The DOI matches its Crossref record; 51 of the 52 references it cites were found in a registry or an index.
Mammalian Microsomal Cytochrome P450 Monooxygenase
Open accessAbstract
Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“There are low-circulating levels of plasma XO in baseline conditions that can increase in disease conditions by the release from damaged cells in liver or other tissues (1010).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1010]
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
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
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., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
Classical Electrostatics in Biology and Chemistry
Honig, B. H., & Nicholls, A. O. (1995) · Science · doi:10.1126/science.7761829 · Cited by 2,891
XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron Density
McRee, D. E. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4094 · Cited by 2,096
Self-citationImproved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,870
IDENTIFYING NONPOLAR TRANSBILAYER HELICES IN AMINO ACID SEQUENCES OF MEMBRANE PROTEINS
Engelman, D. M., Steitz, T. A., & Goldman, A. (1986) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.15.060186.001541 · Cited by 1,508
HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM
Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90190-2 · Cited by 1,419
Gotoh, O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48462-1 · Cited by 1,204
Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's
Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A., & Deisenhofer, J. (1993) · Science · doi:10.1126/science.8342039 · Cited by 879
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
Poulos, T. L., Finzel, B. C., GUNSALUS, I. C., Wagner, G. C., & Kraut, J. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36209-9 · Cited by 826
Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. S., & Kim, J.-J. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8411 · Cited by 744
Structure and function of cytochromes P450: a comparative analysis of three crystal structures
Hasemann, C. A., Kurumbail, R. G., Boddupalli, S. S., Peterson, J. A., & Deisenhofer, J. (1995) · Structure · doi:10.1016/s0969-2126(01)00134-4 · Cited by 692
Structure of a cytochrome P450-redox partner electron-transfer complex
Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501
Li, H., & Poulos, T. L. (1997) · Nature Structural Biology · doi:10.1038/nsb0297-140 · Cited by 471
Crystal structure and refinement of cytochrome P450terp at 2·3 Å resolution
Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., & Deisenhofer, J. (1994) · Journal of Molecular Biology · doi:10.1016/0022-2836(94)90019-1 · Cited by 396
Lindberg, R. L. P., & Negishi, M. (1989) · Nature · doi:10.1038/339632a0 · Cited by 384
Bridges, A., Gruenke, L., Chang, Y.-T., Vakser, I. A., Loew, G., & Waskell, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.17036 · Cited by 287
Miscellaneous Algorithms for Density Modification
Cowtan, K. D., & Main, P. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444997011980 · Cited by 283
Sakaguchi, M., Mihara, K., & Sato, R. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02521.x · Cited by 215
Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum
Park, S., Shimizu, H., Adachi, S., Nakagawa, A., Tanaka, I., Nakahara, K., Shoun, H., OBAYASHI, E., Nakamura, H., lizuka, T., et al. (1997) · Nature Structural Biology · doi:10.1038/nsb1097-827 · Cited by 188
Engineering Microsomal Cytochrome P450 2C5 to Be a Soluble, Monomeric Enzyme
Cosme, J., & Johnson, E. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2545 · Cited by 169
Self-citationMonier, S., Luc, P.-V. T., Kreibich, G., Sabatini, D. D., & Adesnik, M. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.2.457 · Cited by 148
Richardson, T. H., Jung, F., Griffin, K. J., Wester, M., Raucy, J. L., KEMPER, B. W., Bornheim, L. M., Hassett, C., Omiecinski, C. J., & Johnson, E. F. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.0013 · Cited by 146
Self-citationA close family resemblance: the importance of structure in understanding cytochromes P450
Peterson, J. A., & Graham, S. E. (1998) · Structure · doi:10.1016/s0969-2126(98)00109-9 · Cited by 135
Szczesna-Skorupa, E., Browne, N. F., Mead, D. A., & KEMPER, B. W. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.3.738 · Cited by 135
Sakaguchi, M., Mihara, K., & Sato, R. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.11.3361 · Cited by 117
von Wachenfeldt, C., Richardson, T. H., Cosme, J., & Johnson, E. F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.9859 · Cited by 108
Self-citationStructures of Eukaryotic Cytochrome P450 Enzymes
von Wachenfeldt, C., & Johnson, E. F. (1995) · Springer eBooks · doi:10.1007/978-1-4757-2391-5_6 · Cited by 107
Self-citationGriffin, C. B., & Primack, S. L. (2001) · Radiologic Clinics of North America · doi:10.1016/s0033-8389(05)70332-8 · Cited by 92
Pernecky, S. J., Larson, J. R., Philpot, R. M., & Coon, M. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2651 · Cited by 91
Li, Y., & Chiang, J. Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54980-2 · Cited by 82
Site-Directed Mutagenesis as a Tool for Molecular Modeling of Cytochrome P450 2B1
Szklarz, G. D., He, Y. A., & Halpert, J. R. (1995) · Biochemistry · doi:10.1021/bi00044a008 · Cited by 79
Membrane topology of mammalian cytochromes P-450 from liver endoplasmic reticulum
Brown, C. A., & Black, S. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83762-0 · Cited by 76
DuBois, R. N., Simpson, E. R., Tuckey, J. A., Lambeth, J. D., & Waterman, M. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.2.1028 · Cited by 74
Szczesna-Skorupa, E., & Kemper, B. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.4.1237 · Cited by 73
Methods in Enzymology, volume 265
Nimmo, M. (1997) · TrAC Trends in Analytical Chemistry · doi:10.1016/s0165-9936(97)81509-9 · Cited by 73
Sagara, Y., Barnes, H. J., & Waterman, M. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1349 · Cited by 72
He, Y.-A., Luo, Z., Klekotka, P. A., Burnett, V. L., & Halpert, J. R. (1994) · Biochemistry · doi:10.1021/bi00180a040 · Cited by 59
Hybrid cytochromes P-450 identify a substrate binding domain in P-450IIC5 and P-450IIC4.
Kronbach, T., Larabee, T. M., & Johnson, E. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.21.8262 · Cited by 57
Self-citationRole of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1
He, Y. A., Balfour, C. A., Kedzie, K. M., & Halpert, J. R. (1992) · Biochemistry · doi:10.1021/bi00153a015 · Cited by 52
Structural Studies on Prokaryotic Cytochromes P450
Poulos, T. L., Cupp‐Vickery, J. R., & Li, H. (1995) · Springer eBooks · doi:10.1007/978-1-4757-2391-5_4 · Cited by 50
Kempf, A. C., Zanger, U. M., & Meyer, U. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1396 · Cited by 43
Black, S. D., Martin, S. T., & Smith, C. A. (1994) · Biochemistry · doi:10.1021/bi00188a025 · Cited by 39
Ogishima, T., Okada, Y., & Omura, T. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135335 · Cited by 37
Lou, Z., He, Y. A., & Halpert, J. R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1083 · Cited by 35
Cupp‐Vickery, J. R., Li, H., & Poulos, T. L. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340200210 · Cited by 33
Dong, M., Bell, L. C., Guo, Z., Phillips, D. R., Blair, I. A., & Guengerich, F. P. (1996) · Biochemistry · doi:10.1021/bi960873z · Cited by 32
Membrane Topology of Cytochrome P450 2B4 in Langmuir–Blodgett Monolayers
Shank-Retzlaff, M. L., Raner, G. M., Coon, M. J., & Sligar, S. G. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0889 · Cited by 28
Cited by
Sorted by citations
Mechanism of Oxidation Reactions Catalyzed by Cytochrome P450 Enzymes
Meunier, B., de Visser, S. P., & Shaik, S. S. (2004) · Chemical Reviews · doi:10.1021/cr020443g · Cited by 2,433
Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical Toxicity
Guengerich, F. P. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0002583 · Cited by 1,661
Cytochromes P450: a success story.
Werck‐Reichhart, D., & Feyereisen, R. (2000) · Genome biology · doi:10.1186/gb-2000-1-6-reviews3003 · Cited by 962
Cytochromes P450 and metabolism of xenobiotics
Anzenbacher, P., & Anzenbacherová, E. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000897 · Cited by 890
Metadata
- Authors
- Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- McRee, Duncan E.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 5
- Issue
- 1
- Pages
- 121-131
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2051639214
- Cited by
- 696
- References
- 52
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 10 · 2023: 5 · 2022: 8 · 2021: 7 · 2020: 19 · 2019: 15 · 2018: 18 · 2017: 18 · 2016: 21 · 2015: 13 · 2014: 18 · 2013: 20 · 2012: 11
- FWCI
- 53.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p01gm048495-08)
- National Institute of General Medical Sciences (R01GM031001, GM-31001, GM-48495)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- cytochrome P450, endoplasmic reticulum, protein structure, NADPH-cytochrome P450 reductase, xenobiotic detoxification, procarcinogen activation, steroidogenesis, drug-drug interactions, drug discovery
- MeSH terms
- Cytochrome P450 Family 2, Amino Acid Sequence, Animals, Binding Sites, Cytochrome P-450 Enzyme System, Endoplasmic Reticulum, Heme, Mammals, Microsomes, Models, Molecular, Molecular Sequence Data, Steroid 21-Hydroxylase, Protein Structure, Secondary, Crystallography, X-Ray
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review