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.
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“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]
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“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]
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“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]
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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
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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”
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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
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