The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR
Open accessAbstract
Choosing a Path: The β 2 -adrenergic receptor (β 2 AR) is a G protein–coupled receptor that recognizes diverse ligands to trigger signaling in the cell. Besides binding G proteins, activated β 2 AR can be phosphorylated and bind arrestin, which redirects signaling to other pathways. Some β 2 AR ligands are “biased” in that they differentially activate G protein or arrestin signaling. Liu et al. (p. 1106 , published online 19 January; see the Perspective by Sprang and Chief Elk ) used 19 F-NMR spectroscopy to examine conformational changes associated with a range of ligands and discovered that biased ligands caused differential shifts in equilibrium between two conformational states—the G protein binding state and the arrestin binding state—and thus provide a basis for rational design of pharmacological ligands.
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Cites
Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
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 by
The Molecular Basis of G Protein–Coupled Receptor Activation
Weis, W. I., & Kobilka, B. K. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033910 · Cited by 1,227
Structure and dynamics of GPCR signaling complexes
Hilger, D., Masureel, M., & Kobilka, B. K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0011-7 · Cited by 969
Structural Features for Functional Selectivity at Serotonin Receptors
Wacker, D., Wang, C., Katritch, V., Han, G. W., Huang, X.-P., Vardy, E., McCorvy, J. D., Jiang, Y., Chu, M., Siu, F. Y., et al. (2013) · Science · doi:10.1126/science.1232808 · Cited by 664
Self-citationHow Ligands Illuminate GPCR Molecular Pharmacology
Wacker, D., Stevens, R. C., & Roth, B. L. (2017) · Cell · doi:10.1016/j.cell.2017.07.009 · Cited by 560
Self-citationStaus, D. P., Strachan, R. T., Manglik, A., Pani, B., Kahsai, A. W., Kim, T. H., Wingler, L. M., Ahn, S., Chatterjee, A., Masoudi, A., et al. (2016) · Nature · doi:10.1038/nature18636 · Cited by 330
Metadata
- Authors
- Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., & Wüthrich, K.
- Venue
- Science
- Published
- 2012-03-02
- Volume
- 335
- Issue
- 6072
- Pages
- 1106-1110
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2053549636
- Cited by
- 697
- References
- 3
- FWCI
- 26.95
- Type
- journal article
- Language
- en
- Open access
- green
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