The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer
Open accessAbstract
Significance: The absence in the Protein Data Bank of full-length structures of bitopic membrane proteins with one transmembrane helix, probably because of difficulties with ordered crystallization, has limited understanding of how single-transmembrane helices orient enzymes and sensors at the bilayer surface. X-ray crystal structures of full-length yeast lanosterol 14α-demethylase, a cytochrome P450, show how a helix spanning a single transmembrane may lead to constraints on the orientation of the putative substrate entry portal from within the bilayer. The crystal structures also locate the substrate lanosterol, identify putative substrate and product channels, and reveal constrained interactions with triazole antifungal drugs that are important for drug design and understanding the drug resistance associated with orthologs of the enzyme found in fungal pathogens.
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[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
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Interactions between commensal fungi and the C-type lectin receptor Dectin-1 influence colitis
Iliev, I. D., Funari, V. A., Taylor, K. D., Nguyen, Q., Reyes, C. N., Strom, S. P., Brown, J., Becker, C. A., Fleshner, P. R., Dubinsky, M., et al. (2012) · Science · doi:10.1126/science.1221789 · Cited by 1,073
Mammalian Microsomal Cytochrome P450 Monooxygenase
Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696
Structural basis for androgen specificity and oestrogen synthesis in human aromatase
Ghosh, D., Griswold, J., Erman, M., & Pangborn, W. (2009) · Nature · doi:10.1038/nature07614 · Cited by 618
Balzi, E., Wang, M., Leterme, S., Van Dyck, L., & Goffeau, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42155-7 · Cited by 447
Warrilow, A. G. S., Melo, N., Martel, C. M., Parker, J. E., Nes, W. D., Kelly, S. L., & Kelly, D. E. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00316-10 · Cited by 85
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Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development
Salo-Ahen, O. M. H., Alanko, I., Bhadane, R., Bonvin, A. M. J. J., Honorato, R. V., Hossain, S., Juffer, A. H., Kabedev, A., Lahtela-Kakkonen, M., Larsen, A. S., et al. (2020) · Processes · doi:10.3390/pr9010071 · Cited by 659
Azole fungicides – understanding resistance mechanisms in agricultural fungal pathogens
Price, C. L., Parker, J. E., Warrilow, A. G., Kelly, D. E., & Kelly, S. L. (2015) · Pest Management Science · doi:10.1002/ps.4029 · Cited by 321
Clinical implications of globally emerging azole resistance in Aspergillus fumigatus
Meis, J. F., Chowdhary, A., Rhodes, J. L., Fisher, M. C., & Verweij, P. E. (2016) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2015.0460 · Cited by 308
Contribution of Clinically Derived Mutations in ERG11 to Azole Resistance in Candida albicans
Flowers, S. A., Colón, B., Whaley, S. G., Schuler, M. A., & Rogers, P. D. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03470-14 · Cited by 294
Shafiei, M., Peyton, L., Hashemzadeh, M., & Foroumadi, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104240 · Cited by 295
Metadata
- Authors
- Monk, B. C., Tomasiak, T. M., Keniya, M. V., Huschmann, F. U., Tyndall, J. D. A., O’Connell, J. D., Cannon, R. D., McDonald, J. G., Rodriguez, A., Finer-Moore, J. S., & Stroud, R. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-02-03
- Volume
- 111
- Issue
- 10
- Pages
- 3865-3870
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2142627320
- Cited by
- 280
- References
- 9
- FWCI
- 11.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Monk, B. C., Tomasiak, T. M., Keniya, M. V., Huschmann, F. U., Tyndall, J. D. A., O’Connell, J. D., Cannon, R. D., McDonald, J. G., Rodriguez, A., Finer-Moore, J. S., & Stroud, R. M. (2014). Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1324245111
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