The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Discovery of New GPCR Biology: One Receptor Structure at a Time
Open accessAbstract
Summary G protein-coupled receptors (GPCRs) are the largest family of proteins in the human genome. They transmit an exogenous signal to the intracellular second messenger cascade by ligand induced conformational changes within a common seven transmembrane helical bundle. Due to their critical role in biology and drug discovery, tremendous effort has been made over the past several decades to understand the mechanism of signal transduction through the cell membrane. Within the last year we have witnessed a relative explosion in the amount of structural information available for the GPCR family with two new structures of opsin in the presence and absence of transducin peptide, four new structures of β-adrenergic receptors and a recent structure of the human adenosine A2A receptor. The new biological insight being gained such as the highly divergent extracellular loops and areas of structural convergence within the transmembrane helices, allows us to chart a course for further investigation into this important class of membrane proteins.
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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
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
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
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
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 by
Crystal Structure of a Lipid G Protein–Coupled Receptor
Hanson, M. A., Roth, C. B., Jo, E., Griffith, M. T., Scott, F. L., Reinhart, G., Desale, H., Clemons, B., Cahalan, S. M., Schuerer, S. C., et al. (2012) · Science · doi:10.1126/science.1215904 · Cited by 666
Self-citationNormal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins
Bahar, I., Lezon, T. R., Bakan, A., & Shrivastava, I. H. (2010) · Chemical Reviews · doi:10.1021/cr900095e · Cited by 537
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
Selective and potent agonists and antagonists for investigating the role of mouse oxytocin receptors
Busnelli, M., Bulgheroni, E., Manning, M., Kleinau, G., & Chini, B. (2013) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.202994 · Cited by 102
Metadata
- Authors
- Hanson, M. A., & Stevens, R. C.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 17
- Issue
- 1
- Pages
- 8-14
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1980292173
- Cited by
- 196
- References
- 5
- FWCI
- 14.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
