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Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery
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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
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From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Fifteen year mortality in Coronary Drug Project patients: long-term benefit with niacin
Canner, P. L., Berge, K. G., Wenger, N. K., Stamler, J., Friedman, L., Prineas, R. J., & Friedewald, W. (1986) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(86)80293-5 · Cited by 1,824
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
Crystal structure of opsin in its G-protein-interacting conformation
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The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure
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Identification of a serotonin/glutamate receptor complex implicated in psychosis
González-Maeso, J., Ang, R. L., Yuen, T., Chan, P., Weisstaub, N. V., López-Giménez, J. F., Zhou, M., Okawa, Y., Callado, L. F., Milligan, G., et al. (2008) · Nature · doi:10.1038/nature06612 · Cited by 803
Intrinsic Disorder in Transcription Factors
Liu, J., Perumal, N. B., Oldfield, C. J., Su, E. W., Uversky, V. N., & Dunker, A. K. (2006) · Biochemistry · doi:10.1021/bi0602718 · Cited by 792
Cited by
The physiology, signaling, and pharmacology of dopamine receptors
Beaulieu, J.-M., & Gainetdinov, R. R. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.002642 · Cited by 2,763
How were new medicines discovered?
Swinney, D. C., & Anthony, J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3480 · Cited by 1,812
Relaxin family peptides and their receptors
Bathgate, R. A. D., Halls, M. L., van der Westhuizen, E. T., Callander, G. E., Kocan, M., & Summers, R. J. (2013) · Physiological Reviews · doi:10.1152/physrev.00001.2012 · Cited by 534
Emerging paradigms in GPCR allostery: implications for drug discovery
Wootten, D., Christopoulos, A., & Sexton, P. M. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4052 · Cited by 498
Graaf, C. D., Donnelly, D., Wootten, D., Lau, J., Sexton, P. M., Miller, L. J., Ahn, J.-M., Liao, J., Fletcher, M. M., Yang, D., et al. (2016) · Pharmacological Reviews · doi:10.1124/pr.115.011395 · Cited by 403
Self-citation
Metadata
- Authors
- Kenakin, T., & Miller, L. J.
- Venue
- Pharmacological Reviews
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 62
- Issue
- 2
- Pages
- 265-304
- ISSN
- 0031-6997 (ISSN-L)
- OpenAlex
- W2132746917
- Cited by
- 573
- References
- 20
- FWCI
- 27.06
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery. https://app.cochat.ai/papers/10.1124/pr.108.000992
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- Kenakin, T., & Miller, L. J. (2010). Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery. Pharmacological Reviews. https://doi.org/10.1124/pr.108.000992
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.