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1

Paul Bolwell, G. "Cytochrome P450:." Phytochemistry 35, no. 1 (December 1993): 279. http://dx.doi.org/10.1016/s0031-9422(00)90557-0.

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2

Ehrenpreis, Eli D., and Seymour Ehrenpreis. "CYTOCHROME P450." Clinics in Liver Disease 2, no. 3 (August 1998): 457–70. http://dx.doi.org/10.1016/s1089-3261(05)70021-0.

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3

Roos, P. H., and N. Jakubowski. "Cytochrome P450." Analytical and Bioanalytical Chemistry 392, no. 6 (October 9, 2008): 1015–17. http://dx.doi.org/10.1007/s00216-008-2415-z.

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4

D'Arcy, P. F. "Cytochrome P450." International Journal of Pharmaceutics 103, no. 1 (February 1994): 99. http://dx.doi.org/10.1016/0378-5173(94)90211-9.

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5

Poulos, Thomas L. "Cytochrome P450." Current Opinion in Structural Biology 5, no. 6 (December 1995): 767–74. http://dx.doi.org/10.1016/0959-440x(95)80009-3.

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6

Coulson, C. J. "Cytochrome P450." Trends in Biochemical Sciences 10, no. 2 (February 1985): 92. http://dx.doi.org/10.1016/0968-0004(85)90255-5.

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7

Yamazaki, Hiroshi, Elizabeth M. J. Gillam, Mi-Sook Dong, William W. Johnson, F. Peter Guengerich, and Tsutomu Shimada. "Reconstitution of Recombinant Cytochrome P450 2C10(2C9) and Comparison with Cytochrome P450 3A4 and Other Forms: Effects of Cytochrome P450–P450 and Cytochrome P450–b5Interactions." Archives of Biochemistry and Biophysics 342, no. 2 (June 1997): 329–37. http://dx.doi.org/10.1006/abbi.1997.0125.

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8

Guengerich, F. Peter, Martha V. Martin, Christal D. Sohl, and Qian Cheng. "Measurement of cytochrome P450 and NADPH–cytochrome P450 reductase." Nature Protocols 4, no. 9 (August 6, 2009): 1245–51. http://dx.doi.org/10.1038/nprot.2009.121.

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9

de Wildt, Saskia N., Gregory L. Kearns, J. Steven Leeder, and John N. van den Anker. "Cytochrome P450 3A." Clinical Pharmacokinetics 37, no. 6 (1999): 485–505. http://dx.doi.org/10.2165/00003088-199937060-00004.

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10

Poulos, T. L. "Cytochrome P450 flexibility." Proceedings of the National Academy of Sciences 100, no. 23 (November 3, 2003): 13121–22. http://dx.doi.org/10.1073/pnas.2336095100.

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11

Meyer, Urs A. "Cytochrome P450 enzymes." Drug Metabolism and Drug Interactions 27, no. 1 (January 1, 2012): 1–2. http://dx.doi.org/10.1515/dmdi-2012-0002.

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12

Lisitsa, A. V., S. A. Guseva, I. I. Karuzina, A. I. Archakov, and L. Koymans. "Cytochrome P450 Database." SAR and QSAR in Environmental Research 12, no. 4 (August 2001): 359–66. http://dx.doi.org/10.1080/10629360108033244.

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13

Owen, Ryan P., Katrin Sangkuhl, Teri E. Klein, and Russ B. Altman. "Cytochrome P450 2D6." Pharmacogenetics and Genomics 19, no. 7 (July 2009): 559–62. http://dx.doi.org/10.1097/fpc.0b013e32832e0e97.

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14

Harvey, Anne T., and Sheldon H. Preskorn. "Cytochrome P450 Enzymes." Journal of Clinical Psychopharmacology 16, no. 4 (August 1996): 273–85. http://dx.doi.org/10.1097/00004714-199608000-00002.

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15

Harvey, Anne T., and Sheldon H. Preskorn. "Cytochrome P450 Enzymes." Journal of Clinical Psychopharmacology 16, no. 5 (October 1996): 345–55. http://dx.doi.org/10.1097/00004714-199610000-00002.

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16

Wong, Luet-Lok. "Cytochrome P450 monooxygenases." Current Opinion in Chemical Biology 2, no. 2 (April 1998): 263–68. http://dx.doi.org/10.1016/s1367-5931(98)80068-9.

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17

Bolwell, G. Paul, Kristin Bozak, and Alfred Zimmerlin. "Plant cytochrome p450." Phytochemistry 37, no. 6 (December 1994): 1491–506. http://dx.doi.org/10.1016/s0031-9422(00)89567-9.

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18

Plettner, Erika. "Preface: Cytochrome P450." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1866, no. 1 (January 2018): 1. http://dx.doi.org/10.1016/j.bbapap.2017.11.001.

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19

Schwartzman, Michal L., and John C. McGiff. "Renal cytochrome P450." Journal of Lipid Mediators and Cell Signalling 12, no. 2-3 (October 1995): 229–42. http://dx.doi.org/10.1016/0929-7855(95)00021-h.

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20

Gilardi, Gianfranco. "Cytochrome P450 biotechnology." Biotechnology and Applied Biochemistry 60, no. 1 (January 2013): 1. http://dx.doi.org/10.1002/bab.1098.

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21

Xiao, Yi, Raku Shinkyo, and F. Peter Guengerich. "Cytochrome P450 2S1 is Reduced by NADPH-Cytochrome P450 Reductase." Drug Metabolism and Disposition 39, no. 6 (March 23, 2011): 944–46. http://dx.doi.org/10.1124/dmd.111.039321.

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22

Shimada, Tsutomu, Raymond L. Mernaugh, and F. Peter Guengerich. "Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b5 enzymes." Archives of Biochemistry and Biophysics 435, no. 1 (March 2005): 207–16. http://dx.doi.org/10.1016/j.abb.2004.12.008.

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23

Reed, James R., J. Patrick Connick, Dongmei Cheng, George F. Cawley, and Wayne L. Backes. "Effect of homomeric P450–P450 complexes on P450 function." Biochemical Journal 446, no. 3 (August 28, 2012): 489–97. http://dx.doi.org/10.1042/bj20120636.

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Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this problem, the catalytic activities of several P450s were examined in reconstituted systems containing NADPH–POR (cytochrome P450 reductase) and a single P450. CYP2B4 (cytochrome P450 2B4)-, CYP2E1 (cytochrome P450 2E1)- and CYP1A2 (cytochrome P450 1A2)-mediated activities were measured as a function of POR concentration using reconstituted systems containing different concentrations of P450. Although CYP2B4-dependent activities could be explained by a simple Michaelis–Menten interaction between POR and CYP2B4, both CYP2E1 and CYP1A2 activities generally produced a sigmoidal response as a function of [POR]. Interestingly, the non-Michaelis behaviour of CYP1A2 could be converted into a simple mass-action response by increasing the ionic strength of the buffer. Next, physical interactions between CYP1A2 enzymes were demonstrated in reconstituted systems by chemical cross-linking and in cellular systems by BRET (bioluminescence resonance energy transfer). Cross-linking data were consistent with the kinetic responses in that both were similarly modulated by increasing the ionic strength of the surrounding solution. Taken together, these results show that CYP1A2 forms CYP1A2–CYP1A2 complexes that exhibit altered catalytic activity.
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24

Tracy, Timothy S. "Atypical Cytochrome P450 Kinetics." Drugs in R & D 7, no. 6 (2006): 349–63. http://dx.doi.org/10.2165/00126839-200607060-00004.

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25

Kirchheiner, Julia, and Cristina Rodriguez-Antona. "Cytochrome P450 2D6 Genotyping." CNS Drugs 23, no. 3 (2009): 181–91. http://dx.doi.org/10.2165/00023210-200923030-00001.

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26

Gomez-Lechon, Maria, Ramiro Jover, and Maria Donato. "Cytochrome P450 and Steatosis." Current Drug Metabolism 10, no. 7 (September 1, 2009): 692–99. http://dx.doi.org/10.2174/138920009789895543.

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27

Ortiz de Montellano, Paul R. "Cytochrome P450-activated prodrugs." Future Medicinal Chemistry 5, no. 2 (February 2013): 213–28. http://dx.doi.org/10.4155/fmc.12.197.

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28

Byron, K. A. "Cytochrome p450 pharmacogenetic testing." Pathology 42 (2010): S20. http://dx.doi.org/10.1097/01268031-201042001-00035.

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29

HANKINSON, OLIVER, and BYRON KEMPER. "Cytochrome P450 Gene Regulation." DNA 6, no. 6 (December 1987): 515–17. http://dx.doi.org/10.1089/dna.1987.6.515.

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30

Gonzalez, Frank J. "Cytochrome P450 humanised mice." Human Genomics 1, no. 4 (2004): 300. http://dx.doi.org/10.1186/1479-7364-1-4-300.

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31

Park, Jongsun, Seungmin Lee, Jaeyoung Choi, Kyohun Ahn, Bongsoo Park, Jaejin Park, Seogchan Kang, and Yong-Hwan Lee. "Fungal cytochrome P450 database." BMC Genomics 9, no. 1 (2008): 402. http://dx.doi.org/10.1186/1471-2164-9-402.

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32

Schuler, Mary A. "Plant Cytochrome P450 Monooxygenases." Critical Reviews in Plant Sciences 15, no. 3 (January 1996): 235–84. http://dx.doi.org/10.1080/07352689609701942.

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33

Nelson, David R. "Metazoan cytochrome P450 evolution." Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology 121, no. 1-3 (November 1998): 15–22. http://dx.doi.org/10.1016/s0742-8413(98)10027-0.

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34

Stout, C. D. "Cytochrome P450 Conformational Diversity." Structure 12, no. 11 (November 2004): 1921–22. http://dx.doi.org/10.1016/j.str.2004.10.002.

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35

Hong, Young Sook. "Cytochrome P450 and Cancer." Ewha Medical Journal 27, no. 1 (2004): 41. http://dx.doi.org/10.12771/emj.2004.27.1.41.

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36

BRENNA, MAIRIN. "Blueing With Cytochrome P450." Chemical & Engineering News 79, no. 2 (January 8, 2001): 30. http://dx.doi.org/10.1021/cen-v079n002.p030.

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37

Coon, M. J. "Special issue: Cytochrome P450." Biochimica et Biophysica Acta (BBA) - General Subjects 1770, no. 3 (March 2007): 313. http://dx.doi.org/10.1016/j.bbagen.2006.11.004.

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38

Nishida, Clinton R., and Paul R. Ortiz de Montellano. "Thermophilic cytochrome P450 enzymes." Biochemical and Biophysical Research Communications 338, no. 1 (December 2005): 437–45. http://dx.doi.org/10.1016/j.bbrc.2005.08.093.

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39

Luoma, Pauli. "Cytochrome P450 and atherosclerosis." Clinical Pharmacology & Therapeutics 59, no. 4 (April 1996): 484. http://dx.doi.org/10.1016/s0009-9236(96)90122-8.

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40

Hubbard, Paul A., Anna L. Shen, Rosemary Paschke, Charles B. Kasper, and Jung-Ja P. Kim. "NADPH-Cytochrome P450 Oxidoreductase." Journal of Biological Chemistry 276, no. 31 (May 22, 2001): 29163–70. http://dx.doi.org/10.1074/jbc.m101731200.

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41

Strange, Richard C., Tracy Ellison, Futniyo Ichii-Jones, Joanna Bath, Paul Hoban, John T. Lear, Andrew G. Smith, et al. "Cytochrome P450 CYP2D6 genotypes." Pharmacogenetics 9, no. 3 (June 1999): 269–76. http://dx.doi.org/10.1097/00008571-199906000-00001.

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42

Newcomb, Martin, Rui Zhang, R. Esala P. Chandrasena, James A. Halgrimson, John H. Horner, Thomas M. Makris, and Stephen G. Sligar. "Cytochrome P450 Compound I." Journal of the American Chemical Society 128, no. 14 (April 2006): 4580–81. http://dx.doi.org/10.1021/ja060048y.

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43

Cali, James J., Dongping Ma, Mary Sobol, Daniel J. Simpson, Susan Frackman, Troy D. Good, William J. Daily, and David Liu. "Luminogenic cytochrome P450 assays." Expert Opinion on Drug Metabolism & Toxicology 2, no. 4 (July 21, 2006): 629–45. http://dx.doi.org/10.1517/17425255.2.4.629.

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44

Gillam, Elizabeth M. J. "Engineering Cytochrome P450 Enzymes." Chemical Research in Toxicology 21, no. 1 (January 2008): 220–31. http://dx.doi.org/10.1021/tx7002849.

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45

BUTERS, JEROEN T. M., JOHANNES DOEHMER, and FRANK J. GONZALEZ. "CYTOCHROME P450-NULL MICE." Drug Metabolism Reviews 31, no. 2 (January 1999): 437–47. http://dx.doi.org/10.1081/dmr-100101929.

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46

Hansch, Corwin, Suresh Babu Mekapati, Alka Kurup, and Rajeshwar Prasad Verma. "QSAR of Cytochrome P450." Drug Metabolism Reviews 36, no. 1 (January 2004): 105–56. http://dx.doi.org/10.1081/dmr-120028428.

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47

Buchatskii, Alexander G., Konstantin Yu Kazachenko, and Alexander A. Alexandrov. "Cytochrome P450 Pattern Revision." Journal of Biomolecular Structure and Dynamics 19, no. 2 (October 2001): 273–77. http://dx.doi.org/10.1080/07391102.2001.10506737.

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48

Berger, Bradley J., and Alan H. Fairlamb. "Cytochrome P450 in trypanosomatids." Biochemical Pharmacology 46, no. 1 (July 1993): 149–57. http://dx.doi.org/10.1016/0006-2952(93)90359-5.

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49

Krau, Stephen D. "Cytochrome p450, Part 1." Nursing Clinics of North America 48, no. 4 (December 2013): 671–80. http://dx.doi.org/10.1016/j.cnur.2013.09.002.

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50

Krau, Stephen D. "Cytochrome p450 Part 2." Nursing Clinics of North America 48, no. 4 (December 2013): 681–96. http://dx.doi.org/10.1016/j.cnur.2013.09.003.

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