Results 151 to 160 of about 53,054 (215)
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Natural and synthetic inhibitors of UDP-glucuronosyltransferase
Pharmacology & Therapeutics, 2001Glucuronidation is a major detoxification pathway in vertebrates. The reaction is catalyzed by a family of UDP-glucuronosyltransferases (UGTs) and involves conjugation of many endobiotic and xenobiotic substances with glucuronic acid, forming inactive water-soluble glucuronides.
K, Grancharov +3 more
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Isolation and purification of UDP-glucuronosyltransferases
Chemical Research in Toxicology, 1990UDPGTs are members of a class of enzymes located in the endoplasmic reticulum and are encoded by a multigene family. These proteins are responsible for the glucuronidation of hundreds of xenobiotics of many chemical classes and many endogenous substances such as steroid hormones, bile acids, and bilirubin.
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Development of Human Liver UDP-Glucuronosyltransferases
Developmental Pharmacology and Therapeutics, 2017The development of multiple UDPGT activities towards eight substrates has been studied in fetal term and adult post-mortem (less than 5 h after death) liver samples. Most fetal and term liver activities were less than 14% of adult values, except that towards 5-hydroxytryptamine which was present in fetal and term liver at adult levels.
B, Burchell +6 more
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UDP-glucuronosyltransferases: a family of detoxifying enzymes
Trends in Pharmacological Sciences, 1990Glucuronidation is an important process in the metabolism of xenobiotic and endogenous substances leading to enhancement of excretion of these compounds from the body. A multigene family encodes a number of UDP-glucuronosyltransferase enzymes which catalyse this route of metabolism.
T R, Tephly, B, Burchell
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Regulation of UDP glucuronosyltransferases in the gastrointestinal tract
Toxicology and Applied Pharmacology, 2004The UDP glucuronosyltransferases (UGT) of the gastrointestinal (GI) tract have a crucial role in protection against the toxic effects of lipophilic chemicals in the environment. UGTs such as UGT1A7, UGT1A8, and UGT1A10 are exclusively expressed in gastrointestinal tissues, each with a unique tissue distribution pattern that is subject to ...
Gregory, Philip A +3 more
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UDP glucuronosyltransferase in the cirrhotic rat liver
Journal of Gastroenterology and Hepatology, 1996AbstractIn patients with cirrhosis, the elimination of drugs metabolized by glucuronidation is relatively preserved, in comparison with the metabolism of drugs by oxidation. This study explores this phenomenon at a molecular level. In cirrhotic rat livers the content of UDPâglucuronosyltransferase (UGT) was examined by immunohistochemistry and ...
H S, Debinski +7 more
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UDP-glucuronosyltransferases in human intestinal mucosa
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1998While UDP-glucuronosyltransferases (UGTs) are known to be expressed at high levels in human liver, relatively little is known about extrahepatic expression. In the present study, UGT2B family isoforms involved in the glucuronidation of steroid hormones and bile acids have been characterized in microsomes prepared from jejunum, ileum and colon from six ...
A, Radominska-Pandya +6 more
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GLUCURONIDATION AND THE UDP-GLUCURONOSYLTRANSFERASES IN HEALTH AND DISEASE
Drug Metabolism and Disposition, 2004This article is an updated report of a symposium held at the June 2000 annual meeting of the American Society for Pharmacology and Experimental Therapeutics in Boston. The symposium was sponsored by the ASPET Divisions for Drug Metabolism and Molecular Pharmacology.
Wells, Peter G +10 more
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Cloning and Characterization of a Canine UDP-Glucuronosyltransferase
Archives of Biochemistry and Biophysics, 2001UDP-glucuronosyltransferases (UGTs) are a major family of enzymes catalyzing the transfer of glucuronic acid to a range of endogenous compounds and xenobiotics facilitating their elimination in either urine or bile. Although the dog is commonly used in drug metabolism studies, relatively little is known about the expression and activity of UGTs in this
M G, Soars +3 more
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Polymorphisms of UDP-Glucuronosyltransferase and Pharmacokinetics of Irinotecan
Therapeutic Drug Monitoring, 2002Irinotecan is a prodrug that is hydrolyzed by carboxylesterase in vivo to form an active metabolite SN-38. SN-38 is further conjugated and detoxified by UDP-glucuronosyltransferase (UGT) to yield its beta-glucuronide (SN-38G). Although irinotecan is widely used, the drug causes unpredictably severe, occasionally fatal, toxicity of leukopenia or ...
Yuichi, Ando +5 more
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