- CYP1A1/2 and prostaglandin H synthase catalyze reductive activation of inflammatory drug aristolochic acid and that results in DNA adduct formation2000 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Reductive activation of Cr(VI) by nitric oxide synthase2005 | First Faculty of Medicine
- Reductive activation of Cr(VI) by nitric oxide synthase2005 | Faculty of Physical Education and Sport
- The binding of aristolochic acid I to the active site of human cytochromes P450 1A1 and 1A2 explains their potential to reductively activate this human carcinogen2005 | Faculty of Science, First Faculty of Medicine, Faculty of Physical Education and Sport
- Reductive activation of environmental pollutants 3-nitrobenzanthrone and 2-nitrobenzanthrone2007 | Faculty of Science
- CYP1A1/2 and prostaglandin H synthase catalyze reductive activation of inflammatory drug aristolochic acid and that results in DNA adduct formation2000 | Faculty of Science
- Identification of human enzymes activating carcinogenic aristolochic acids: evidence for reductive activation by CYP1A1 and CYP1A22000 | Faculty of Science
- Identification of human enzymes activating carcinogenic aristolochic acids: evidence for reductive activation by CYP1A1 and CYP1A22000 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Evidence for reductive activation of carcinogenic aristolochic acids by prostaglandin H synthase - 32P-postlabeling analysis of DNA adduct formation2001 | Faculty of Science
- Evidence for reductive activation of carcinogenic aristolochic acids by prostaglandin H synthase - 32P-postlabeling analysis of DNA adduct formation2001 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Evidence for reductive activation of carcinogenic aristolochic acid by CYP1A1 and CYP1A2 enzymes: 32P-postlabelling analysis of DNA adduct formation1999 | Faculty of Science
- Comparison of DNA adduct formation by aristolochic acids in various in vitro activation systems by 32P-postlabelling: evidence for reductive activation by peroxidases1997 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Enhanced oxygen reduction activity with rare earth metal alloy catalysts in proton exchange membrane fuel cells2021 | Faculty of Mathematics and Physics
- Human enzymes involved in metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A22001 | Faculty of Science
- Human enzymes involved in metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A22001 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Comparison of DNA adduct formation by aristolochic acids in various in vitro activation systems by 32P-post-labelling: evidence for reductive activation by peroxidases1997 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Coparison of DNA adduct formation by aristolochic acids in various in vitro activation systems by 32p-post-labelling: evidence for reductive activation by peroxidases +11997 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Human enzymes involved in the metabolic activation of the environmental contaminant 3-nitrobenzanthrone: evidence for reductive activation by human NADPH:cytochrome P450 reductase2003 | Faculty of Science
- Human cytosolic enzymes involved in the metabolic activation of carcinogenic aristolochic acid: evidence for reductive activation by human NAD(P)H:quinone oxidoreductase2003 | Faculty of Science
- Human enzymes involved in the metabolic activation of the environmental contaminant 3-nitrobenzanthrone: evidence for reductive activation by human NADPH:cytochrome P450 reductase2003 | First Faculty of Medicine, Faculty of Mathematics and Physics
- Induction of cytochromes P450 1A1 and 1A2 suppresses formation of DNA adducts by carcinogenic aristolochic acid I in rats in vivo2016 | Faculty of Science
- 3-aminobenzanthrone, a human metabolite of the environmental pollutant 3-nitrobenzanthrone, forms DNA adducts after metabolic activation by human and rat liver microsomes: Evidence for activation by cytochrome P450 1A1 and P450 1A22004 | Faculty of Science
- Role of P450 1A1 and P450 1A2 in Bioactivation versus Detoxication of the Renal Carcinogen Aristolochic Acid I: Studies in Cyp1a1(-/-), Cyp1a2(-/-), and Cyp1a1/1a2(-/-) Mice2011 | Faculty of Science
- Bioactivation versus Detoxication of the Urothelial Carcinogen Aristolochic Acid I by Human Cytochrome P450 1A1 and 1A22012 | Faculty of Science
- The environmental pollutant and carcinogen 3-nitrobenzanthrone and its human metabolite 3-aminobenzanthrone are potent inducers of rat hepatic cytochromes P450 1A1 and-1A2 and NAD(P) H : quinone oxidoreductase2006 | Faculty of Science
- Enzymes involved in the metabolism of the carcinogen 2-nitroanisole: Evidence for its oxidative detoxication by human cytochromes P4502004 | Faculty of Science
- Induction of biotransformation enzymes by the carcinogenic air-pollutant 3-nitrobenzanthrone in liver, kidney and lung, after intra-tracheal instillation in rats2011 | Faculty of Science
- Identification of a genotoxic mechanism for 2-nitroanisole carcinogenicity and of its carcinogenic potential for humans2004 | Faculty of Science
- The Human Carcinogen Aristolochic Acid I Is Activated to Form DNA Adducts by Human NAD(P)H:quinone Oxidoreductase Without the Contribution of Acetyltransferases or Sulfotransferases2011 | Faculty of Science, First Faculty of Medicine, Faculty of Physical Education and Sport