Alain Belanger

Universite Laval (Canada) 
Molecular Biology, Biochemistry
"Alain Belanger"
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Grosse L, Pâquet S, Caron P, et al. (2013) Androgen glucuronidation: an unexpected target for androgen deprivation therapy, with prognosis and diagnostic implications. Cancer Research. 73: 6963-71
Giton F, Caron P, Bérubé R, et al. (2010) Plasma estrone sulfate assay in men: Comparison of radioimmunoassay, mass spectrometry coupled to gas chromatography (GC-MS), and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Clinica Chimica Acta; International Journal of Clinical Chemistry. 411: 1208-13
Trottier J, El Husseini D, Perreault M, et al. (2010) The human UGT1A3 enzyme conjugates norursodeoxycholic acid into a C23-ester glucuronide in the liver. The Journal of Biological Chemistry. 285: 1113-21
Barbier O, Bélanger A. (2008) Inactivation of androgens by UDP-glucuronosyltransferases in the human prostate. Best Practice & Research. Clinical Endocrinology & Metabolism. 22: 259-70
Luu-The V, Bélanger A, Labrie F. (2008) Androgen biosynthetic pathways in the human prostate. Best Practice & Research. Clinical Endocrinology & Metabolism. 22: 207-21
Kaeding J, Bélanger J, Caron P, et al. (2008) Calcitrol (1alpha,25-dihydroxyvitamin D3) inhibits androgen glucuronidation in prostate cancer cells. Molecular Cancer Therapeutics. 7: 380-90
Nguyen N, Bonzo JA, Chen S, et al. (2008) Disruption of the ugt1 locus in mice resembles human Crigler-Najjar type I disease. The Journal of Biological Chemistry. 283: 7901-11
Kaeding J, Bouchaert E, Bélanger J, et al. (2008) Activators of the farnesoid X receptor negatively regulate androgen glucuronidation in human prostate cancer LNCAP cells. The Biochemical Journal. 410: 245-53
Chouinard S, Barbier O, Bélanger A. (2007) UDP-glucuronosyltransferase 2B15 (UGT2B15) and UGT2B17 enzymes are major determinants of the androgen response in prostate cancer LNCaP cells. The Journal of Biological Chemistry. 282: 33466-74
Shet MS, Fisher CW, Tremblay Y, et al. (2007) Comparison of the 17 alpha-hydroxylase/C17,20-lyase activities of porcine, guinea pig and bovine P450c17 using purified recombinant fusion proteins containing P450c17 linked to NADPH-P450 reductase. Drug Metabolism Reviews. 39: 289-307
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