{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T15:41:25Z","timestamp":1791560485699,"version":"4.3.4"},"reference-count":104,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2011,1,1]],"date-time":"2011-01-01T00:00:00Z","timestamp":1293840000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2011,1]]},"DOI":"10.1016\/j.bbapap.2010.06.021","type":"journal-article","created":{"date-parts":[[2010,7,8]],"date-time":"2010-07-08T08:41:31Z","timestamp":1278578491000},"page":"200-209","source":"Crossref","is-referenced-by-count":109,"title":["At the crossroads of steroid hormone biosynthesis: The role, substrate specificity and evolutionary development of CYP17"],"prefix":"10.1016","volume":"1814","author":[{"given":"Andrei A.","family":"Gilep","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatyana A.","family":"Sushko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey A.","family":"Usanov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2010.06.021_bb0005","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/0022-4731(87)90147-6","article-title":"Structure of genes encoding steroidogenic enzymes","volume":"27","author":"Miller","year":"1987","journal-title":"J. Steroid Biochem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0010","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1095\/biolreprod.103.026732","article-title":"Colocalization of P450c17 and cytochrome b5 in androgen-synthesizing tissues of the human","volume":"71","author":"Dharia","year":"2004","journal-title":"Biol. Reprod."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0015","doi-asserted-by":"crossref","first-page":"2746","DOI":"10.1210\/jc.81.7.2746","article-title":"ACTH receptor, CYP11A1, CYP17 and CYP21A2 genes are expressed in skin","volume":"81","author":"Slominski","year":"1996","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0020","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.jsbmb.2003.07.006","article-title":"Profiling transcript levels for steroidogenic enzymes in fetal tissues","volume":"87","author":"Pezzi","year":"2003","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0025","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1210\/jcem-63-5-1145","article-title":"Developmental expression of genes for the stereoidogenic enzymes P450scc (20, 22-desmolase), P450c17 (17 alpha-hydroxylase\/17, 20-lyase), and P450c21 (21-hydroxylase) in the human fetus","volume":"63","author":"Voutilainen","year":"1986","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0030","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1210\/me.15.8.1277","article-title":"NF-1C, Sp1, and Sp3 are essential for transcription of the human gene for P450c17 (steroid 17alpha-hydroxylase\/17, 20 lyase) in human adrenal NCI-H295A cells","volume":"15","author":"Lin","year":"2001","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0035","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0378-5122(02)00021-X","article-title":"Genetic modelling of the estrogen metabolism as a risk factor of hormone-dependent disorders","volume":"42","author":"Huber","year":"2002","journal-title":"Maturitas"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0040","first-page":"118","article-title":"Interrelation of structural (\u0421\/\u0422-34) polymorphism of human gene CYP17A1 with biochemical and bionergetics characteristics of the organism","volume":"4","author":"Gilep","year":"2009","journal-title":"Vestn. FFR"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0045","doi-asserted-by":"crossref","first-page":"25811","DOI":"10.1016\/S0021-9258(19)74462-7","article-title":"Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency","volume":"268","author":"Monno","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0050","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1210\/jc.79.1.160","article-title":"Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency","volume":"79","author":"Fardella","year":"1994","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0055","doi-asserted-by":"crossref","first-page":"15992","DOI":"10.1016\/S0021-9258(18)98506-6","article-title":"Missense mutation serine106\u2014proline causes 17 alpha-hydroxylase deficiency","volume":"266","author":"Lin","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0060","doi-asserted-by":"crossref","first-page":"19681","DOI":"10.1016\/S0021-9258(19)36570-6","article-title":"Expression and purification of functional human 17 alpha-hydroxylase\/17, 20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase\/17, 20-lyase deficiency","volume":"268","author":"Imai","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0065","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1210\/jc.74.3.667","article-title":"Compound heterozygous mutations (Arg 239\u2014stop, Pro 342\u2014Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase\/17, 20-lyase deficiency","volume":"74","author":"Ahlgren","year":"1992","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0070","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/0925-4439(92)90100-2","article-title":"Molecular basis of apparent isolated 17, 20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)\u2014Cys, Gln(461)\u2014Stop) actually cause combined 17 alpha-hydroxylase\/17, 20-lyase deficiency","volume":"1139","author":"Yanase","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0075","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/ng1097-201","article-title":"The genetic and functional basis of isolated 17, 20-lyase deficiency","volume":"17","author":"Geller","year":"1997","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0080","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1210\/me.13.1.167","article-title":"P450c17 mutations R347H and R358Q selectively disrupt 17, 20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5","volume":"13","author":"Geller","year":"1999","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0085","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1210\/me.13.7.1169","article-title":"Molecular modeling of human P450c17 (17alpha-hydroxylase\/17, 20-lyase): insights into reaction mechanisms and effects of mutations","volume":"13","author":"Auchus","year":"1999","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0090","doi-asserted-by":"crossref","first-page":"3807","DOI":"10.1210\/jc.82.11.3807","article-title":"A single amino acid substitution in the putative redox partner-binding site of P450c17 as cause of isolated 17, 20-lyase deficiency","volume":"82","author":"Biason-Lauber","year":"1997","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0095","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1210\/jc.77.1.98","article-title":"Progesterone 16 alpha-hydroxylase activity is catalyzed by human cytochrome P450 17 alpha-hydroxylase","volume":"77","author":"Swart","year":"1993","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0100","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1089\/dna.1998.17.707","article-title":"Modulation of 17alpha-hydroxylase\/17, 20-lyase activity of guinea pig cytochrome P450c17 by site-directed mutagenesis","volume":"17","author":"Beaudoin","year":"1998","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0105","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1089\/dna.1997.16.357","article-title":"Characterization of the adrenal cytochrome P450C17 in the hamster, a small animal model for the study of adrenal dehydroepiandrosterone biosynthesis","volume":"16","author":"Cloutier","year":"1997","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0110","doi-asserted-by":"crossref","first-page":"4665","DOI":"10.1210\/en.2002-220456","article-title":"Molecular evolution of adrenarche: structural and functional analysis of P450c17 from four primate species","volume":"143","author":"Arlt","year":"2002","journal-title":"Endocrinology"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0115","doi-asserted-by":"crossref","first-page":"2112","DOI":"10.1210\/endo-103-6-2112","article-title":"Adrenarche: a survey of rodents, domestic animals, and primates","volume":"103","author":"Cutler","year":"1978","journal-title":"Endocrinology"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0120","first-page":"305","article-title":"Pubertal endocrinology of the baboon: adrenarche","volume":"241","author":"Castracane","year":"1981","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0125","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0022-4731(72)90011-8","article-title":"16-Unsaturated C 19 steroids. A review of their chemistry, biochemistry and possible physiological role","volume":"3","author":"Gower","year":"1972","journal-title":"J. Steroid Biochem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0130","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1042\/bj1080233","article-title":"The biosynthesis of some androst-16-enes from C21 and C19 steroids in boar testicular and adrenal tissue","volume":"108","author":"Ahmad","year":"1968","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0135","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/0006-291X(85)91190-8","article-title":"Cytochrome b5 promotes the synthesis of delta 16-C19 steroids by homogeneous cytochrome P-450 C21 side-chain cleavage from pig testis","volume":"132","author":"Nakajin","year":"1985","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0140","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1046\/j.1432-1033.2003.03508.x","article-title":"Assessment of porcine and human 16-ene-synthase, a third activity of P450c17, in the formation of an androstenol precursor. Role of recombinant cytochrome b5 and P450 reductase","volume":"270","author":"Soucy","year":"2003","journal-title":"Eur. J. Biochem."},{"issue":"Pt 3","key":"10.1016\/j.bbapap.2010.06.021_bb0145","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1042\/bj3080901","article-title":"Modulation of the activity of human 17 alpha-hydroxylase-17, 20-lyase (CYP17) by cytochrome b5: endocrinological and mechanistic implications","volume":"308","author":"Lee-Robichaud","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0150","doi-asserted-by":"crossref","first-page":"5608","DOI":"10.1046\/j.1432-1033.2002.03268.x","article-title":"Baboon cytochrome P450 17alpha-hydroxylase\/17, 20-lyase (CYP17)","volume":"269","author":"Swart","year":"2002","journal-title":"Eur. J. Biochem."},{"issue":"2\u20133","key":"10.1016\/j.bbapap.2010.06.021_bb0155","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1080\/03602530701468391","article-title":"Comparison of the 17 alpha-hydroxylase\/C17, 20-lyase activities of porcine, guinea pig and bovine P450c17 using purified recombinant fusion proteins containing P450c17 linked to NADPH-P450 reductase","volume":"39","author":"Shet","year":"2007","journal-title":"Drug Metab. Rev."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0160","doi-asserted-by":"crossref","first-page":"8729","DOI":"10.1016\/S0021-9258(17)47213-9","article-title":"Multiple catalytic properties of the purified and reconstituted cytochrome P-450 (P-450sccII) system of pig testis microsomes","volume":"259","author":"Suhara","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0165","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.abb.2003.07.003","article-title":"5alpha-reduced C21 steroids are substrates for human cytochrome P450c17","volume":"418","author":"Gupta","year":"2003","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0170","doi-asserted-by":"crossref","first-page":"14754","DOI":"10.1073\/pnas.2336107100","article-title":"A pathway for the metabolism of vitamin D3: unique hydroxylated metabolites formed during catalysis with cytochrome P450scc (CYP11A1)","volume":"100","author":"Guryev","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0175","series-title":"16th International Symposium on Microsomes and Drug Oxidation, Budapest, Hungary, September 3\u20137","first-page":"178","article-title":"CYP17 substrate specificity","author":"Pechurskaya","year":"2006"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0180","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1210\/me.2004-0271","article-title":"Cytochrome P450 17alpha hydroxylase\/17, 20 lyase (CYP17) function in cholesterol biosynthesis: identification of squalene monooxygenase (epoxidase) activity associated with CYP17 in Leydig cells","volume":"19","author":"Papadopoulos","year":"2005","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0185","doi-asserted-by":"crossref","first-page":"14284","DOI":"10.1021\/bi035512f","article-title":"Broad substrate specificity of human cytochrome P450 46A1 which initiates cholesterol degradation in the brain","volume":"42","author":"Mast","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0190","doi-asserted-by":"crossref","first-page":"20895","DOI":"10.1074\/jbc.270.36.20895","article-title":"Novel involvement of a mitochondrial steroid hydroxylase (P450c11) in xenobiotic metabolism","volume":"270","author":"Lund","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0195","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1080\/004982599238731","article-title":"Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine","volume":"29","author":"Niwa","year":"1999","journal-title":"Xenobiotica"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0200","doi-asserted-by":"crossref","first-page":"31","DOI":"10.2174\/157489207779561453","article-title":"Inhibitors of steroidal cytochrome P450 enzymes as targets for drug development","volume":"2","author":"Baston","year":"2007","journal-title":"Recent Pat. Anticancer Drug Discov."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0205","doi-asserted-by":"crossref","first-page":"163","DOI":"10.2174\/1381612805666230109214333","article-title":"Inhibitors of 17alpha-hydroxylase\/17, 20-lyase (CYP17): potential agents for the treatment of prostate cancer","volume":"5","author":"Njar","year":"1999","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0210","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0960-0760(96)00225-7","article-title":"Biochemistry and pharmacokinetics of potent non-steroidal cytochrome P450(17alpha) inhibitors","volume":"60","author":"Barrie","year":"1997","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0215","doi-asserted-by":"crossref","first-page":"2463","DOI":"10.1021\/jm00013a022","article-title":"Novel steroidal inhibitors of human cytochrome P45017 alpha (17 alpha-hydroxylase-C17, 20-lyase): potential agents for the treatment of prostatic cancer","volume":"38","author":"Potter","year":"1995","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0220","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1021\/bi00355a036","article-title":"NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins","volume":"25","author":"Porter","year":"1986","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0225","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/0968-0004(91)90059-5","article-title":"An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals","volume":"16","author":"Porter","year":"1991","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0230","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1073\/pnas.82.4.973","article-title":"Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains","volume":"82","author":"Porter","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"2\u20133","key":"10.1016\/j.bbapap.2010.06.021_bb0235","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1080\/03602530701498455","article-title":"Inhibition of cytochromes p450: existing and new promising therapeutic targets","volume":"39","author":"Schuster","year":"2007","journal-title":"Drug Metab. Rev."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0240","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.pharmthera.2005.07.006","article-title":"CYP 17- and CYP11B-dependent steroid hydroxylases as drug development targets","volume":"111","author":"Hakki","year":"2006","journal-title":"Pharmacol. Therap."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0245","doi-asserted-by":"crossref","first-page":"4210","DOI":"10.1021\/bi00132a009","article-title":"31P NMR spectroscopic studies on purified, native and cloned, expressed forms of NADPH-cytochrome P450 reductase","volume":"31","author":"Narayanasami","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0250","doi-asserted-by":"crossref","first-page":"3012","DOI":"10.1021\/bi00333a031","article-title":"Flavins of NADPH-cytochrome P-450 reductase: evidence for structural alteration of flavins in their one-electron-reduced semiquinone states from resonance Raman spectroscopy","volume":"24","author":"Sugiyama","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0255","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1038\/embor.2009.82","article-title":"Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase","volume":"10","author":"Aigrain","year":"2009","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0260","doi-asserted-by":"crossref","first-page":"8411","DOI":"10.1073\/pnas.94.16.8411","article-title":"Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes","volume":"94","author":"Wang","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0265","doi-asserted-by":"crossref","first-page":"29163","DOI":"10.1074\/jbc.M101731200","article-title":"NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer","volume":"276","author":"Hubbard","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0270","doi-asserted-by":"crossref","first-page":"11374","DOI":"10.1074\/jbc.M807868200","article-title":"Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450","volume":"284","author":"Hamdane","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0275","doi-asserted-by":"crossref","first-page":"8812","DOI":"10.1016\/S0021-9258(17)34250-3","article-title":"Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase","volume":"253","author":"Vermilion","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0280","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1021\/bi00510a004","article-title":"Studies on the microsomal mixed-function oxidase system: mechanism of action of hepatic NADPH-cytochrome P-450 reductase","volume":"20","author":"Iyanagi","year":"1981","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0285","doi-asserted-by":"crossref","first-page":"3714","DOI":"10.1016\/S0021-9258(18)83427-5","article-title":"Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components","volume":"244","author":"Lu","year":"1969","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0290","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1006\/bbrc.2001.5075","article-title":"An enzymatically active chimeric protein containing the hydrophilic form of NADPH-cytochrome P450 reductase fused to the membrane-binding domain of cytochrome b5","volume":"284","author":"Gilep","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0295","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1007\/s10541-005-0122-3","article-title":"Engineering of proteolytically stable NADPH-cytochrome P450 reductase","volume":"70","author":"Bonina","year":"2005","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0300","doi-asserted-by":"crossref","first-page":"17036","DOI":"10.1074\/jbc.273.27.17036","article-title":"Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase","volume":"273","author":"Bridges","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0305","doi-asserted-by":"crossref","first-page":"6536","DOI":"10.1074\/jbc.M111408200","article-title":"Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase","volume":"277","author":"Shen","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0310","doi-asserted-by":"crossref","first-page":"6103","DOI":"10.1128\/MCB.23.17.6103-6116.2003","article-title":"Identification of novel roles of the cytochrome p450 system in early embryogenesis: effects on vasculogenesis and retinoic Acid homeostasis","volume":"23","author":"Otto","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0315","doi-asserted-by":"crossref","first-page":"25895","DOI":"10.1074\/jbc.M303125200","article-title":"Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase","volume":"278","author":"Gu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0320","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0028-3908(76)90100-3","article-title":"Membrane capacitance measurements during acetylcholine action","volume":"15","author":"Dunning","year":"1976","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0325","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1097\/01.mop.0000236395.71956.5c","article-title":"P450 oxidoreductase deficiency: a new form of congenital adrenal hyperplasia","volume":"18","author":"Fluck","year":"2006","journal-title":"Curr. Opin. Pediatr."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0330","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1081\/ERC-200044134","article-title":"P450 oxidoreductase deficiency: a new disorder of steroidogenesis affecting all microsomal P450 enzymes","volume":"30","author":"Pandey","year":"2004","journal-title":"Endocr. Res."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0335","doi-asserted-by":"crossref","first-page":"2579","DOI":"10.1210\/me.2007-0245","article-title":"Modulation of human CYP19A1 activity by mutant NADPH P450 oxidoreductase","volume":"21","author":"Pandey","year":"2007","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0340","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1530\/eje.1.02172","article-title":"Clinical and biochemical description of a novel CYP21A2 gene mutation 962_963insA using a new 3D model for the P450c21 protein","volume":"155","author":"Janner","year":"2006","journal-title":"Eur. J. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0345","doi-asserted-by":"crossref","first-page":"3361","DOI":"10.1073\/pnas.81.11.3361","article-title":"Signal recognition particle is required for co-translational insertion of cytochrome P-450 into microsomal membranes","volume":"81","author":"Sakaguchi","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0350","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S0014-5793(99)01361-7","article-title":"A soluble NH(2)-terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria(1)","volume":"460","author":"Neve","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0355","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1021\/bi972046j","article-title":"Interaction of adrenodoxin with P4501A1 and its truncated form P450MT2 through different domains: differential modulation of enzyme activities","volume":"37","author":"Anandatheerthavarada","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0360","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0076-6879(96)72005-0","article-title":"N-terminal modifications that alter P450 membrane targeting and function","volume":"272","author":"Pernecky","year":"1996","journal-title":"Meth. Enzymol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0365","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/abbi.1993.1401","article-title":"Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme","volume":"305","author":"Gillam","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0370","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1006\/abbi.1994.1280","article-title":"Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties","volume":"312","author":"Gillam","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0375","doi-asserted-by":"crossref","first-page":"2651","DOI":"10.1073\/pnas.90.7.2651","article-title":"Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes","volume":"90","author":"Pernecky","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0380","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1006\/abbi.1996.9859","article-title":"Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus","volume":"339","author":"von Wachenfeldt","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0385","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1074\/jbc.275.4.2545","article-title":"Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding","volume":"275","author":"Cosme","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0390","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1006\/abbi.1993.1349","article-title":"Expression in Escherichia coli of functional cytochrome P450c17 lacking its hydrophobic amino-terminal signal anchor","volume":"304","author":"Sagara","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0395","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1083\/jcb.104.2.209","article-title":"Determination of the membrane topology of the phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4 using site-specific antibodies","volume":"104","author":"De Lemos-Chiarandini","year":"1987","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0400","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1002\/pro.5560040605","article-title":"A three-dimensional model of aromatase cytochrome P450","volume":"4","author":"Graham-Lorence","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0405","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/S0969-2126(98)00109-9","article-title":"A close family resemblance: the importance of structure in understanding cytochromes P450","volume":"6","author":"Peterson","year":"1998","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0410","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1134\/S0006297908070092","article-title":"Engineering, expression, and purification of \u201csoluble\u201d human cytochrome P45017alpha and its functional characterization","volume":"73","author":"Pechurskaya","year":"2008","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0415","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1006\/bbrc.1998.9889","article-title":"Some properties of mitochondrial adrenodoxin associated with its nonconventional electron donor function toward rabbit liver microsomal cytochrome P450 2B4","volume":"254","author":"Lehnerer","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0420","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1006\/abbi.1996.0086","article-title":"Recombinant human cytochrome P450 1A2 and an N-terminal-truncated form: construction, purification, aggregation properties, and interactions with flavodoxin, ferredoxin, and NADPH-cytochrome P450 reductase","volume":"327","author":"Dong","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0425","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.bbrc.2006.12.047","article-title":"Adrenodoxin supports reactions catalyzed by microsomal steroidogenic cytochrome P450s","volume":"353","author":"Pechurskaya","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0430","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0026-0495(71)90091-6","article-title":"Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control","volume":"20","author":"Estabrook","year":"1971","journal-title":"Metabolism"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0435","doi-asserted-by":"crossref","first-page":"12852","DOI":"10.1021\/bi980674a","article-title":"Interactions among P450 enzymes when combined in reconstituted systems: formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase","volume":"37","author":"Backes","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0440","doi-asserted-by":"crossref","first-page":"15807","DOI":"10.1021\/bi061803n","article-title":"Heteromeric complex formation between CYP2E1 and CYP1A2: evidence for the involvement of electrostatic interactions","volume":"45","author":"Kelley","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0445","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1021\/bi00004a018","article-title":"Substrate-dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase","volume":"34","author":"Cawley","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0450","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1124\/dmd.104.001578","article-title":"Interactions between CYP2C9 and CYP2C19 in reconstituted binary systems influence their catalytic activity: possible rationale for the inability of CYP2C19 to catalyze methoxychlor demethylation in human liver microsomes","volume":"33","author":"Hazai","year":"2005","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0455","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1124\/dmd.109.026500","article-title":"CYP2D6\u2013CYP2C9 protein\u2013protein interactions and isoform-selective effects on substrate binding and catalysis","volume":"37","author":"Subramanian","year":"2009","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0460","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1021\/bi0477900","article-title":"Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2","volume":"44","author":"Kelley","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0465","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1006\/abbi.1997.9995","article-title":"Competitive interactions between cytochromes P450 2A6 and 2E1 for NADPH-cytochrome P450 oxidoreductase in the microsomal membranes produced by a baculovirus expression system","volume":"342","author":"Tan","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0470","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0163-7258(03)00031-7","article-title":"Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes","volume":"98","author":"Backes","year":"2003","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0475","doi-asserted-by":"crossref","first-page":"33224","DOI":"10.1074\/jbc.M109.006064","article-title":"Organization of cytochrome P450 enzymes involved in sex steroid synthesis: protein\u2013protein interactions in lipid membranes","volume":"284","author":"Praporski","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.bbapap.2010.06.021_bb0480","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1124\/dmd.109.030155","article-title":"CYP2C9\u2013CYP3A4 protein\u2013protein interactions: role of the hydrophobic N-terminus","volume":"38","author":"Subramanian","year":"2010","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0485","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1677\/joe.1.06375","article-title":"Cytochrome b(5) modulation of 17{alpha} hydroxylase and 17\u201320 lyase (CYP17) activities in steroidogenesis","volume":"187","author":"Akhtar","year":"2005","journal-title":"J. Endocrinol."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0490","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1023\/A:1022101703670","article-title":"Molecular cloning and heterologous expression in E. coli of cytochrome P45017alpha. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species","volume":"68","author":"Gilep","year":"2003","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0495","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1023\/B:BIRY.0000026190.80583.c3","article-title":"Chimerogenesis in estimation of specificity and pathway directions for cytochrome p45017alpha catalyzed reactions","volume":"69","author":"Gilep","year":"2004","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0500","doi-asserted-by":"crossref","first-page":"3158","DOI":"10.1074\/jbc.273.6.3158","article-title":"Cytochrome b5 augments the 17, 20-lyase activity of human P450c17 without direct electron transfer","volume":"273","author":"Auchus","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0505","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.1021\/bi002305w","article-title":"Interaction of apo-cytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions","volume":"40","author":"Guryev","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2010.06.021_bb0510","doi-asserted-by":"crossref","first-page":"21204","DOI":"10.1074\/jbc.M301698200","article-title":"Identification of outer mitochondrial membrane cytochrome b5 as a modulator for androgen synthesis in Leydig cells","volume":"278","author":"Ogishima","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0515","doi-asserted-by":"crossref","first-page":"5832","DOI":"10.1111\/j.1742-4658.2005.04977.x","article-title":"Molecular identification of adrenal inner zone antigen as a heme-binding protein","volume":"272","author":"Min","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2010.06.021_bb0520","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1021\/bi051623y","article-title":"Human cytochrome b5 requires residues E48 and E49 to stimulate the 17, 20-lyase activity of cytochrome P450c17","volume":"45","author":"Naffin-Olivos","year":"2006","journal-title":"Biochemistry"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963910001809?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963910001809?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,6,2]],"date-time":"2023-06-02T00:15:12Z","timestamp":1685664912000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963910001809"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,1]]},"references-count":104,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2011,1]]}},"alternative-id":["S1570963910001809"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2010.06.021","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2011,1]]}}}