The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Heterotrimeric G protein activation by G-protein-coupled receptors
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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
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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
G Protein–Coupled Receptor Rhodopsin
Palczewski, K. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142743 · Cited by 764 · cited 1×
“Within ∼6 ms, metarhodopsin II (MII), the G protein signalling conformation of rhodopsin, is forme”
BackgroundRhodopsin dimers in native disc membranes
Fotiadis, D., Liang, Y., Filipek, S., Saperstein, D. A., Engel, A., & Palczewski, K. (2003) · Nature · doi:10.1038/421127a · Cited by 749
Cited by
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
The Radical-Pair Mechanism of Magnetoreception
Hore, P. J., & Mouritsen, H. (2016) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-032116-094545 · Cited by 813
Regulation, signaling, and physiological functions of G-Proteins
Syrovatkina, V., Alegre, K. O., Dey, R., & Huang, X.-Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.002 · Cited by 498
Selectivity determinants of GPCR–G-protein binding
Flock, T., Hauser, A. S., Lund, N., Gloriam, D. E., Balaji, S., & Babu, M. M. (2017) · Nature · doi:10.1038/nature22070 · Cited by 384
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
Fribourg, M., Moreno, J. L., Holloway, T., Provasi, D., Baki, L., Mahajan, R., Park, G., Adney, S. K., Hatcher, C., Eltit, J. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.055 · Cited by 311
G-Protein–Coupled Receptors in Heart Disease
Wang, J., Gareri, C., & Rockman, H. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.311403 · Cited by 303
Subcellular Organization of GPCR Signaling
Eichel, K., & von Zastrow, M. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.11.009 · Cited by 250
Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121
Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations
Hertig, S., Latorraca, N. R., & Dror, R. O. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004746 · Cited by 118
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Control of Iron Metabolism in Bacteria
Andrews, S., Norton, I., Salunkhe, A. S., Goodluck, H., Aly, W. S. M., Mourad-Agha, H., & Cornelis, P. (2013) · Metal Ions in Life Sciences · doi:10.1007/978-94-007-5561-1_7 · Cited by 72
Wacker, J. L., Feller, D. B., Tang, X.-B., DeFino, M. C., Namkung, Y., Lyssand, J. S., Mhyre, A. J., Tan, X., Jensen, J. B., & Hague, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805251200 · Cited by 71
Periole, X. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00344 · Cited by 58
Structural Evidence for a Sequential Release Mechanism for Activation of Heterotrimeric G Proteins
Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P., & Sakmar, T. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.043 · Cited by 47
Pro-phagocytic function and structural basis of GPR84 signaling
Zhang, X., Wang, Y., Supekar, S., Cao, X., Zhou, J., Dang, J., Chen, S., Jenkins, L., Marsango, S., Li, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41201-0 · Cited by 46
From Atomic Structures to Neuronal Functions of G Protein–Coupled Receptors
Palczewski, K., & Orban, T. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062012-170313 · Cited by 44
“As predicted from biochemical studies (Oldham & Hamm 2008), the amino- and carboxy-terminal α-helices of the G protein exhibited conformational changes that propagated to its nucleotidebinding pocket.”
BackgroundCholinergic and Adenosinergic Modulation of Synaptic Release
Yang, D., Ding, C., Qi, G., & Feldmeyer, D. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2020.06.006 · Cited by 24
Direct modulation of TRPC ion channels by Gα proteins
Kang, H., Kim, J., Park, C. H., Jeong, B., & So, I. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1362987 · Cited by 14
Leemann, S., & Kleinlogel, S. (2023) · doi:10.1101/2023.01.27.525823 · Cited by 2
Metadata
- Authors
- Oldham, W. M., & Hamm, H. E.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2008-01
- Volume
- 9
- Issue
- 1
- Pages
- 60-71
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2044775506
- Cited by
- 1,184
- References
- 6
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
