The involvement of human placental microsomal cytochrome P-450 in aromatization
Thompson, E. A., Jr.; Siiteri, P. K. The involvement of human placental microsomal cytochrome P-450 in aromatization J. Biol. Chem. 1974, 249, 5373-5378
Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis
Simpson, E. R.; Mahendroo, M. S.; Means, G. D.; Kilgore, M. W.; Hinshelwood, M. M.; Graham-Lorence, S.; Amarneh, B.; Ito, Y.; Fisher, C. R.; Michael, M. D. Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis Endocr. Rev. 1994, 15, 342-355
Core glycosylation of cytochrome P-450(arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen
Shimozawa, O.; Sakaguchi, M.; Ogawa, H.; Harada, N.; Mihara, K.; Omura, T. Core glycosylation of cytochrome P-450(arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen J. Biol. Chem. 1993, 268, 21399-21402
Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis
Amarneh, B.; Corbin, C. J.; Peterson, J. A.; Simpson, E. R.; Graham-Lorence, S. Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis Mol. Endocrinol. 1993, 7, 1617-1624
Structural basis for androgen specificity and oestrogen synthesis in human aromatase
Ghosh, D.; Griswold, J.; Erman, M.; Pangborn, W. Structural basis for androgen specificity and oestrogen synthesis in human aromatase Nature 2009, 457, 219-223
In; Giudice, L. C. Evers, J. L. H. Healy, D. L. Wiley-Blackwell: Oxford, U.K. DOI: 10.1002/9781444398519.ch35.
Bulun, S. E.; Attar, E.; Gurates, B.; Chen, Y.-H.; Tokunaga, H.; Monsivais, D.; Pavone, M. E. Medical Therapies: Aromatase Inhibitors. In Endometriosis: Science and Practice; Giudice, L. C.; Evers, J. L. H.; Healy, D. L., Eds.; Wiley-Blackwell: Oxford, U.K., 2012; DOI: 10.1002/9781444398519.ch35.
Aromatase inhibitors in the treatment of recurrent ovarian granulosa cell tumors: Brief report and review of the literature
AlHilli, M.; Long, H.; Podratz, K.; Bakkum-Gamez, J. Aromatase inhibitors in the treatment of recurrent ovarian granulosa cell tumors: brief report and review of the literature J. Obstet. Gynaecol. Res. 2012, 38, 340-344
Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization
Yoshida, N.; Osawa, Y. Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization Biochemistry 1991, 30, 3003-3010
Mutagenesis study at a postulated hydrophobic region near the active site of aromatase cytochrome P450
Zhou, D.; Cam, L. L.; Laughton, C. A.; Korzekwa, K. R.; Chen, S. Mutagenesis study at a postulated hydrophobic region near the active site of aromatase cytochrome P450 J. Biol. Chem. 1994, 269, 19501-19508
A three-dimensional model of aromatase cytochrome P450
Graham-Lorence, S.; Amarneh, B.; White, R. E.; Peterson, J. A.; Simpson, E. R. A three-dimensional model of aromatase cytochrome P450 Protein Sci. 1995, 4, 1065-1080
Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase
Hong, Y.; Yu, B.; Sherman, M.; Yuan, Y. C.; Zhou, D.; Chen, S. Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase Mol. Endocrinol. 2007, 21, 401-414
Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase
Hong, Y.; Cho, M.; Yuan, Y. C.; Chen, S. Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase Biochem. Pharmacol. 2008, 75, 1161-1169
Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of a stable antigenic complex
Lala, P.; Higashiyama, T.; Erman, M.; Griswold, J.; Wagner, T.; Osawa, Y.; Ghosh, D. Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of a stable antigenic complex J. Steroid Biochem. Mol. Biol. 2004, 88, 235-245
X-ray structure of human aromatase reveals an androgen-specific active site
Ghosh, D.; Griswold, J.; Erman, M.; Pangborn, W. X-ray structure of human aromatase reveals an androgen-specific active site J. Steroid Biochem. Mol. Biol. 2010, 118, 197-202
New structure-activity relationships of A- and D-ring modified steroidal aromatase inhibitors: Design, synthesis, and biochemical evaluation
Varela, C.; Tavares da Silva, E. J.; Amaral, C.; Correia da Silva, G.; Baptista, T.; Alcaro, S.; Costa, G.; Carvalho, R. A.; Teixeira, N. A.; Roleira, F. M. New structure-activity relationships of A- and D-ring modified steroidal aromatase inhibitors: design, synthesis, and biochemical evaluation J. Med. Chem. 2012, 55, 3992-4002
Aromatase and dual aromatase-steroid sulfatase inhibitors from the letrozole and vorozole templates
Wood, P. M.; Woo, L. W.; Thomas, M. P.; Mahon, M. F.; Purohit, A.; Potter, B. V. Aromatase and dual aromatase-steroid sulfatase inhibitors from the letrozole and vorozole templates ChemMedChem 2011, 6, 1423-1438
Structure-based design of potent aromatase inhibitors by high-throughput docking
Caporuscio, F.; Rastelli, G.; Imbriano, C.; Del Rio, A. Structure-based design of potent aromatase inhibitors by high-throughput docking J. Med. Chem. 2011, 54, 4006-4017
Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
Bahar, I.; Atilgan, A. R.; Erman, B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential Folding Des. 1997, 2, 173-181
Inhibition of drug metabolizing cytochrome P450s by the aromatase inhibitor drug letrozole and its major oxidative metabolite 4,4'-methanol- bisbenzonitrile in vitro
Jeong, S. W., M.; Flockhart, D.; Zerusenav, D Inhibition of drug metabolizing cytochrome P450s by the aromatase inhibitor drug letrozole and its major oxidative metabolite 4,4′-methanol-bisbenzonitrile in vitro Cancer Chemother. Pharmacol. 2009, 64, 867-875
CYP3A4 and CYP2A6 Are Involved in the Biotransformation of Letrozole (Femara)
ISSX: Washington, DC
Wirz, B.; Valle, B.; Parkinson, A. CYP3A4 and CYP2A6 Are Involved in the Biotransformation of Letrozole (Femara). Proceedings of 7th North American ISSX Meeting; ISSX: Washington, DC, 1996; p 359.
An overview of the pharmacology and pharmacokinetics of the newer generation aromatase inhibitors anastrozole, letrozole, and exemestane
Budzar, A. U.; Roberston, J. F.; Eiermann, W.; Nabholtz, J. M. An overview of the pharmacology and pharmacokinetics of the newer generation aromatase inhibitors anastrozole, letrozole, and exemestane Cancer 2002, 95, 2006-2016
Exemestane's 17-hydroxylated metabolite exerts biological effects as an androgen
Ariazi, E. A.; Leitao, A.; Oprea, T. I.; Chen, B.; Louis, T.; Bertucci, A. M.; Sharma, C. G.; Gill, S. D.; Kim, H. R.; Shupp, H. A.; Pyle, J. R.; Madrack, A.; Donato, A. L.; Cheng, D.; Paige, J. R.; Jordan, V. C. Exemestane's 17-hydroxylated metabolite exerts biological effects as an androgen Mol. Cancer Ther. 2007, 6, 2817-2827
Convenient method for the functionalization of the 4- and 6-positions of the androgen skeleton
Morton, D.; Dick, A. R.; Ghosh, D.; Davies, H. M. L. Convenient method for the functionalization of the 4- and 6-positions of the androgen skeleton Chem. Commun. 2012, 48, 5838-5840
Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3
Anzenbacherova, E.; Bec, N.; Anzenbacher, P.; Hudecek, J.; Soucek, P.; Jung, C.; Munro, A. W.; Lange, R. Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3 Eur. J. Biochem. 2000, 267, 2916-2920
Structural flexibility and functional versatility of mammalian P450 enzymes
Negishi, M.; Uno, T.; Darden, T. A.; Sueyoshi, T.; Pedersen, L. G. Structural flexibility and functional versatility of mammalian P450 enzymes FASEB J. 1996, 10, 683-689
Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: Conformational flexibility and histidine ligation state
Xu, L. H.; Fushinobu, S.; Ikeda, H.; Wakagi, T.; Shoun, H. Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: conformational flexibility and histidine ligation state J. Bacteriol. 2009, 191, 1211-1219
Classical carbonyl reactivity enables a short synthesis of the core structure of acutumine
Moreau, R. J.; Sorensen, E. J. Classical carbonyl reactivity enables a short synthesis of the core structure of acutumine Tetrahedron 2007, 63, 6446-6453
Development of intravascular contrast agents for MRI using gadolinium chelates
Kittigowittana, K.; Yang, C. T.; Cheah, W. C.; Chuang, K. H.; Tuang, C. Y.; Chang, Y. T.; Golay, X.; Bates, R. W. Development of intravascular contrast agents for MRI using gadolinium chelates ChemMedChem 2011, 6, 781-787
Structural basis for the selective inhibition of human 3β-hydroxysteroid dehydrogenase 1 in human breast tumor MCF-7 cells
Thomas, J. L.; Bucholtz, K. M.; Sun, J.; Mack, V. L.; Kacsoh, B. Structural basis for the selective inhibition of human 3β-hydroxysteroid dehydrogenase 1 in human breast tumor MCF-7 cells Mol. Cell. Endocrinol. 2009, 301, 174-182
Refinement of macromolecular structures by the maximum-likelihood method
Murshudov, G. N.; Vagin, A. A.; Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D: Biol. Crystallogr. 1997, 53, 240-255
Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank Nucleic Acids Res. 2000, 28, 235-242