The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
OPM: Orientations of Proteins in Membranes database
Open accessAbstract
Summary: The Orientations of Proteins in Membranes (OPM) database provides a collection of transmembrane, monotopic and peripheral proteins from the Protein Data Bank whose spatial arrangements in the lipid bilayer have been calculated theoretically and compared with experimental data. The database allows analysis, sorting and searching of membrane proteins based on their structural classification, species, destination membrane, numbers of transmembrane segments and subunits, numbers of secondary structures and the calculated hydrophobic thickness or tilt angle with respect to the bilayer normal. All coordinate files with the calculated membrane boundaries are available for downloading. Availabililty: Contact: almz@umich.edu
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Cites
Lipid–protein interactions in biological membranes: A structural perspective
Lee, A. G. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(03)00056-7 · Cited by 886 · cited 2×
“…X-ray scattering, neutron diffraction, electron cryo-microscopy, and NMR or infrared spectroscopy for several dozen cases, such as rhodopsin, lactose permease, mechanosensitive and potassium channels, or C2 domains (Frilingos et al., 1998, Lee 2003, Hubbell et al., 2003, Malmberg and Falke, 2005).”
Background
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Cited by
CHARMM‐GUI: A web‐based graphical user interface for CHARMM
Jo, S., Kim, T., Iyer, V. G., & Im, W. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.20945 · Cited by 9,284
Wassenaar, T. A., Ingólfsson, H. I., Böckmann, R. A., Tieleman, D. P., & Marrink, S. J. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00209 · Cited by 1,174
Semrau, J. D., DiSpirito, A. A., & Yoon, S. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00212.x · Cited by 760
Molecular code for transmembrane-helix recognition by the Sec61 translocon.
Hessa, T., Meindl-Beinker, N. M., Bernsel, A., Kim, H., Sato, Y., Lerch-Bader, M., Nilsson, I., White, S. H., & von Heijne, G. (2007) · Nature · doi:10.1038/nature06387 · Cited by 708
Antidepressant drugs act by directly binding to TRKB neurotrophin receptors
Casarotto, P. C., Girych, M., Fred, S. M., Kovaleva, V., Moliner, R., Enkavi, G., Biojone, C., Cannarozzo, C., Sahu, M. P., Kaurinkoski, K., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.034 · Cited by 663
Metadata
- Authors
- Lomize, M. A., Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-01-05
- Volume
- 22
- Issue
- 5
- Pages
- 623-625
- ISSN
- 1367-4803 (ISSN-L)
- 1367-4811
- OpenAlex
- W2097775366
- Cited by
- 1,173
- References
- 1
- FWCI
- 10.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Lomize, M. A., Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2006). OPM: Orientations of Proteins in Membranes database. Bioinformatics. https://doi.org/10.1093/bioinformatics/btk023
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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.
