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Pelkonen, Paivi, Lang, Matti A., Wild, Christopher P., Negishi, Masahiko and Juvonen, Risto O. (1994) Activation of aflatoxin B1 by mouse CYP2A enzymes and cytotoxicity in recombinant yeast cells. European Journal of Pharmacology: Environmental Toxicology and Pharmacology, 292 1: 67-73. doi:10.1016/0926-6917(94)90027-2 45   26 0
Yoshioka, Hidefumi, Lang, Matti, Wong, Garry and Negishi, Masahiko (1990) A specific cis-acting element regulates in vitro transcription of sex-dependent mouse steroid 16α-hydroxylase (C-P450 16α) gene. Journal of Biological Chemistry, 265 24: 14612-14617. 32   18 Cited 14 times in Scopus14
Kocer, Zeliha, Raunio, Hannu, Pasanen, Markku, Arvela, Pentti, Raiskila, Tero, Honkakoski, Paavo, Lang, Matti A., Negishi, Masahiko and Pelkonen, Olavi (1991) Comparison between cobalt and pyrazole in the increased expression of coumarin 7-hydroxylase in mouse liver. Biochemical Pharmacology, 41 3: 462-465. doi:10.1016/0006-2952(91)90547-I 35   14 Cited 18 times in Scopus18 0
Pelkonen, Paivi, Lang, Matti A., Negishi, Masahiko, Wild, Christopher P. and Juvonen, Risto O. (1997) Interaction of aflatoxin B-1 with cytochrome P450 2A5 and its mutants: Correlation with metabolic activation and toxicity. Chemical Research in Toxicology, 10 1: 85-90. doi:10.1021/tx960078m 21   28 Cited 29 times in Scopus29 0
Chen, Yuan-Tsong, Lang, Matti A., Jensen, Nancy M., Negishi, Masahiko, Tukey, Robert H., Sidransky, Ellen, Guenther, Thomas M. and Nebert, Daniel W. (1982) Similarities between mouse and rat-liver microsomal cytochromes P-450 induced by 3-methylcholanthrene. Evidence from catalytic, immunologic, and recombinant DNA studies. European Journal of Biochemistry, 122 2: 361-368. doi:10.1111/j.1432-1033.1982.tb05889.x 32   27 Cited 9 times in Scopus9 0
Hempel, Nadine, Wang, Hongbing, LeCluyse, Edward L., McManus, Michael E. and Negishi, Masahiko (2004) The human sulfotransferase SULT1A1 gene is regulated in a synergistic manner by Sp1 and GA binding protein. Molecular Pharmacology, 66 6: 1690-1701. doi:10.1124/mol.104.003350 78   30 Cited 34 times in Scopus34 0