., & Bernhard, F. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.05.031 · Cited by 60
Structure of metabotropic glutamate receptor C-terminal domains in contact with interacting proteins
Enz, R. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00052 · Cited by 63
Rab8 Interacts with Distinct Motifs in α2B- and β2-Adrenergic Receptors and Differentially Modulates Their Transport
Dong, C., Yang, L., Zhang, X., Gu, H., Lam, M. L., Claycomb, W. C., Xia, H., & Wu, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081521 · Cited by 62
Regeneration and rewiring of rodent olfactory sensory neurons
Yu, C. R., & Wu, Y. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.06.001 · Cited by 60
“The ORs are intrinsically active, even without ligands (Rosenbaum et al., 2009; Reisert, 2010; Nakashima et al., 2013).”
Background
Contribution of heteromerization to G protein-coupled receptor function
Gaitonde, S. A., & González‐Maeso, J. (2016) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2016.10.006 · Cited by 59
Detection of Pathways Affected by Positive Selection in Primate Lineages Ancestral to Humans
Daub, J. T., Moretti, S., Davydov, I. I., Excoffier, L., & Robinson‐Rechavi, M. (2017) · Molecular Biology and Evolution · doi:10.1093/molbev/msx083 · Cited by 65
Recognition in the Face of Diversity: Interactions of Heterotrimeric G proteins and G Protein-coupled Receptor (GPCR) Kinases with Activated GPCRs
Huang, C.-C., & Tesmer, J. J. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.051847 · Cited by 61
Emerging Role of Surface Plasmon Resonance in Fragment-Based Drug Discovery
Navratilova, I. H., & Hopkins, A. L. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.128 · Cited by 58
Control of Intracellular Calcium Signaling as a Neuroprotective Strategy
Duncan, R. S., Goad, D. L., Grillo, M. A., Kaja, S., Payne, A. J., & Koulen, P. (2010) · Molecules · doi:10.3390/molecules15031168 · Cited by 59
Nanobodies detecting and modulating GPCRs outside in and inside out
Heukers, R., Groof, T. W. M. D., & Smit, M. J. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.01.003 · Cited by 61
Role of GPCR signaling and calcium dysregulation in Alzheimer's disease
Sushma, & Mondal, A. C. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103414 · Cited by 56
Selective activation of Gαob by an adenosine A1 receptor agonist elicits analgesia without cardiorespiratory depression
Wall, M. J., Hill, E., Huckstepp, R. T. R., Barkan, K., Deganutti, G., Leuenberger, M., Preti, B., Winfield, I. J., Carvalho, S., Suchankova, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31652-2 · Cited by 60
Mapping the intramolecular signal transduction of G‐protein coupled receptors
Lee, Y., Choi, S., & Hyeon, C. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24451 · Cited by 55
The roles played by highly truncated splice variants of G protein-coupled receptors
Wise, H. M. (2012) · Journal of Molecular Signaling · doi:10.1186/1750-2187-7-13 · Cited by 57
17β-Estradiol on the Expression of G-Protein Coupled Estrogen Receptor (GPER/GPR30) Mitophagy, and the PI3K/Akt Signaling Pathway in ATDC5 Chondrocytes In Vitro
Fan, D., Yang, X., Li, Y., & Guo, L. (2018) · Medical Science Monitor · doi:10.12659/msm.909365 · Cited by 59
G protein-regulated endocytic trafficking of adenylyl cyclase type 9
Lazar, A. M., Irannejad, R., Baldwin, T. A., Sundaram, A. A., Gutkind, J. S., Inoue, A., DESSAUER, C. W., & von Zastrow, M. (2020) · eLife · doi:10.7554/elife.58039 · Cited by 62
“The beta-2 adrenergic receptor (b2AR) provides a clear example, and is generally considered a model for the GPCR family more broadly (Lefkowitz, 2007; Rosenbaum et al., 2009).”
Background
Minireview: Role of Intracellular Scaffolding Proteins in the Regulation of Endocrine G Protein-Coupled Receptor Signaling
Walther, C., & Ferguson, S. S. G. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1091 · Cited by 58
The pyrokinin/ pheromone biosynthesis‐activating neuropeptide (PBAN) family of peptides and their receptors in Insecta: evolutionary trace indicates potential receptor ligand‐binding domains
Jurenka, R. A., & Nusawardani, T. (2010) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2010.01065.x · Cited by 57
N-Linked Glycosylation of Protease-activated Receptor-1 Second Extracellular Loop
Soto, A. G., & Trejo, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.111088 · Cited by 57
A Non-Mammalian Type Opsin 5 Functions Dually in the Photoreceptive and Non-Photoreceptive Organs of Birds
Ohuchi, H., Yamashita, T., Tomonari, S., Fujita-Yanagibayashi, S., Sakai, K., Noji, S., & Shichida, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031534 · Cited by 56
Covalent Molecular Probes for Class A G Protein-Coupled Receptors: Advances and Applications
Weichert, D., & Gmeiner, P. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00070 · Cited by 59
Structure-Based Design of Highly Selective and Potent G Protein-Coupled Receptor Kinase 2 Inhibitors Based on Paroxetine
Waldschmidt, H. V., Homan, K. T., Cato, M. C., Cruz-Rodríguez, O., Cannavò, A., Wilson, M. W., Song, J., Cheung, J. Y., Koch, W. J., Tesmer, J. J. G., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00112 · Cited by 57
The essential role of G protein-coupled receptor (GPCR) signaling in regulating T cell immunity
Wang, D. (2018) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2018.1434792 · Cited by 57
Solid-state 2 H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
Владимирович, С. А., Salgado, G. F. J., & Brown, M. F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014692108 · Cited by 57
Regulation of Smoothened Phosphorylation and High-Level Hedgehog Signaling Activity by a Plasma Membrane Associated Kinase
Li, S., Li, S., Han, Y., Tong, C., Wang, B., Chen, Y., & Jiang, J. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002481 · Cited by 60
Molecular Basis of the Extracellular Ligands Mediated Signaling by the Calcium Sensing Receptor
Zhang, C., Miller, C. L., Gorkhali, R., Zou, J., Huang, K., Brown, E. M., & Yang, J. J. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00441 · Cited by 59
The anatomy of mammalian sweet taste receptors
Chéron, J.-B., Golebiowski, J., Antonczak, S., & Fiorucci, S. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25228 · Cited by 56
Mechanical signaling through the discoidin domain receptor 1 plays a central role in tissue fibrosis
Coelho, N. M., & McCulloch, C. A. (2018) · Cell Adhesion & Migration · doi:10.1080/19336918.2018.1448353 · Cited by 59
β-Arrestin Recruitment and G Protein Signaling by the Atypical Human Chemokine Decoy Receptor CCX-CKR
Watts, A. O., Verkaar, F., van der Lee, M. M. C., Timmerman, C. A. W., Kuijer, M., van Offenbeek, J., van Lith, L. H. C. J., Smit, M. J., Leurs, R., Zaman, G. J. R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.406108 · Cited by 55
Subtype-dependent regulation of Gβγ signalling
Tennakoon, M., Senarath, K., Kankanamge, D., Ratnayake, K., Wijayaratna, D., Olupothage, K., Ubeysinghe, S., Martins-Cannavino, K., Hébert, T. E., & Karunarathne, A. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109947 · Cited by 49
Succinate receptor GPR91, a Gα i coupled receptor that increases intracellular calcium concentrations through PLCβ
Sundström, L., Greasley, P. J., Engberg, S., Wallander, M., & Ryberg, E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.067 · Cited by 59
Current hypotheses regarding the pathophysiology behind the takotsubo syndrome
Redfors, B., Shao, Y., Ali, A., & Ömerovic, E. (2014) · International Journal of Cardiology · doi:10.1016/j.ijcard.2014.10.156 · Cited by 55
GPCRRD: G protein-coupled receptor spatial restraint database for 3D structure modeling and function annotation
Zhang, J., & Zhang, Y. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq563 · Cited by 55
Targeting the dopamine D3 receptor: an overview of drug design strategies
Cortés, A., Moreno, E., Rodríguez-Ruiz, M., Canela, E. I., & Casadó, V. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2016.1185413 · Cited by 57
The G protein-coupled receptor N-terminus and receptor signalling: N-tering a new era
Coleman, J. L. J., Ngo, T., & Smith, N. J. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.004 · Cited by 55
Viral GPCR US28 can signal in response to chemokine agonists of nearly unlimited structural degeneracy
Miles, T. F., Spieß, K., Jude, K. M., Tsutsumi, N., Burg, J. S., Ingram, J. R., Waghray, D., Hjortø, G. M., Larsen, O., Ploegh, H. L., et al. (2018) · eLife · doi:10.7554/elife.35850 · Cited by 58
“, 2015) (Nb7 or Nb11) enable purification of stable, apo-US28 (Figure 2— figure supplement 1) that can be used to stain yeast cells displaying chemokine on their surface (Figure 2a), thereby solving the general problem of structural instability of GPCRs purified in apo form (Handel, 2015; Rosenbaum et al., 2009; Wu et…”
Background
Detailed insight on β-adrenoceptors as therapeutic targets
Velmurugan, B. K., Baskaran, R., & Huang, C. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109039 · Cited by 54
G-Protein coupled receptors: structure and function in drug discovery
Odoemelam, C. S., Percival, B. C., Wallis, H., Chang, M., Ahmad, Z., Scholey, D. V., Burton, E. J., Williams, I. H., Kamerlin, S. C. L., & Wilson, P. (2020) · RSC Advances · doi:10.1039/d0ra08003a · Cited by 55
Targeting G protein coupled receptor-related pathways as emerging molecular therapies
Ghanemi, A. (2015) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2013.07.007 · Cited by 53
Simulations of Biased Agonists in the β2 Adrenergic Receptor with Accelerated Molecular Dynamics
Tikhonova, I. G., Selvam, B., Ivetac, A., Wereszczynski, J., & McCammon, J. A. (2013) · Biochemistry · doi:10.1021/bi400499n · Cited by 53
Limits of Ligand Selectivity from Docking to Models: In Silico Screening for A1 Adenosine Receptor Antagonists
Kolb, P., Phan, K., Gao, Z., Marko, A. C., Šali, A., & Jacobson, K. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049910 · Cited by 53
Retinal Ligand Mobility Explains Internal Hydration and Reconciles Active Rhodopsin Structures
Leioatts, N., Mertz, B., Martínez‐Mayorga, K., Romo, T. D., Pitman, M. C., Feller, S. E., Grossfield, A. M., & Brown, M. F. (2013) · Biochemistry · doi:10.1021/bi4013947 · Cited by 55
Fluorescent probes for G-protein-coupled receptor drug discovery
Iliopoulos‐Tsoutsouvas, C., Kulkarni, R., Makriyannis, A., & Nikas, S. P. (2018) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2018.1518975 · Cited by 54
Mechanistic origin of partial agonism of tetrahydrocannabinol for cannabinoid receptors
Dutta, S., Selvam, B., Das, A., & Shukla, D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101764 · Cited by 54
“Cannabinoid receptor 1(CB1) belongs to the family of class A G-protein-coupled receptors (GPCRs) (1, 2), whichmodulates diverse cellular signaling processes via intracellular G-proteins (3) and β-arrestins (4).”
Background
Isothermal titration calorimetry in membrane protein research
Drączkowski, P., Matosiuk, D., & Jóźwiak, K. (2013) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2013.09.003 · Cited by 58
Phosphoinositide 3-Kinase-Dependent Antagonism in Mammalian Olfactory Receptor Neurons
Ukhanov, K., Brunert, D., Corey, E. A., & Ache, B. W. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3698-10.2011 · Cited by 54
“…receptors (GPCRs) (Buck and Axel, 1991) and that ligand-induced selective signaling is rapidly becoming a generic theme for GPCRs (for review, see Rosenbaum et al., 2009; Millar and Newton, 2010), it is reasonable to consider the possible existence of odorant-specific modes of signaling in…”
BackgroundInfluential
Norepinephrine Inhibition of Mesenchymal Stem Cell and Chondrogenic Progenitor Cell Chondrogenesis and Acceleration of Chondrogenic Hypertrophy
Jenei‐Lanzl, Z., Grässel, S., Pongratz, G., Kees, F., Miosge, N., Angele, P., & Straub, R. H. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38695 · Cited by 53
Prediction of G Protein-Coupled Receptors with SVM-Prot Features and Random Forest
Liao, Z., Ju, Y., & Zou, Q. (2016) · Scientifica · doi:10.1155/2016/8309253 · Cited by 53
A Critical Analysis of Molecular Mechanisms Underlying Membrane Cholesterol Sensitivity of GPCRs
Jafurulla, M., Kumar, G. A., Rao, B. D., & Chattopadhyay, A. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-04278-3_2 · Cited by 56
Receptors Mediating Host-Microbiota Communication in the Metaorganism: The Invertebrate Perspective
Dierking, K., & Pita, L. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01251 · Cited by 57
“GPCRs are thus involved in a multitude of different physiological functions, such as development, reproduction, metabolism, neuronal function, taste, smell, cell adhesion, immune function, and the regulation of feeding (160, 161).”
Background
Conformationally Preorganized Diastereomeric Norbornane-Based Maltosides for Membrane Protein Study: Implications of Detergent Kink for Micellar Properties
Das, M., Du, Y., Ribeiro, O., Hariharan, P., Mortensen, J. S., Patra, D., Skiniotis, G., Loland, C. J., Guan, L., Kobilka, B. K., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11997 · Cited by 52
Self-citation
Recent advances in the synthesis of C-terminally modified peptides
Arbour, C. A., Mendoza, L. G., & Stockdill, J. L. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob01417f · Cited by 52
NIR-Activated Content Release from Plasmon Resonant Liposomes for Probing Single-Cell Responses
Leung, S. J., & Romanowski, M. (2012) · ACS Nano · doi:10.1021/nn304434a · Cited by 51
Why are polar residues within the membrane core evolutionary conserved?
Illergård, K., Kauko, A., & Elofsson, A. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22859 · Cited by 52
Transmembrane peptides as unique tools to demonstrate the in vivo action of a cross‐class GPCR heterocomplex
Lee, L. T. O., Ng, S., Chu, J., Sekar, R., Harikumar, K. G., Miller, L. J., & Chow, B. (2014) · The FASEB Journal · doi:10.1096/fj.13-246868 · Cited by 52
Silencing of Odorant Receptor Genes by G Protein βγ Signaling Ensures the Expression of One Odorant Receptor per Olfactory Sensory Neuron
Ferreira, T., Wilson, S. R., Choi, Y. G., Risso, D., Dudoit, S., Speed, T. P., & Ngai, J. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.001 · Cited by 52
Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems
Magliery, T. J., Lavinder, J. J., & Sullivan, B. J. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.03.015 · Cited by 52
Understanding cadherin EGF LAG seven‐pass G‐type receptors
Wang, X., Zhang, D., Xu, Z., Ma, M., Wang, W., Li, L., Han, X., Huo, Y., Yu, X., & Sun, J. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12955 · Cited by 49
“(Shukla et al. 2008; Hanson and Stevens 2009; Rosenbaum et al. 2009; Kahsai et al. 2011).”
Transmembrane Protein Activation Refined by Site‐Specific Hydration Dynamics
Hussain, S., Franck, J. M., & Han, S. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201206147 · Cited by 53
How Do Branched Detergents Stabilize GPCRs in Micelles?
Lee, S., Ghosh, S., Jana, S., Robertson, N. J., Tate, C. G., & Vaidehi, N. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00183 · Cited by 52
Noradrenaline in the aging brain: Promoting cognitive reserve or accelerating Alzheimer's disease?
Mather, M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.05.013 · Cited by 57
Critical roles of G protein-coupled receptors in regulating intestinal homeostasis and inflammatory bowel disease
Feng, Z., Sun, R., Cong, Y., & Liu, Z. (2022) · Mucosal Immunology · doi:10.1038/s41385-022-00538-3 · Cited by 50
“They share numerous developmental and functional characteristics with CD4 T cells and are divided into three subtypes based on the signature transcription factors and effector cytokines: (1) ILC1s require the transcription factor T-BET and express interferon-γ; (2) ILC2s depend on the transcription factor GATA3 and ma…”
Background
Dynamic ligand binding dictates partial agonism at a G protein–coupled receptor
Böck, A., Chirinda, B., Krebs, F., Messerer, R., Bätz, J., Muth, M., Dallanoce, C., Klingenthal, D., Tränkle, C., Hoffmann, C., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1384 · Cited by 51
Not Just an Oil Slick: How the Energetics of Protein-Membrane Interactions Impacts the Function and Organization of Transmembrane Proteins
Mondal, S., Khelashvili, G., & Weinstein, H. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.04.032 · Cited by 52
Transmembrane signaling by GPCRs: Insight from rhodopsin and opsin structures
Choe, H., Park, J. H., Kim, Y. J., & Ernst, O. P. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.018 · Cited by 50
Coupling Mechanism of a GPCR and a Heterotrimeric G Protein During Chemoattractant Gradient Sensing in Dictyostelium
Xu, X., Meckel, T., Brzostowski, J. A., Yan, J., Meier‐Schellersheim, M., & Jin, T. (2010) · Science Signaling · doi:10.1126/scisignal.2000980 · Cited by 51
Constitutive Activities and Inverse Agonism in Dopamine Receptors
Zhang, B., Albaker, A. B., Plouffe, B., Lefèbvre, C., & Tiberi, M. (2014) · Advances in pharmacology · doi:10.1016/b978-0-12-417197-8.00007-9 · Cited by 54
Microfluidics: From crystallization to serial time-resolved crystallography
Sui, S., & Perry, S. L. (2017) · Structural Dynamics · doi:10.1063/1.4979640 · Cited by 51
Angiogenesis-related non-coding RNAs and gastrointestinal cancer
Razavi, Z. S., Asgarpour, K., Mahjoubin‐Tehran, M., Rasouli, S., Khan, H. Z., Shahrzad, M. K., Hamblin, M. R., & Mirzaei, H. (2021) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2021.04.002 · Cited by 51
Modulating Neuromodulation by Receptor Membrane Traffic in the Endocytic Pathway
von Zastrow, M., & Williams, J. T. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.022 · Cited by 50
Endogenous cannabinoid signaling at inhibitory interneurons
Younts, T. J., & Castillo, P. E. (2014) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.12.006 · Cited by 52
“Inverse agonism effectively decreases the activity of a given receptor below its basal level and can only be observed when GPCRs constitutively signal in the absence of endogenous ligand [78,79].”
Background
Bihelix: Towards de novo structure prediction of an ensemble of G‐protein coupled receptor conformations
Abrol, R., Bray, J. K., & Goddard, W. A. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23216 · Cited by 50
Virtual Screening-Based Discovery and Mechanistic Characterization of the Acylthiourea MRT-10 Family as Smoothened Antagonists
Manetti, F., Faure, H., Roudaut, H., Gorojankina, T., Traiffort, É., Schoenfelder, A., Mann, A., Solinas, A., Taddei, M., & Ruat, M. (2010) · Molecular Pharmacology · doi:10.1124/mol.110.065102 · Cited by 50
Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins
Shalaeva, D. N., Galperin, M. Y., & Mulkidjanian, A. Y. (2015) · Biology Direct · doi:10.1186/s13062-015-0091-4 · Cited by 49
An overview of Ca2+mobilization assays in GPCR drug discovery
Ma, Q., Ye, L., Liu, H., Shi, Y., & Zhou, N. (2017) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2017.1303473 · Cited by 50
Mechanisms of cardiovascular toxicity induced by PM2.5: a review
Zhao, T., Qi, W., Pan, Y., Yang, L., Shi, Y., Zhou, L., & Ye, L. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-16735-9 · Cited by 50
In silico analysis of the binding of agonists and blockers to the β2-adrenergic receptor
Vilar, S., Karpiak, J. D., Berk, B., & Costanzi, S. (2011) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2011.01.005 · Cited by 49
Metabolic limits on classical information processing by biological cells
Fields, C., & Levin, M. G. (2021) · Biosystems · doi:10.1016/j.biosystems.2021.104513 · Cited by 47
Minireview: From the Bench, Toward the Clinic: Therapeutic Opportunities for Cannabinoid Receptor Modulation
Picone, R. P., & Kendall, D. A. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1062 · Cited by 49
Non-HLA-antibodies targeting Angiotensin type 1 receptor and antibody mediated rejection
Dragun, D., Catar, R. A., Kusch, A., Heidecke, H., & Philippe, A. (2012) · Human Immunology · doi:10.1016/j.humimm.2012.07.010 · Cited by 49
Modulation of G-protein coupled receptor sample quality by modified cell-free expression protocols: A case study of the human endothelin A receptor
Junge, F., Luh, L. M., Proverbio, D., Schäfer, B., Abele, R., Beyermann, M., Dötsch, V., & Bernhard, F. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.05.004 · Cited by 49
“G-protein coupled receptors (GPCRs) are the most abundant class of MPs encoded by the human genome and are the key players in signal perception and transduction (Kristiansen, 2004; Rosenbaum et al., 2009).”
Equine skeletal muscle adaptations to exercise and training: evidence of differential regulation of autophagosomal and mitochondrial components
Bryan, K. R., McGivney, B. A., Farries, G., McGettigan, P., McGivney, C. L., Gough, K. F., MacHugh, D. E., Katz, L. M., & Hill, E. W. (2017) · BMC Genomics · doi:10.1186/s12864-017-4007-9 · Cited by 50
Mechanoactivation of the angiotensin II type 1 receptor induces β‐arrestin‐biased signaling through Gα i coupling
Wang, J., Hanada, K., Gareri, C., & Rockman, H. A. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26552 · Cited by 49
Statin-Induced Chronic Cholesterol Depletion Switches GPCR Endocytosis and Trafficking: Insights from the Serotonin1A Receptor
Kumar, G. A., & Chattopadhyay, A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00659 · Cited by 50
Modular transient nanoclustering of activated β2-adrenergic receptors revealed by single-molecule tracking of conformation-specific nanobodies
Gormal, R. S., Padmanabhan, P., Kasula, R., Bademosi, A. T., Coakley, S., Giacomotto, J., Blum, A., Joensuu, M., Wallis, T. P., Lo, H. P., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2007443117 · Cited by 48
Neuropeptide System Regulation of Prefrontal Cortex Circuitry: Implications for Neuropsychiatric Disorders
Casello, S. M., Flores, R. J., Yarur, H. E., Wang, H., Awanyai, M., Arenivar, M. A., Jaime-Lara, R. B., Bravo-Rivera, H., & Tejeda, H. A. (2022) · Frontiers in Neural Circuits · doi:10.3389/fncir.2022.796443 · Cited by 50
Correlated evolution of social organization and lifespan in mammals
Zhu, P., Liu, W., Zhang, X., Li, M., Liu, G., Yu, Y., Li, X., Li, X., Du, J., Wang, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-35869-7 · Cited by 55
Relevance of G protein‐coupled receptor (GPCR) dynamics for receptor activation, signalling bias and allosteric modulation
Lopez‐Balastegui, M., Stępniewski, T. M., Kogut, M. M., Pizio, A. D., ROSENKILDE, M. M., Mao, J., & Selent, J. (2024) · British Journal of Pharmacology · doi:10.1111/bph.16495 · Cited by 47
“This pre-coupling already promotes a significant shift of the conformational equilibrium to active-like conformations — a property that can yield ‘ basal or constitutive activity ’ (Rosenbaum et al., 2009).”
The crystallographic structure of the human adenosine A2A receptor in a high-affinity antagonist-bound state: implications for GPCR drug screening and design
Jaakola, V., & IJzerman, A. P. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.05.002 · Cited by 52
Naturally evolved G protein-coupled receptors adopt metastable conformations
Chen, K.-Y. M., Zhou, F., Fryszczyn, B. G., & Barth, P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205512109 · Cited by 48
Formation of Nanopore-Spanning Lipid Bilayers through Liposome Fusion
Kumar, K., Isa, L., Egner, A., Schmidt, R., Textor, M., & Reimhult, E. (2011) · Langmuir · doi:10.1021/la2019132 · Cited by 48
A mutation in Drosophila methuselah resists paraquat induced Parkinson-like phenotypes
Shukla, A. K., Pragya, P., Chaouhan, H. S., Patel, D. K., Abdin, M. Z., & Chowdhuri, D. K. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.04.008 · Cited by 48

Authors: Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K.
Affiliations: Stanford Medicine (US)
ORCID: Rasmussen, Søren G. F.
Kobilka, Brian K.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2009-05
Volume: 459
Issue: 7245
Pages: 356-363
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature08144
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

The structure and function of G-protein-coupled receptors

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks