@article{mihaich_erler_le blanc_gallagher_2015, title={Short-term fish reproduction assays with methyl tertiary butyl ether with zebrafish and fathead minnow: Implications for evaluation of potential for endocrine activity}, volume={34}, number={9}, journal={Environmental Toxicology and Chemistry}, author={Mihaich, E. and Erler, S. and Le Blanc, G. and Gallagher, S.}, year={2015}, pages={2013–2022} }
 @article{thomson_baldwin_wang_kwon_leblanc_2009, title={Annotation, phylogenetics, and expression of the nuclear receptors in Daphnia pulex}, volume={10}, journal={BMC Genomics}, author={Thomson, S. A. and Baldwin, W. S. and Wang, Y. H. and Kwon, G. and LeBlanc, G. A.}, year={2009} }
 @article{wang_leblanc_2009, title={Interactions of methyl farnesoate and related compounds with a crustacean retinoid X receptor}, volume={309}, ISSN={0303-7207}, url={http://dx.doi.org/10.1016/j.mce.2009.05.016}, DOI={10.1016/j.mce.2009.05.016}, abstractNote={While a functional role for the sesquiterpenoid hormone methyl farnesoate in arthropods has been recognized for decades, the identification of a receptor that mediates the action of this hormone remains equivocal. Luciferase reporter assays were used in the present study to evaluate the ability of methyl farnesoate and other putative ligands to activate gene transcription associated with the retinoid X receptor (RXR) and RXR:EcR heterodimeric complexes from the crustacean (Daphnia magna). The daphnid RXR constructs, transfected into HepG2 cells along with the reporter construct, significantly activated luciferase gene expression in response to tributyltin indicating that the crustacean RXR is indeed ligand activated. However, RXR was not activated by methyl farnesoate or other putative RXR ligands. Cells co-transfected with the daphnid RXR and EcR produced luciferase in response to ecdysteroids and this activation was significantly enhanced when cells were also provided either methyl farnesoate or other putative RXR ligands. This synergy among RXR and EcR ligands was not dependent upon the co-activator SRC-1 and did not correlate to a physiological response of daphnids to juvenoid hormones (male sex determination). Results indicate that methyl farnesoate, along with compounds that are functionally similar to methyl farnesoate synergize with ecdysteroids to activate the RXR:EcR receptor complex. However, this effect appears to be unrelated to the ability of these compounds to stimulate male sex determination.}, number={1-2}, journal={Molecular and Cellular Endocrinology}, publisher={Elsevier BV}, author={Wang, Ying H. and LeBlanc, Gerald A.}, year={2009}, month={Oct}, pages={109–116} }
 @article{le blanc_stuart_dunn_baldwin_1994, title={Effect of the plant compound indole-3-carbinol on hepatic cholesterol homoeostasis}, volume={32}, ISSN={["1873-6351"]}, DOI={10.1016/0278-6915(94)90007-8}, abstractNote={The aim of this study was to elucidate the effects of the compound indole-3-carbinol (I3C), which is found in cruciferous vegetables, on hepatic cholesterol homoeostasis and metabolism in male CD-1 mice. Oral administration of 500 and 750 mg I3C/kg/day to mice for 1 wk resulted in increased liver mass and microsomal protein content. Hepatic microsomal cholesterol levels were not significantly altered following treatment with 100 and 250 mg I3C/kg/day, but were significantly decreased following treatment with 500 and 750 mg/kg/day. Conversely, the lower doses of I3C administered decreased serum cholesterol levels whereas the higher doses of I3C had no effect on this parameter. Alterations in cholesterol homoeostasis by I3C were not related to liver hypertrophy, since administration of phenobarbital to mice increased liver size, but had no significant effect on hepatic microsomal or serum cholesterol levels. Activities of the hepatic enzymes cholesterol ester hydrolase and cholesterol 7 alpha-hydroxylase were not altered by I3C. However, 500 and 750 mg I3C/kg/day elevated the activity of hepatic acyl-CoA:cholesterol acyltransferase (ACAT), the enzyme responsible for the formation of hepatic cholesteryl esters. These results demonstrate that (a) I3C lowers serum cholesterol levels at concentrations that have no discernible effect on hepatic cholesterol homoeostasis, and (b) at higher doses of I3C, hepatic microsomal cholesterol levels are significantly lowered and ACAT activity is significantly elevated. These latter effects are not accompanied by changes in serum cholesterol levels and may represent compensatory mechanisms to restore cholesterol homoeostasis in the body. Mechanisms responsible for the effects of I3C on cholesterol homoeostasis are proposed.}, number={7}, journal={Food and Chemical Toxicology}, author={Le Blanc, G.A. and Stuart, J.D. and Dunn, S.E. and Baldwin, W.S}, year={1994}, month={Jul}, pages={633–639} }