Relevant bibliographies by topics / UDP-glucuronosyltransferase

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Academic literature on the topic 'UDP-glucuronosyltransferase'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "UDP-glucuronosyltransferase"

1

Matsui, M., and F. Nagai. "Genetic deficiency of androsterone UDP-glucuronosyltransferase activity in Wistar rats is due to the loss of enzyme protein." Biochemical Journal 234, no. 1 (1986): 139–44. http://dx.doi.org/10.1042/bj2340139.

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Hepatic microsomal UDP-glucuronosyltransferases towards androsterone and testosterone were purified by chromatofocusing and UDP-hexanolamine affinity chromatography in Wistar rats which had genetic deficiency of androsterone UDP-glucuronosyltransferase activity. In rats with the high-activity phenotype, androsterone (the 3-hydroxy androgen) UDP-glucuronosyltransferase was eluted at about pH 7.4 and had a subunit Mr of 52 000, whereas testosterone (the 17-hydroxy steroid) UDP-glucuronosyltransferase was eluted at about pH 8.4 and had a subunit Mr of 50 000. The transferase that conjugates both
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Jackson, M. R., L. R. McCarthy, D. Harding, S. Wilson, M. W. H. Coughtrie, and B. Burchell. "Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA." Biochemical Journal 242, no. 2 (1987): 581–88. http://dx.doi.org/10.1042/bj2420581.

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A cDNA clone (HLUG 25) encoding the complete sequence of a human liver UDP-glucuronosyltransferase was isolated from a lambda gt11 human liver cDNA library. The library was screened by hybridization to a partial-length human UDP-glucuronosyltransferase cDNA (pHUDPGT1) identified from a human liver pEX cDNA expression library by using anti-UDP-glucuronosyltransferase antibodies. The authenticity of the cDNA clone was confirmed by hybrid-select translation and extensive sequence homology to rat liver UDP-glucuronosyltransferase cDNAs. The sequence of HLUG 25 cDNA was determined to be 2104 base-p
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Falany, C. N., M. D. Green, E. Swain та T. R. Tephly. "Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases". Biochemical Journal 238, № 1 (1986): 65–73. http://dx.doi.org/10.1042/bj2380065.

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Purified preparations of rat liver 17-hydroxysteroid, 3-hydroxyandrogen and p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferases were further characterized as to their substrate specificities, phospholipid-dependency and physical properties. The two steroid UDP-glucuronosyltransferases were shown to exhibit strict stereospecificity with respect to the conjugation of steroids and bile acids. These enzymes have been renamed 17 beta-hydroxysteroid and 3 alpha-hydroxysteroid UDP-glucuronosyltransferase to reflect this specificity for important endogenous substrates. An endog
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4

Golovinsky, E., Z. Naydenova, and K. Grancharov. "UDP-Glucuronosyltransferase inhibitors." European Journal of Drug Metabolism and Pharmacokinetics 23, no. 4 (1998): 453–56. http://dx.doi.org/10.1007/bf03189994.

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BÁNHEGYI, Gábor, László BRAUN, Paola MARCOLONGO, et al. "Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles." Biochemical Journal 315, no. 1 (1996): 171–76. http://dx.doi.org/10.1042/bj3150171.

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The transport of glucuronides synthesized in the luminal compartment of the endoplasmic reticulum by UDP-glucuronosyltransferase isoenzymes was studied in rat liver microsomal vesicles. Microsomal vesicles were loaded with p-nitrophenol glucuronide (5 mM), phenolphthalein glucuronide or UDP-glucuronic acid, by a freeze–thawing method. It was shown that: (i) the loading procedure resulted in millimolar intravesicular concentrations of the different loading compounds; (ii) addition of UDP-glucuronic acid (5 mM) to the vesicles released both intravesicular glucuronides within 1 min; (iii) glucuro
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Little, J. M., R. Lester, F. Kuipers, et al. "Variability of human hepatic UDP-glucuronosyltransferase activity." Acta Biochimica Polonica 46, no. 2 (1999): 351–63. http://dx.doi.org/10.18388/abp.1999_4168.

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The availability of a unique series of liver samples from human subjects, both control patients (9) and those with liver disease (6; biliary atresia (2), retransplant, chronic tyrosinemia type I, tyrosinemia, Wilson's disease) allowed us to characterize human hepatic UDP-glucuronosyltransferases using photoaffinity labeling, immunoblotting and enzymatic assays. There was wide inter-individual variation in photoincorporation of the photoaffinity analogs, [32P]5-azido-UDP-glucuronic acid and [32P]5-azido-UDP-glucose and enzymatic glucuronidation of substrates specific to the two subfamilies of U
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Radominska-Pandya, A., J. Little, and P. Czernik. "Human UDP-Glucuronosyltransferase 2B7." Current Drug Metabolism 2, no. 3 (2001): 283–98. http://dx.doi.org/10.2174/1389200013338379.

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Leaver, Michael J., Joy Wright, Paul Hodgson, Evridiki Boukouvala, and Stephen G. George. "Piscine UDP-glucuronosyltransferase 1B." Aquatic Toxicology 84, no. 3 (2007): 356–65. http://dx.doi.org/10.1016/j.aquatox.2007.06.015.

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Roy Chowdhury, J., N. Roy Chowdhury, C. N. Falany, T. R. Tephly, and I. M. Arias. "Isolation and characterization of multiple forms of rat liver UDP-glucuronate glucuronosyltransferase." Biochemical Journal 233, no. 3 (1986): 827–37. http://dx.doi.org/10.1042/bj2330827.

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UDP-glucuronosyltransferase (EC 2.4.1.17) activity was solubilized from male Wistar rat liver microsomal fraction in Emulgen 911, and six fractions with the transferase activity were separated by chromatofocusing on PBE 94 (pH 9.4 to 6.0). Fraction I was further separated into Isoforms Ia, Ib and Ic by affinity chromatography on UDP-hexanolamine-Sepharose 4B. UDP-glucuronosyltransferase in Fraction III was further purified by rechromatofocusing (pH 8.7 to 7.5). UDP-glucuronosyltransferases in Fractions IV and V were purified by UDP-hexanolamine-Sepharose chromatography. The transferase isoform
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Haque, Md Azizul, Laila Shamima Sharmin, Mohd Harun or Rashid, MA Alim, ARM Saifuddin Ekram, and Syed Ghulam Mogni Mowla. "Crigler-Najjar Syndrome Type 2 in a Young Adult." Journal of Medicine 12, no. 1 (2011): 86–88. http://dx.doi.org/10.3329/jom.v12i1.6359.

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Crigler-Najjar syndrome type 2 in an autosomal recessive congenital non-hemolytic hyperbilirubinemia caused by UDP-glucuronosyltransferase deficiency. Only a few hundred cases have been described in the literature so far. We are reporting Crigler-Najjar syndrome type 2 in an 18 year old female born out of consanguineous marriage. Keyword: Crigler-Najjar syndrome; UDP-glucuronosyltransferase; Bangladesh DOI: 10.3329/jom.v12i1.6359J Medicine 2011; 12 : 81-85
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Dissertations / Theses on the topic "UDP-glucuronosyltransferase"

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Pritchard, Michael P. "UDP-glucuronosyltransferase : purification and activities in rat and human hepatocytes." Thesis, University of Aberdeen, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.332309.

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The UDP-glucuronosyltransferases (GT) represent a major family of drug-metabolising enzymes, but little is known about their multiplicity in man. The aims of this project were to purify and characterise a GT isozyme from human liver, and to investigate glucuronidation in rat and human hepatocytes, with the aim of using human hepatocytes in primary culture as an <i>in vitro</i> model for the study of human drug metabolism. Chromatofocusing of human liver microsomes produced separation of GT isozymes, providing evidence for heterogeneity. However, purification in an active form was not achieved,
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McCleary, Ryan J. R. "Uridinediphosphate-glucuronosyltransferase (UDP-GT) Ontogeny and PCB Effects in Galliform Birds." Thesis, Virginia Tech, 2001. http://hdl.handle.net/10919/35962.

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Hepatic UDP-GTs are partly responsible for metabolism of the thyroid hormone, thyroxine (T4), in mammals, but little is known of UDP-GT activity in birds. To determine the ontogenic pattern of UDP-GT activity in precocial birds, we measured activity in Japanese quail (Coturnix japonica) liver at days 12 and 14 of the 16.5-day incubation, 3 perihatch stages and <1, 1, 4, 6, 7, 20 and 42 days posthatch. We used an enzymatic reaction with para-nitrophenol (pNP) as substrate that was validated for quail tissue. The pattern of UDP-GT development included low embryonic activity, increased activit
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Bendaly, Jean. "UDP-glucuronosyltransferase (UGT) genetic variants and their potential role in carcinogenesis." [Tampa, Fla.] : University of South Florida, 2004. http://purl.fcla.edu/fcla/etd/SFE0000450.

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Schmohl, Stefan. "Transkriptionelle Aktivierung der humanen UDP-Glucuronosyltransferase Isoform-UGT1A6 durch Induktoren vom Antioxidantien-Typ." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=963784900.

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Gardner-Stephen, Dione Anne, and dione bourne@flinders edu au. "Transcriptional Regulation of Human UDP-Glucuronosyltransferases." Flinders University. Medicine, 2008. http://catalogue.flinders.edu.au./local/adt/public/adt-SFU20081111.223136.

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The UDP-glucuronosyltransferases (UGTs) are a superfamily of enzymes that glucuronidate small, lipophilic molecules, thereby altering their biological activity and excretion. In humans, important examples of UGT substrates include molecules of both endogenous and xenobiotic origin; thus, UGTs are considered essential contributors to homeostatic regulation and an important defence mechanism against chemical insult. In keeping with both roles, UGTs are most strongly expressed in the liver, a predominant organ involved in detoxification. Rates of glucuronidation in humans are neither uniform amon
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Kard, Peter Somphone. "Genetic polymorphism of UDP-glucuronosyltransferase UGT2B7 and in vivo glucuronidation of oxazepam, a genotype-phenotype comparative study." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape9/PQDD_0007/MQ45553.pdf.

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Adiji, Olubu Adeoye. "Identification, Characterization and Engineering of UDP-Glucuronosyltransferases for Synthesis of Flavonoid Glucuronides." Thesis, University of North Texas, 2020. https://digital.library.unt.edu/ark:/67531/metadc1752363/.

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Flavonoids are polyphenolics compounds that constitute a major group of plant specialized metabolites, biosynthesized via the phenylpropanoid/polymalonate pathways. The resulting specialized metabolites can be due to decoration of flavonoid compounds with sugars, usually glucose, by the action of regiospecific UDP-glycosyltransferase (UGT) enzymes. In some cases, glycosylation can involve enzymatic attachment of other sugar moieties, such as glucuronic acid, galactose, rhamnose or arabinose. These modifications facilitate or impact the bioactivity, stability, solubility, bioavailability and ta
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Bruni, Silvia. "The effect of encapsulated hepatocytes on hyperbilirubinemia in Gunn rats characterized by a deficiency of hepatic UDP-glucuronosyltransferase activity." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=28427.

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Free and microencapsulated hepatocytes in an alginate-polylysine-alginate artificial membrane (APA), were implanted intraperitoneally into the Gunn rat, the animal model for Crigler-Najjar syndrome, to reduce serum bilirubin level. Hepatocytes from guinea pigs, Wistar and Sprague-Dawley rats whether free or microencapsulated were equally effective in lowering serum bilirubin levels in the Gunn rat. Buffalo rat hepatocytes however, were immunorejected unless microencapsulated. Decrease in serum bilirubin was concomitant with the appearance of conjugated bilirubin in the bile of Gunn rats as dem
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Van, der Merwe Jennie. "Isolation and evaluation of the sugarcane UDP-glucose dehydrogenase gene and promoter." Thesis, Link to the online version, 2006. http://hdl.handle.net/10019/1254.

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Nishihara, Mitsuhiro. "Investigation of Drug Metabolism by Non-Cytochrome P450 Enzymes and Its Clinical Relevance." Kyoto University, 2014. http://hdl.handle.net/2433/189328.

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Books on the topic "UDP-glucuronosyltransferase"

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Noort, Daniël. Design, synthesis, and evaluation of potential inhibitors of UDP-glucuronosyltransferase. s.n.], 1992.

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Genetic polymorphism of UDP-glucuronosyltransferase UGT2B7 and in vivo glucuronidation of oxazepam: A genotype-phenotype comparative study. National Library of Canada, 1999.

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Book chapters on the topic "UDP-glucuronosyltransferase"

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Sai, Kimie, Hironobu Minami, Yoshiro Saito, and Jun-ichi Sawada. "Impact of UDP-Glucuronosyltransferase 1A Haplotypes on Irinotecan Treatment." In Genomics and Pharmacogenomics in Anticancer Drug Development and Clinical Response. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-088-5_15.

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Emi, Yoshikazu, Shin-Ichi Ikushiro, and Takashi Iyanagi. "Gene Organization and Genetic Defects of Bilirubin UDP-Glucuronosyltransferase." In Oxygen Homeostasis and Its Dynamics. Springer Japan, 1998. http://dx.doi.org/10.1007/978-4-431-68476-3_31.

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Miners, John O., Thomas M. Polasek, Peter I. Mackenzie, and Kathleen M. Knights. "The In Vitro Characterization of Inhibitory Drug–Drug Interactions Involving UDP-Glucuronosyltransferase." In Enzyme- and Transporter-Based Drug-Drug Interactions. Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0840-7_8.

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Ishii, Yuji, Yuu Miyauchi, and Hideyuki Yamada. "Cytochrome P450-Dependent Change in UDP-Glucuronosyltransferase Function and Its Reverse Regulation." In Fifty Years of Cytochrome P450 Research. Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54992-5_18.

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Mehboob, Huma, Imtiaz Mahmood Tahir, Tahir Iqbal, Naheed Akhter, Naveed Munir, and Muhammad Riaz. "Genetic Polymorphism of UDP-Glucuronosyltransferase." In Genetic Polymorphisms. InTech, 2017. http://dx.doi.org/10.5772/intechopen.69206.

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Tephly, T. R., M. D. Green, B. L. Coffman, C. King, Z. Cheng, and G. Rios. "Metabolism of Endobiotics and Xenobiotics by UDP-Glucuronosyltransferase." In Advances in Pharmacology. Elsevier, 1997. http://dx.doi.org/10.1016/s1054-3589(08)60760-7.

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Walter Bock, Karl, and Christoph Köhle. "UDP‐Glucuronosyltransferase 1A6: Structural, Functional, and Regulatory Aspects." In Methods in Enzymology. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)00004-2.

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Dellinger, Ryan W., and Frank L. Meyskens. "Detection of Total UDP-Glucuronosyltransferase (UGT) Activity in Melanoma Cells." In Methods in Molecular Biology. Humana Press, 2015. http://dx.doi.org/10.1007/7651_2015_298.

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Burchell, B., C. H. Brierley, G. Monaghan, and D. J. Clarke. "The Structure and Function of the UDP-Glucuronosyltransferase Gene Family." In Advances in Pharmacology. Elsevier, 1997. http://dx.doi.org/10.1016/s1054-3589(08)60758-9.

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Skierka, Jennifer M., and Dennis J. O’Kane. "UDP-Glucuronosyltransferase 1A1 and the Glucuronidation in Oncology Applications and Hyperbilirubinemia." In Molecular Diagnostics. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-12-369428-7.00033-1.

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Conference papers on the topic "UDP-glucuronosyltransferase"

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Dellinger, Ryan W., Harry H. Matundan, Alisa L. West, and Frank L. Meyskens. "Abstract A9: UDP-glucuronosyltransferase 2B7 (UGT2B7) inhibits melanoma invasiveness." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-a9.

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Dluzen, Douglas F., Anna Salzberg, Dongxiao Sun, Nathan Jones, Ryan Bushey', and Philip Lazarus. "Abstract 3089: miR-491-3p regulation of the UDP-glucuronosyltransferase (UGT) 1A gene family." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3089.

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Bushey, Ryan, Gang Chen, Andrea S. Blevins-Primeau, and Philip Lazarus. "Abstract 1698: Characterization of the activity and expression of UDP-Glucuronosyltransferase 2A1 variants and potential role in tobacco carcinogenesis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1698.

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Starlard-Davenport, Athena, Beverly R. Word, and Beverly D. Lyn-Cook. "Abstract 4120: UDP-Glucuronosyltransferase 1 (UGT1A1) down-regulation correlates to menopausal status and stage of disease in human breast cancer tissues." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4120.

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Tucker, Cocoa, Adriana C. Vidal, Joellen M. Schildkraut, et al. "Abstract B51: Genetic polymorphisms of the UDP-glucuronosyltransferase 2B15 and 2B17 genes are associated with prostate cancer in African American men." In Abstracts: Fifth AACR Conference on the Science of Cancer Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; Oct 27–30, 2012; San Diego, CA. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1055-9965.disp12-b51.

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Sun, C., D. Huo, B. Nemesure, et al. "Abstract P3-12-07: Polymorphisms in the UDP-Glucuronosyltransferase 2B Gene Family and Risk of Breast Cancer in Women of African Descent." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-p3-12-07.

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