The role of glutathione and... [Adv Enzymol Relat Areas Mol Biol. 1969] - PubMed

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Mercapturic acid formation and enzyme-catalyzed conjugations with glutathione in pigeons. [Biochim Biophys Acta. 1969]
Mercapturic acid formation and enzyme-catalyzed conjugations with glutathione in pigeons.
Wit JG, Leeuwangh P. Biochim Biophys Acta. 1969 Apr 1; 177(2):329-35.
Review The nature and distribution of enzymes catalyzing the conjugation of glutathione with foreign compounds. [Drug Metab Rev. 1973]
Review The nature and distribution of enzymes catalyzing the conjugation of glutathione with foreign compounds.
Chasseaud LF. Drug Metab Rev. 1973; 2(2):185-220.
Review Species differences in drug metabolism. [Annu Rev Pharmacol. 1970]
Review Species differences in drug metabolism.
Hucker HB. Annu Rev Pharmacol. 1970; 10:99-118.
Distribution of enzymes that catalyse reactions of glutathione with alpha beta-unsaturated compounds. [Biochem J. 1973]
Distribution of enzymes that catalyse reactions of glutathione with alpha beta-unsaturated compounds.
Chasseaud LF. Biochem J. 1973 Apr; 131(4):765-9.
The metabolic formation of mercapturic acids from allyl halides. [Xenobiotica. 1972]
The metabolic formation of mercapturic acids from allyl halides.
Kaye CM, Clapp JJ, Young L. Xenobiotica. 1972 Mar; 2(2):129-39.

Metabolomic profiling unravels DNA adducts in human breast that are formed from peroxidase mediated activation of estrogens to quinone methides. [PLoS One. 2013]
Metabolomic profiling unravels DNA adducts in human breast that are formed from peroxidase mediated activation of estrogens to quinone methides.
Gaikwad NW. PLoS One. 2013; 8(6):e65826. Epub 2013 Jun 6.
Molecular mechanisms of ursodeoxycholic Acid toxicity & side effects: ursodeoxycholic Acid freezes regeneration & induces hibernation mode. [Int J Mol Sci. 2012]
Molecular mechanisms of ursodeoxycholic Acid toxicity & side effects: ursodeoxycholic Acid freezes regeneration & induces hibernation mode.
Kotb MA. Int J Mol Sci. 2012; 13(7):8882-914. Epub 2012 Jul 17.
Oxidative processing of latent Fas in the endoplasmic reticulum controls the strength of apoptosis. [Mol Cell Biol. 2012]
Oxidative processing of latent Fas in the endoplasmic reticulum controls the strength of apoptosis.
Anathy V, Roberson E, Cunniff B, Nolin JD, Hoffman S, Spiess P, Guala AS, Lahue KG, Goldman D, Flemer S, et al. Mol Cell Biol. 2012 Sep; 32(17):3464-78. Epub 2012 Jul 2.

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The role of glutathione and glutathione S-transferases in mercapturic acid biosy...
The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis.
Adv Enzymol Relat Areas Mol Biol. 1969 ;32:173-219.

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