The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
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Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Deisenhofer, J., Epp, O., Miki, K., Huber, R., & Michel, H. (1985) · Nature · doi:10.1038/318618a0 · Cited by 3,068
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,006
Oesterhelt, D., & Stoeckenius, W. (1974) · Methods in Enzymology · doi:10.1016/0076-6879(74)31072-5 · Cited by 1,687
Structure of bacteriorhodopsin at 1.55 Å resolution
Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J.-P., & Lanyi, J. K. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3027 · Cited by 1,450
Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
Landau, E. M., & Rosenbusch, J. P. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14532 · Cited by 984
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., & Landau, E. M. (1997) · Science · doi:10.1126/science.277.5332.1676 · Cited by 860
Cited by
The structure and function of G-protein-coupled receptors
Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534
The crystal structure of a voltage-gated sodium channel
Payandeh, J., Scheuer, T., Zheng, N., & Catterall, W. A. (2011) · Nature · doi:10.1038/nature10238 · Cited by 1,429
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
Ujwal, R., Cascio, D., Colletier, J.-P., Faham, S., Zhang, J., Toro, L., Ping, P., & Abramson, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809634105 · Cited by 543
Self-citationMembrane protein crystallization
Caffrey, M. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(03)00043-1 · Cited by 340
Metadata
- Authors
- Faham, S., & Bowie, J. U.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 316
- Issue
- 1
- Pages
- 1-6
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2020465369
- Cited by
- 324
- References
- 24
- FWCI
- 13.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. https://app.cochat.ai/papers/10.1006/jmbi.2001.5295
- The paper
- Faham, S., & Bowie, J. U. (2002). Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.2001.5295
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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.