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                       Dorval J. and A. Hontela. (2003). Role of glutathione redox cycle and catalase in defense against oxidative
                          stress induced by endosulfan in adrenocortical cells of rainbow trout (Oncorhynchus mykiss). Toxicol.
                          Appl. Pharmacol., 192, 191–200.
                       Dorval, J., V. Leblond, C. Deblois, and A. Hontela. (2005). Oxidative stress and endocrine endpoints in white
                          sucker (Catostomus commersoni) from a river impacted by agricultural chemicals. Environ. Toxicol. Chem.,
                          24, 1273–1280.
                       Dorval, J., V. S. Leblond, and A. Hontela. (2003). Oxidative stress and loss of cortisol secretion in adreno-
                          cortical cells of rainbow trout (Oncorhynchus mykiss) exposed in vitro to endosulfan, an organochlorine
                          pesticide. Aquat. Toxicol., 63, 229–241.
                       Dowla, H. A., M. Panamangalore, and M. E. Byers. (1996). Comparative inhibition of enzymes of human
                          erythrocytes and plasma in vitro by agricultural chemicals. Arch. Environ. Contam. Toxicol., 31, 107–114.
                       Eaton, D. L. and T. K. Bammler. (1999). Concise review of the glutathione S-transferases and their significance
                          to toxicology. Toxicol. Sci., 49, 156–164.
                       Eggler, A. L., G. Liu, J. M. Pezzuto, R. B. van Breeman, and A. D. Mesecar. (2005). Modifying specific
                          cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2
                          domain Neh2. PNAS, 102, 10070–10075.
                       El-Alawi, Y. S., X.-D. Huang, D. G. Dixon, and B. M Greenberg. (2002). Quantitative structure–activity
                          relationship for the photoinduced toxicity of polycyclic aromatic hydrocarbons to the luminescent bacteria
                          Vibrio fischeri. Environ. Toxicol. Chem., 21, 2225–2232.
                       Elia,  A. C.,  W.  T.  Waller, and S. J. Norton. (2002). Biochemical responses of bluegill sunfish (Lepomis
                          macrochirus, Rafinesque) to atrazine induced oxidative stress. Bull. Environ. Contam. Toxicol., 68, 809–816.
                       Ellis, E. M., C. M. Slattery, and J. D. Hayes. (2003). Characterization of the rat aflatoxin B 1  aldehyde reductase
                          gene, AKR7A1: structure and chromosomal localization of AKR7A1 as well as identification of antioxidant
                          response elements in the gene promoter. Carcinogenesis, 24, 727–737.
                       Elskus, A. A., E. Monosson, A. E. McElroy, J. J. Stegeman, and D. S. Woltering. (1999). Altered CYP1A
                          expression in Fundulus heteroclitus adults and larvae: a sign of pollution resistance? Aquat. Toxicol., 45,
                          99–113.
                       Eufemia, N. A., T. K. Collier, J. E. Stein, D. E. Watson, and R. T. Di Giulio. (1997). Biochemical responses
                          to sediment-associated contaminants in brown bullhead (Ameriurus nebulosus) from the Niagara River
                          ecosystem. Ecotoxicology, 6, 13–34.
                       Fabacher, D. L., E. E. Little, S. B. Jones, E. C. DeFabo, and L. J. Webber. (1994). Ultraviolet-B radiation and
                          the immune response of rainbow trout. In Modulators of Fish Immune Responses, Stolen, J. S. and Fletcher,
                          T. C., Eds., SOS Publications, Fair Haven, NJ, pp. 205–217.
                       Fatima, M., I. Ahmad, I. Sayeed, M. Athar, and S. Raisuddin. (2000). Pollutant-induced over-activation of
                          phagocytes is concomitantly associated with peroxidative damage in fish tissues.  Aquat. Toxicol.,  49,
                          243–250.
                       Favreau, L. V. and C. B. Pickett. (1991). Transcriptional regulation of the rat NAD(P)H:quinone oxidoreductase
                          gene: identification of regulatory elements controlling basal level expression and inducible expression by
                          planar aromatic compounds and phenolic antioxidants. J. Biol. Chem., 266, 4556–4561.
                       Field, L. S., E. Luk, and V. C. Culotta. (2002). Copper chaperones: personal escorts for metal ions. J. Bioenerg.
                          Biomembr., 34, 373–379.
                       Finkel, T. (2000). Redox-dependent signal transduction. FEBS Lett., 476, 52–54.
                       Finkel, T. and N. J. Holbrook. (2000). Oxidants, oxidative stress and the biology of ageing. Nature, 408,
                          239–247.
                       Förlin, L., P. Lemaire, and D. R. Livingstone. (1995). Comparative studies of hepatic xenobiotic metabolizing
                          and antioxidant enzymes in different fish species. Mar. Environ. Res., 39, 201–204.
                       Förlin, L., S. Blom, M. Celander, and J. Sturve. (1996). Effects on UDP glucuronosyl transferase, glutathione
                          transferase, DT-diaphorase, and glutathione reductase activities in rainbow trout liver after long-term
                          exposure to PCB. Mar. Environ. Res., 42, 213–216.
                       Foster, C. E., M. A. Bianchet, P. Talalay, M. Faig, and L. M. Amzel. (2000). Structures of mammalian cytosolic
                          quinone reductases. Free Radic. Biol. Med., 29, 241–245.
                       Fridovich, I. (1978). The biology of oxygen radicals. Science, 201, 875–880.
                       Fridovich, I. (1995). Superoxide radical and superoxide dismutases. Annu. Rev. Biochem., 64, 97–112.
                       Fridovich, I. (1998). An overview of oxyradicals in medical biology. Adv. Mol. Cell. Biol., 25, 1–14.
                       Fridovich, I. (2004). Mitochondria: are they the seat of senescence? Aging Cell, 3, 13–16.
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