Relevant bibliographies by topics / UDP-glucuronosyltransferase

Academic literature on the topic 'UDP-glucuronosyltransferase'

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Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "UDP-glucuronosyltransferase"

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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 (February 15, 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 androsterone and testosterone was eluted at about pH 8.0, had subunit Mr values of 50 000 and 52 000, and appeared to be an aggregate or hybrid of androsterone and testosterone UDP-glucuronosyltransferases. In rats with the low-activity phenotype, androsterone UDP-glucuronosyltransferase was absent, whereas testosterone UDP-glucuronosyltransferase was eluted at around pH 8.5, with a subunit Mr of 50 000.
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Golovinsky, E., Z. Naydenova, and K. Grancharov. "UDP-Glucuronosyltransferase inhibitors." European Journal of Drug Metabolism and Pharmacokinetics 23, no. 4 (December 1998): 453–56. http://dx.doi.org/10.1007/bf03189994.

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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 (March 1, 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-pairs long, including a poly(A) tail, and contains a long open reading frame. The possible site of translation initiation of this sequence is discussed with reference to a rat UDP-glucuronosyltransferase cDNA clone (RLUG 38).
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Falany, C. N., M. D. Green, E. Swain, and T. R. Tephly. "Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases." Biochemical Journal 238, no. 1 (August 15, 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 endogenous substrate has not yet been identified for the p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferase. The steroid UDP-glucuronosyltransferase activities were dependent on phospholipid for maximal catalytic activity. Complete delipidation rendered the UDP-glucuronosyltransferases inactive, and enzymic activity was not restored when phospholipid was added to the reaction mixture. After partial delipidation, phosphatidylcholine was the most efficient phospholipid for restoration of enzymic activity. Partial delipidation also altered the kinetic parameters of the 3 alpha-hydroxysteroid UDP-glucuronosyltransferase. The three purified UDP-glucuronosyltransferases are separate and distinct proteins, with different amino acid compositions and peptide maps generated by limited proteolysis with Staphylococcus aureus V8 proteinase. Some similarity was observed between the amino acid composition and limited proteolytic maps of the steroid UDP-glucuronosyltransferases, suggesting they are more closely related to each other than to the p-nitrophenol UDP-glucuronosyltransferase.
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Radominska-Pandya, A., J. Little, and P. Czernik. "Human UDP-Glucuronosyltransferase 2B7." Current Drug Metabolism 2, no. 3 (September 1, 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 (October 2007): 356–65. http://dx.doi.org/10.1016/j.aquatox.2007.06.015.

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BÁNHEGYI, Gábor, László BRAUN, Paola MARCOLONGO, Miklós CSALA, Rosella FULCERI, József MANDL, and BENEDETTI BENEDETTI. "Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles." Biochemical Journal 315, no. 1 (April 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) glucuronides stimulated the release of UDP-glucuronic acid from UDP-glucuronic acid-loaded microsomal vesicles; (iv) trans-stimulation of UDP-glucuronic acid entry by loading of microsomal vesicles with p-nitrophenol glucuronide, phenolphthalein glucuronide, UDP-glucuronic acid and UDP-N-acetylglucosamine almost completely abolished the latency of UDP-glucuronosyltransferase, although mannose 6-phosphatase latency remained unaltered; (v) the loading compounds by themselves did not stimulate UDP-glucuronosyltransferase activity. This study indicates that glucuronides synthesized in the lumen of endoplasmic reticulum can leave by an antiport, which concurrently transports UDP-glucuronic acid into the lumen of the endoplasmic reticulum.
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Little, J. M., R. Lester, F. Kuipers, R. Vonk, P. I. Mackenzie, R. R. Drake, L. Frame, and A. Radominska-Pandya. "Variability of human hepatic UDP-glucuronosyltransferase activity." Acta Biochimica Polonica 46, no. 2 (June 30, 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 UDP-glucuronosyltransferases. However, the largest differences were between subjects with liver disease. Glucuronidation activities toward one substrate from each of the UDP-glucuronosyltransferases subfamilies, 1A and 2B, for control and liver disease, respectively, were 1.7-4.5 vs 0.4-4.7 nmol/mg x min for hyodeoxycholic acid (2B substrate) and 9.2-27.9 vs 8.1-75 nmol/mg x min for pchloro-m-xylenol (1A substrate). Microsomes from a patient with chronic tyrosinemia (HL32) photoincorporated [32P]5-azido-UDP-glucuronic acid at a level 1.5 times higher than the other samples, was intensely photolabeled by [32P]5-azido-UDP-glucose and had significantly higher enzymatic activity toward p-chloro-m-xylenol. Immunoblot analysis using anti-UDP-glucuronosyltransferase antibodies demonstrated wide inter-individual variations in UDP-glucuronosyltransferase protein with increased UDP-glucuronosyltransferase protein in HL32 microsomes, corresponding to one of the bands photolabeled by both probes. Detailed investigation of substrate specificity, using substrates representative of both the 1A (bilirubin, 4-nitrophenol) and 2B (androsterone, testosterone) families was carried out with HL32, HL38 (age and sex matched control) and HL18 (older control). Strikingly increased (5-8-fold) glucuronidation activity was seen in comparison to HL18 only with the phenolic substrates. The results indicate that one or more phenol-specific UDP-glucuronosyltransferase 1A isoforms are expressed at above normal levels in this tyrosinemic subject.
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Mackenzie, P., P. Gregory, D. Gardner-Stephen, R. Lewinsky, B. Jorgensen, T. Nishiyama, Wen Xie, and A. Radominska-Pandya. "Regulation of UDP Glucuronosyltransferase Genes." Current Drug Metabolism 4, no. 3 (June 1, 2003): 249–57. http://dx.doi.org/10.2174/1389200033489442.

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Debinski, H. S., C. S. Lee, A. P. Dhillon, P. Mackenzie, J. Rhode, and P. V. Desmond. "UDP-Glucuronosyltransferase in gilbert’s syndrome." Pathology 28, no. 3 (1996): 238–41. http://dx.doi.org/10.1080/00313029600169064.

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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 in vitro 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, due to lability in the presence of detergent. Rat liver 17β-hydroxysteroid-GT was purified, and antibodies raised against this protein recognised a single protein in human liver microsomes. Rates of glucuronidation of 1-naphthol and phenolphthalein were significantly higher in rat hepatocyte homogenates than in hepatocytes, the magnitude of the difference being greater for 1-naphthol. This was attributed to the presence of excess UDPGA in homogenate assays and the limitation imposed by lipophilicity on substrate uptake into cells by passive diffusion. In contrast, the rate of bilirubin glucuronidation was greater in hepatocytes, possibly as a result of intact carrier-mediated uptake mechanisms, combined with a suitable environment for efficient delivery of bilirubin to the endoplasmic reticulum by membrane-membrane transfer. The same three substrates were glucuronidated at a reduced rate in human compared with rat hepatocytes, apparently due to a lower intracellular UDPGA level and isozyme-specific differences in intrinsic activity and latency. As a result, the rate of glucuronidation of all these substrates was greater in human hepatocyte homogenates than in hepatocytes. Isozyme-specific changes were observed in GT activities in human hepatocytes in primary culture, indicating the need to develop culture systems allowing stable expression of these enzymes before such a model could be used for predictive human drug metabolism.
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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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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 activity beginning in the perihatch period, a peak in activity at day 4 posthatch and a return to lower activity levels from day 6 to adults. The profile of UDP-GT activity, in relation to the ontogeny of circulating T4 and triiodothyronine (T3) in quail, is consistent with UDP-GT playing a role in regulating circulating T4 and with the perihatch peak in T3 stimulating the posthatch peak in UDP-GT activity. To examine the effects of polychlorinated biphenyls (PCBs) on UDP-GT in developing precocial birds, we dosed chicken (Gallus domesticus) eggs with concentrations of PCB 126 from 0 to 0.80 ng/g egg (in sunflower oil) prior to incubation. Tissues were sampled at day 20 of the 21-day incubation and assayed for plasma hormones and UDP-GT activity. Eggs also were dosed with 0 or 0.25 ng PCB 126/g egg or with 0 or 0.64 ng/g egg of the coplanar PCB 77, allowed to hatch, and sampled at 42 days posthatch. There was no consistent pattern of altered thyroid hormones or UDP-GT activity in developing chickens exposed to either of these coplanar PCBs although previous studies indicated developmental alterations from exposure to the higher doses.
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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 among individuals, nor constant in an individual over time. Genetic determinants and non-endogenous signals are both known to influence the expression of UGTs, which in turn may affect the efficacy of certain pharmaceutical treatments or alter long-term risk of developing disease. Thus, this thesis focuses on the transcriptional regulation of UGT genes in humans, particularly on mechanisms that are likely to be relevant to their expression and variation in the liver. Two major approaches were used: firstly, extensive studies of several UGT promoters were performed to identify and characterise transcriptional elements that are important for UGT expression; and secondly, important hepatic transcription factors were investigated as potential regulators of UGT genes. UGT1A3, UGT1A4 and UGT1A5 are a subset of highly related, but independently regulated, genes of the human UGT1 subfamily. UGT1A3 and UGT1A4 are expressed in the liver, whereas UGT1A5 is not. The presented analysis of the UGT1A3, UGT1A4 and UGT1A5 proximal promoters demonstrates that a hepatocyte nuclear factor (HNF)1-binding site common to all three promoters is important for UGT1A3 and UGT1A4 promoter activity in vitro, but is insufficient to drive UGT1A5 expression. Two additional elements required for the maximal activity of the UGT1A3 promoter were also identified that may distinguish this gene from UGT1A4. UGT1A3 was investigated further, focusing on mechanisms that may contribute to interindividual variation in UGT1A3 expression. Polymorphisms in the UGT1A3 proximal promoter were identified and their functional consequences tested. Known variants of HNF1alpha were also tested for altered activity towards the UGT1A3 gene. UGT1A9 is the only hepatic member of the UGT1A7-1A10 subgroup of UGT1 enzymes. Previous work had identified HNF1-binding sites in all four genes, and HNF4alpha as an UGT1A9-specific regulator. The work presented herein extends these findings to show that HNF1 factors and HNF4alpha synergistically regulate UGT1A9, and that HNF4alpha is not the only transcription factor responsible for the unique presence of UGT1A9 in the liver. Liver-enriched transcription factors screened as potential UGT regulators were chosen from the HNF1, HNF4, HNF6, FoxA and C/EBP protein families. Functional interactions newly identified by this work were HNF4alpha with UGT1A1 and UGT1A6, HNF6 with UGT1A4 and UGT2B11, FoxA1 and FoxA3 with UGT2B11, UGT2B15 and UGT2B28 and C/EBPalpha with UGT2B17. Observations were also made regarding different patterns of interaction between each UGT and the transcription factors tested, particularly HNF1alpha.
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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 taste of the resulting flavonoid metabolites. The present work shows the limitations of utilizing mammalian UDP-glucuronosyltransferases (UGATs) for flavonoid glucuronidation, and then proceeds to investigate plant UG(A)T candidates from the model legume Medicago truncatula for glucuronidating brain-targeted flavonoid metabolites that have shown potential in neurological protection. We identified and characterized several UG(A)T candidates from M. truncatula which efficiently glycosylate various flavonoids compounds with different/multiple regiospecificities. Biochemical characterization identified one enzyme, UGT84F9, that efficiently glucuronidates a range of flavonoid compounds in vitro. In addition, examination of the ugt84f9 gene knock-out mutation in M. truncatula indicates that UGT84F9 is the major UG(A)T enzyme that is necessary and sufficient for attaching glucuronic acid to flavonoid aglycones, particularly flavones, in this species. Finally, the identified UG(A)T candidates were analyzed via homology modeling and site-directed mutagenesis towards increasing the repertoire of UG(A)Ts applicable for synthesis of flavonoid glucuronides with potential human health benefits in neurological protection.
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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 demonstrated by HPLC analysis. Microcapsules containing guinea pig hepatocytes showed less fibrosis than microcapsules containing hepatocytes from different strains of rats and empty microcapsules. In the Gunn rat there is significant accumulation of bilirubin in various tissues which affects the net removal of bilirubin upon implantation of the encapsulated hepatocytes. This deposition increases with time and it is organ-dependent. The kinetic data of UDP-glucuronosyltransferase (UDPGT) indicated that it is a multisubunit enzyme in which there is cooperative binding of the substrate to the subunits. The binding of bilirubin showed positive cooperativity while the binding of UDPGA exhibited kinetics with mixed cooperativity. Encapsulated hepatocytes when incubated with bilirubin and UDP-glucuronic acid can form bilirubin conjugates. This was shown by HPLC analysis.The comparison of UDPGT activity between liver homogenate, intact hepatocytes and encapsulated hepatocytes showed that there is mass transfer resistance of the APA membrane.
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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. [The Netherlands: s.n.], 1992.

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

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Book chapters on the topic "UDP-glucuronosyltransferase"

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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, 248–51. Tokyo: Springer Japan, 1998. http://dx.doi.org/10.1007/978-4-431-68476-3_31.

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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, 267–86. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-088-5_15.

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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, 217–36. New York, NY: 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, 307–26. Tokyo: 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, 343–46. 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, 57–75. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)00004-2.

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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, 335–38. Elsevier, 1997. http://dx.doi.org/10.1016/s1054-3589(08)60758-9.

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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. Totowa, NJ: Humana Press, 2015. http://dx.doi.org/10.1007/7651_2015_298.

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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, 409–19. 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, Ricardo M. Richardson, Stephen J. Freedland, Cathrine Hoyo, and Delores J. Grant. "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, A. Hennis, D. Witonsky, Q. Niu, A. Di Rienzo, and OI Olopade. "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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