The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Agonists induce conformational changes in transmembrane domains III and VI of the beta 2 adrenoceptor
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Cites
Optimization by Simulated Annealing
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HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor
Feng, Y., Broder, C. C., Kennedy, P. E., & Berger, E. A. (1996) · Science · doi:10.1126/science.272.5263.872 · Cited by 4,172
Ballesteros, J. A., & Weinstein, H. (1995) · Methods in Neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 2,999
Dowsland, K. A., & Thompson, J. M. (2012) · Handbook of Natural Computing · doi:10.1007/978-3-540-92910-9_49 · Cited by 2,432
The β-Chemokine Receptors CCR3 and CCR5 Facilitate Infection by Primary HIV-1 Isolates
Choe, H., Farzan, M., Sun, Y., Sullivan, N., Rollins, B., Ponath, P. D., Wu, L., Mackay, C. R., LaRosa, G., Newman, W., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81313-6 · Cited by 2,287
Samama, P., Cotecchia, S., Costa, T., & Lefkowitz, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53442-6 · Cited by 1,257
Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., & Khorana, H. G. (1996) · Science · doi:10.1126/science.274.5288.768 · Cited by 1,179
STRUCTURE AND FUNCTION OF G PROTEIN-COUPLED RECEPTORS
Strader, C. D., Fong, T. M., Tota, M. R., Underwood, D., & Dixon, R. A. F. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.000533 · Cited by 1,079
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Sequence Alignment of the G-Protein Coupled Receptor Superfamily
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Cited by
G protein coupled receptor structure and activation
Kobilka, B. K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.10.021 · Cited by 623
Mutant G-protein-coupled receptors as a cause of human diseases
Schöneberg, T., Schulz, A., Biebermann, H., Hermsdorf, T., Römpler, H., & Sangkuhl, K. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.08.008 · Cited by 337
Angel, T. E., Chance, M. R., & Palczewski, K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903545106 · Cited by 235
Park, P. S.-H., Lodowski, D. T., & Palczewski, K. (2008) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094630 · Cited by 131
Crystal structure of rhodopsin: implications for vision and beyond
Okada, T. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00227-x · Cited by 121
Metadata
- Authors
- Gether, U.
- Venue
- The EMBO Journal
- Published
- 1997-11-15
- Volume
- 16
- Issue
- 22
- Pages
- 6737-6747
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W1999767086
- Cited by
- 386
- References
- 51
- FWCI
- 6.97
- Type
- journal article
- Language
- en
- Open access
- bronze
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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- CoChat. (2026). Citation check: Agonists induce conformational changes in transmembrane domains III and VI of the beta 2 adrenoceptor. https://app.cochat.ai/papers/10.1093/emboj/16.22.6737
- The paper
- Gether, U. (1997). Agonists induce conformational changes in transmembrane domains III and VI of the beta 2 adrenoceptor. The EMBO Journal. https://doi.org/10.1093/emboj/16.22.6737
Data sources
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.
