메뉴 건너뛰기




Volumn 31, Issue 4, 1999, Pages 817-899

Structural and functional studies of UDP-glucuronosyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; GLUCURONOSYLTRANSFERASE; HISTIDINE; LYSINE; PROLINE;

EID: 0032707765     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-100101944     Document Type: Article
Times cited : (444)

References (213)
  • 1
    • 0023701349 scopus 로고
    • Morphine-6-glucuronide. Analgesic effects and receptor binding profile in rats
    • F. V. Abbot and R. M. Palmour, Morphine-6-glucuronide. Analgesic effects and receptor binding profile in rats, Life Sci., 43, 1685 (1988).
    • (1988) Life Sci. , vol.43 , pp. 1685
    • Abbot, F.V.1    Palmour, R.M.2
  • 2
    • 0021091051 scopus 로고
    • Steroid D-ring glucuronides: Characterization of a new class of cholestatic agents
    • M. Vore, C. Montgomery, and M. Meyers, Steroid D-ring glucuronides: Characterization of a new class of cholestatic agents, Drug Metab. Rev., 14, 1005 (1983).
    • (1983) Drug Metab. Rev. , vol.14 , pp. 1005
    • Vore, M.1    Montgomery, C.2    Meyers, M.3
  • 3
    • 0001570065 scopus 로고
    • Steroid D-ring glucuronides: A new class of cholestatic agents
    • M. Vore and W. Slikker, Steroid D-ring glucuronides: A new class of cholestatic agents Trends Pharmacol. Sci., 6, 256 (1985).
    • (1985) Trends Pharmacol. Sci. , vol.6 , pp. 256
    • Vore, M.1    Slikker, W.2
  • 5
    • 0026605427 scopus 로고
    • Enhancement of biological activity by conjugation reactions
    • J. A. Olson, R. C. Moon, M. W. Anders, C. Fenselau, and B. Shane, Enhancement of biological activity by conjugation reactions, J. Nutr., 122, 615 (1992).
    • (1992) J. Nutr. , vol.122 , pp. 615
    • Olson, J.A.1    Moon, R.C.2    Anders, M.W.3    Fenselau, C.4    Shane, B.5
  • 6
    • 0030296437 scopus 로고    scopus 로고
    • Tissue-specific 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible expression of human UDP-glucuronosyltransferase UGT1A6
    • P. A. Munzel, G. Bookjans, G. Mehner, T. Lehmkoster, and K. W. Bock, Tissue-specific 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible expression of human UDP-glucuronosyltransferase UGT1A6, Arch. Biochem. Biophys., 335, 205 (1996).
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 205
    • Munzel, P.A.1    Bookjans, G.2    Mehner, G.3    Lehmkoster, T.4    Bock, K.W.5
  • 10
    • 0033538021 scopus 로고    scopus 로고
    • Preferential expression of biotransformation enzymes in the olfactory organs of Drosophila melanogaster, the antennae
    • Q. Wang, G. Hasan, and C. W. Pikielny, Preferential expression of biotransformation enzymes in the olfactory organs of Drosophila melanogaster, the antennae, J. Biol. Chem., 274, 10,309 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10309
    • Wang, Q.1    Hasan, G.2    Pikielny, C.W.3
  • 12
    • 0030028130 scopus 로고    scopus 로고
    • Identification of bilirubin UDP-GTs in the human alimentary tract in accordance with the gut as a putative metabolic organ
    • W. M. McDonnell, E. Hitomi, and F. K. Askari, Identification of bilirubin UDP-GTs in the human alimentary tract in accordance with the gut as a putative metabolic organ, Biochem. Pharmacol., 51, 483 (1996).
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 483
    • McDonnell, W.M.1    Hitomi, E.2    Askari, F.K.3
  • 13
    • 85034892163 scopus 로고
    • Glutathione S-transferase, cytochrome P450, and uridine 5′-diphosphate-glucuronosyltransferase in human small intestine and liver
    • W. H. M. Peters, F. M. Nagengast, and J. H. M. van Tongeren, Glutathione S-transferase, cytochrome P450, and uridine 5′-diphosphate-glucuronosyltransferase in human small intestine and liver, Gastroenterology, 96, 783 (1989).
    • (1989) Gastroenterology , vol.96 , pp. 783
    • Peters, W.H.M.1    Nagengast, F.M.2    Van Tongeren, J.H.M.3
  • 14
    • 0023858335 scopus 로고
    • Immunocharacterization of UDP-glucuronyltransferase isoenzymes in human liver, intestine and kidney
    • W. H. Peters and P. L. Jansen, Immunocharacterization of UDP-glucuronyltransferase isoenzymes in human liver, intestine and kidney, Biochem. Pharmacol., 37, 564 (1988).
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 564
    • Peters, W.H.1    Jansen, P.L.2
  • 15
    • 0021961432 scopus 로고
    • Infante, glucuronidation of bile acids in human liver, intestine and kidney. An in vitro study on hyodeoxycholic acid
    • M. Parquet, M. Pessah, E. Sacquet, C. Salvat, A. Raizman, and R. Infante, Glucuronidation of bile acids in human liver, intestine and kidney. An in vitro study on hyodeoxycholic acid, FEBS Lett., 189, 183 (1985).
    • (1985) FEBS Lett. , vol.189 , pp. 183
    • Parquet, M.1    Pessah, M.2    Sacquet, E.3    Salvat, C.4    Raizman, A.5
  • 16
    • 0021134465 scopus 로고
    • Hepatic and extrahepatic glucuronidation of bile acids in man. Characterization of bile acid uridine 5′-diphosphate-glucuronosyltransferase in hepatic, renal, and intestinal microsomes
    • S. Matern, H. Matern, E. H. Farthmann, and W. Gerok, Hepatic and extrahepatic glucuronidation of bile acids in man. Characterization of bile acid uridine 5′-diphosphate-glucuronosyltransferase in hepatic, renal, and intestinal microsomes, J. Clin. Invest., 74, 402 (1984).
    • (1984) J. Clin. Invest. , vol.74 , pp. 402
    • Matern, S.1    Matern, H.2    Farthmann, E.H.3    Gerok, W.4
  • 17
    • 0032055273 scopus 로고    scopus 로고
    • Drug glucuronidation by human renal UDP-glucuronosyltransferases
    • K. A. McGurk, C. H. Brierly, and B. Burchell, Drug glucuronidation by human renal UDP-glucuronosyltransferases, Biochem. Pharmacol., 55, 1005 (1998).
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1005
    • McGurk, K.A.1    Brierly, C.H.2    Burchell, B.3
  • 18
    • 0022620186 scopus 로고
    • Sex differences in drug conjugation and their consequences for drug toxicity. Sulfation, glucuronidation and glutathione conjugation
    • G. J. Mulder, Sex differences in drug conjugation and their consequences for drug toxicity. Sulfation, glucuronidation and glutathione conjugation, Chem. Biol. Interact., 57, 1 (1986).
    • (1986) Chem. Biol. Interact. , vol.57 , pp. 1
    • Mulder, G.J.1
  • 19
    • 0029859993 scopus 로고    scopus 로고
    • Hormonal regulation of hepatic enzymes involved in foreign compound metabolism
    • R. A. Prough, M. W. Linder, J. A. Pinaire, G.-H. Xiao, and K. C. Falkner, Hormonal regulation of hepatic enzymes involved in foreign compound metabolism, FASEB J., 10, 1369 (1996).
    • (1996) FASEB J. , vol.10 , pp. 1369
    • Prough, R.A.1    Linder, M.W.2    Pinaire, J.A.3    Xiao, G.-H.4    Falkner, K.C.5
  • 20
    • 0030867709 scopus 로고    scopus 로고
    • Genetic and environmental factors associated with variation of human xenobiotic glucuronidation and sulfation
    • B. Burchell and M. W. H. Coughtrie, Genetic and environmental factors associated with variation of human xenobiotic glucuronidation and sulfation, Environ. Health Persp., 105, 739 (1997).
    • (1997) Environ. Health Persp. , vol.105 , pp. 739
    • Burchell, B.1    Coughtrie, M.W.H.2
  • 22
    • 0026376260 scopus 로고
    • Proposed role of drug-metabolizing enzymes: Regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions
    • D. W. Nebert, Proposed role of drug-metabolizing enzymes: Regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions, Mol. Endocrinol., 5, 1203 (1991).
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1203
    • Nebert, D.W.1
  • 23
    • 0028040226 scopus 로고
    • Drug-metabolizing enzymes in ligand-modulated transcription
    • D. W. Nebert, Drug-metabolizing enzymes in ligand-modulated transcription, Biochem. Pharmacol., 47, 25 (1994).
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 25
    • Nebert, D.W.1
  • 24
    • 0030868851 scopus 로고    scopus 로고
    • Cytochromes P450 and uridine triphosphate (sic)-glucuronosyltransferases: Model autoantigens to study drug-induced, virus-induced, and autoimmune liver disease
    • M. P. Manns and P. Obermayer-Straub, Cytochromes P450 and uridine triphosphate (sic)-glucuronosyltransferases: Model autoantigens to study drug-induced, virus-induced, and autoimmune liver disease, Hepatology, 26, 1054 (1997).
    • (1997) Hepatology , vol.26 , pp. 1054
    • Manns, M.P.1    Obermayer-Straub, P.2
  • 25
    • 0032483045 scopus 로고    scopus 로고
    • Required buried alphahelical structure in the bilirubin UDP-glucuronosyltransferase, UGT1A1, contains a nonreplaceable phenylalanine
    • M. Ciotti, J. W. Cho, J. George, and I. S. Owens, Required buried alphahelical structure in the bilirubin UDP-glucuronosyltransferase, UGT1A1, contains a nonreplaceable phenylalanine, Biochemistry, 37, 11018 (1998).
    • (1998) Biochemistry , vol.37 , pp. 11018
    • Ciotti, M.1    Cho, J.W.2    George, J.3    Owens, I.S.4
  • 27
    • 0030889553 scopus 로고    scopus 로고
    • Arginine 52 and Histidine 54 located in a conserved N-terminal hydrophobic region (LX2-R52-G-H54-X3-V-L) are important amino acids for the functional and structural integrity of the human liver UDP-glucuronosyltransferase UGT1*6
    • C. Senay, M. Ouzzine, E. Battaglia, D. Pless, V. Cano, B. Burchell, A. Radominska, J. Magdalou, and S. Fournel-Gigleux, Arginine 52 and Histidine 54 located in a conserved N-terminal hydrophobic region (LX2-R52-G-H54-X3-V-L) are important amino acids for the functional and structural integrity of the human liver UDP-glucuronosyltransferase UGT1*6, Mol. Pharmacol., 51, 406 (1997).
    • (1997) Mol. Pharmacol. , vol.51 , pp. 406
    • Senay, C.1    Ouzzine, M.2    Battaglia, E.3    Pless, D.4    Cano, V.5    Burchell, B.6    Radominska, A.7    Magdalou, J.8    Fournel-Gigleux, S.9
  • 28
    • 0030879658 scopus 로고    scopus 로고
    • A critical amino acid residue, asp446, in UDP-glucuronosyltransferase
    • H. Iwano, H. Yokota, S. Ohgiya, N. Yotumoto, and A. Yuasa, A critical amino acid residue, asp446, in UDP-glucuronosyltransferase, Biochem. J., 325, 587 (1997).
    • (1997) Biochem. J. , vol.325 , pp. 587
    • Iwano, H.1    Yokota, H.2    Ohgiya, S.3    Yotumoto, N.4    Yuasa, A.5
  • 29
    • 0033102535 scopus 로고    scopus 로고
    • The significance of amino acid residue Asp446 for enzymatic stability of rat UDP-glucuronosyltransferase UGT1A6
    • H. Iwano, H. Yokota, S. Ohgiya, and A. Yuasa, The significance of amino acid residue Asp446 for enzymatic stability of rat UDP-glucuronosyltransferase UGT1A6, Arch. Biochem. Biophys., 363, 116 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 116
    • Iwano, H.1    Yokota, H.2    Ohgiya, S.3    Yuasa, A.4
  • 30
    • 0030778114 scopus 로고    scopus 로고
    • Structure and function of uridine diphosphate glucuronosyltransferases
    • R. Meech and P. I. Mackenzie, Structure and function of uridine diphosphate glucuronosyltransferases, Clin. Exp. Pharmacol. Physiol., 24, 907 (1997).
    • (1997) Clin. Exp. Pharmacol. Physiol. , vol.24 , pp. 907
    • Meech, R.1    Mackenzie, P.I.2
  • 31
    • 0008690963 scopus 로고    scopus 로고
    • Bilirubin metabolism and the pathophysiology of jaundice
    • (E. R. Schiff, M. F. Sorell, and W. C. Maddrey, eds.), Lippincott-Raven, Philadelphia
    • C. L. Berg, J. M. Crawford, and J. L. Gollan, Bilirubin metabolism and the pathophysiology of jaundice, in Diseases of the Liver (E. R. Schiff, M. F. Sorell, and W. C. Maddrey, eds.), Lippincott-Raven, Philadelphia, 1999.
    • (1999) Diseases of the Liver
    • Berg, C.L.1    Crawford, J.M.2    Gollan, J.L.3
  • 32
    • 0032413678 scopus 로고    scopus 로고
    • Biochemical and molecular aspects of genetic disorders of bilirubin metabolism
    • T. Iyanagi, Y. Emi, and S. Ikushiro, Biochemical and molecular aspects of genetic disorders of bilirubin metabolism, Biochim. Biophys. Acta, 1407, 173 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1407 , pp. 173
    • Iyanagi, T.1    Emi, Y.2    Ikushiro, S.3
  • 33
    • 0031706608 scopus 로고    scopus 로고
    • Glucuronidation of amine substrates by purified and expressed UDP-glucuronosyltransferase proteins
    • M. D. Green and T. R. Tephly, Glucuronidation of amine substrates by purified and expressed UDP-glucuronosyltransferase proteins, Drug Metab. Disp., 26, 860 (1998).
    • (1998) Drug Metab. Disp. , vol.26 , pp. 860
    • Green, M.D.1    Tephly, T.R.2
  • 34
    • 0028875109 scopus 로고
    • Specificity of human UDP-glucuronosyltransferases and xenobiotic glucuronidation
    • B. Burchell, C. H. Brierly, and D. Rance, Specificity of human UDP-glucuronosyltransferases and xenobiotic glucuronidation, Life Sci., 57, 1819 (1995).
    • (1995) Life Sci. , vol.57 , pp. 1819
    • Burchell, B.1    Brierly, C.H.2    Rance, D.3
  • 35
    • 0344936870 scopus 로고
    • Molecular biology of the uridine diphosphate glucuronosyltransferases
    • (N. Tavaloni and P. D. Berk, eds.), Raven Press, New York
    • B. Burchell, Molecular biology of the uridine diphosphate glucuronosyltransferases, in Hepatic Transport and Bile Secretion: Physiology and Pathophysiology (N. Tavaloni and P. D. Berk, eds.), Raven Press, New York, 1993, p. 489.
    • (1993) Hepatic Transport and Bile Secretion: Physiology and Pathophysiology , pp. 489
    • Burchell, B.1
  • 36
    • 0028044817 scopus 로고
    • A recombinant phenobarbital-inducible rat liver UDP-glucuronosyltransferase (UDP-glucuronosyltransferase 2B1) stably expressed in V79 cells catalyzes the glucuronidation of morphine, penols, and carboxylic acids
    • M. Pritchard, S. Fournel-Gigleux, G. Siest, P. Mackenzie, and J. Magdalou, A recombinant phenobarbital-inducible rat liver UDP-glucuronosyltransferase (UDP-glucuronosyltransferase 2B1) stably expressed in V79 cells catalyzes the glucuronidation of morphine, penols, and carboxylic acids, Mol. Pharmacol., 45, 42 (1994).
    • (1994) Mol. Pharmacol. , vol.45 , pp. 42
    • Pritchard, M.1    Fournel-Gigleux, S.2    Siest, G.3    Mackenzie, P.4    Magdalou, J.5
  • 38
    • 0026010397 scopus 로고
    • Quantitative structure-activity relationships of the metabolism of drugs by uridine diphosphate glucuronosyltransferase
    • K. H. Kim, Quantitative structure-activity relationships of the metabolism of drugs by uridine diphosphate glucuronosyltransferase, J. Pharm. Sci., 80, 966 (1991).
    • (1991) J. Pharm. Sci. , vol.80 , pp. 966
    • Kim, K.H.1
  • 39
    • 0028331320 scopus 로고
    • Mechanistic studies of uridine diphosphate glucuronosyltransferase
    • H. Yin, G. Bennett, and J. P. Jones, Mechanistic studies of uridine diphosphate glucuronosyltransferase, Chem.-Biol, Interact., 90, 47 (1994).
    • (1994) Chem.-biol, Interact. , vol.90 , pp. 47
    • Yin, H.1    Bennett, G.2    Jones, J.P.3
  • 40
    • 0025871397 scopus 로고
    • Glucuronidation of 3′-azido-3′-deoxythymidine catalyzed by human liver UDP-glucuronosyltransferase. Significance of nucleoside hydrophobicity and inhibition by xenobiotics
    • A. Resetar, D. Minick, and T. Spector, Glucuronidation of 3′-azido-3′-deoxythymidine catalyzed by human liver UDP-glucuronosyltransferase. Significance of nucleoside hydrophobicity and inhibition by xenobiotics, Biochem. Pharmacol., 42, 559 (1991).
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 559
    • Resetar, A.1    Minick, D.2    Spector, T.3
  • 41
    • 0024241217 scopus 로고
    • Examination of the substrate specificity of cloned rat kidney phenol UDP-glucuronyltransferase expressed in COS-7 cells
    • M.R. Jackson, S. Fournel-Gigleux, D. Harding, and B. Burchell, Examination of the substrate specificity of cloned rat kidney phenol UDP-glucuronyltransferase expressed in COS-7 cells, Mol. Pharmacol., 34, 638 (1988).
    • (1988) Mol. Pharmacol. , vol.34 , pp. 638
    • Jackson, M.R.1    Fournel-Gigleux, S.2    Harding, D.3    Burchell, B.4
  • 42
    • 0025265006 scopus 로고
    • Inhibition of UDP glucuronosyltransferase activity by possible transition state analogues in rat liver microsomes
    • D. Noort, M. W. H. Coughtrie, B. Burchell, G. A. van der Marel, J. H. Van Boom, and G. J. Mulder, Inhibition of UDP glucuronosyltransferase activity by possible transition state analogues in rat liver microsomes, Eur. J. Biochem, 188, 309 (1990).
    • (1990) Eur. J. Biochem , vol.188 , pp. 309
    • Noort, D.1    Coughtrie, M.W.H.2    Burchell, B.3    Van Der Marel, G.A.4    Van Boom, J.H.5    Mulder, G.J.6
  • 44
    • 0028303560 scopus 로고
    • Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: Possible involvement of a histidine residue in the catalytic process
    • E. Battaglia, M. Pritchard, M. Ouzzine, S. Fournel-Gigleux, A. Radominska, G. Siest, and J. Magdalou, Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: possible involvement of a histidine residue in the catalytic process, Arch. Biochem. Biophys., 309, 266 (1994).
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 266
    • Battaglia, E.1    Pritchard, M.2    Ouzzine, M.3    Fournel-Gigleux, S.4    Radominska, A.5    Siest, G.6    Magdalou, J.7
  • 45
    • 0028360401 scopus 로고
    • The chemical modification of human liver UDP-glucuronosyltransferase UGT1*6 reveals the involvement of a carboxyl group in catalysis
    • E. Battaglia, C. Senay, S. Fournel-Gigleux, R. Herber, G. Siest, and J. Magdalou, The chemical modification of human liver UDP-glucuronosyltransferase UGT1*6 reveals the involvement of a carboxyl group in catalysis, FEBS Lett., 309, 266 (1994).
    • (1994) FEBS Lett. , vol.309 , pp. 266
    • Battaglia, E.1    Senay, C.2    Fournel-Gigleux, S.3    Herber, R.4    Siest, G.5    Magdalou, J.6
  • 46
    • 0030800075 scopus 로고    scopus 로고
    • Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: Identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue
    • C. P. Strassburg, K. Oldhaffer, M. P. Manns, and R. H. Tukey, Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: Identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue, Mol. Pharmacol., 52, 212 (1997).
    • (1997) Mol. Pharmacol. , vol.52 , pp. 212
    • Strassburg, C.P.1    Oldhaffer, K.2    Manns, M.P.3    Tukey, R.H.4
  • 47
    • 0032502764 scopus 로고    scopus 로고
    • Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic 1A8
    • C. P. Strassburg, M. P. Manns, and R. H. Tukey, Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic 1A8, J. Biol. Chem., 273, 8719 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8719
    • Strassburg, C.P.1    Manns, M.P.2    Tukey, R.H.3
  • 48
    • 0013588037 scopus 로고    scopus 로고
    • CDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3
    • B. Mojarrabi, R. Butler, and P. I. Mackenzie, cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3, Biochem. Biophys. Res. Commun., 225, 785 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 785
    • Mojarrabi, B.1    Butler, R.2    Mackenzie, P.I.3
  • 49
    • 0032529231 scopus 로고    scopus 로고
    • Cloning and expression of human UDP-glucuronosyltransferase (UGT) 1A8
    • Z. Cheng, A. Radominska-Pandya, and T. R. Tephly, Cloning and expression of human UDP-glucuronosyltransferase (UGT) 1A8, Arch. Biochem. Biophys., 356, 301 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 301
    • Cheng, Z.1    Radominska-Pandya, A.2    Tephly, T.R.3
  • 51
    • 0027235464 scopus 로고
    • Glucuronidation of thyroid hormone by human bilirubin and phenol UDP-glucuronyltransferase isoenzymes
    • T. J. Visser, E. Kaptein, A. L. Gijzel, W. W. de Herder, T. Ebner, and B. Burchell, Glucuronidation of thyroid hormone by human bilirubin and phenol UDP-glucuronyltransferase isoenzymes, FEBS Lett., 324, 358 (1993).
    • (1993) FEBS Lett. , vol.324 , pp. 358
    • Visser, T.J.1    Kaptein, E.2    Gijzel, A.L.3    De Herder, W.W.4    Ebner, T.5    Burchell, B.6
  • 54
    • 0027433317 scopus 로고
    • Complementary deoxyribonucleic acid cloning and expression of human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs
    • C. Jin, J. O. Miners, K. J. Lillywhite, and P. I. Mackenzie, Complementary deoxyribonucleic acid cloning and expression of human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs, J. Pharm. Exp. Ther., 264, 475 (1993).
    • (1993) J. Pharm. Exp. Ther. , vol.264 , pp. 475
    • C, J.1    Miners, J.O.2    Lillywhite, K.J.3    Mackenzie, P.I.4
  • 55
    • 0031894377 scopus 로고    scopus 로고
    • The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268)
    • B. L. Coffman, C. D. King, G. R. Rios, and T. R. Tephly, The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268), Drug Metab. Disp., 26, 73 (1998).
    • (1998) Drug Metab. Disp. , vol.26 , pp. 73
    • Coffman, B.L.1    King, C.D.2    Rios, G.R.3    Tephly, T.R.4
  • 57
    • 0027267719 scopus 로고
    • CDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily
    • C. Jin, J. O. Miners, K. J. Lillywhite, and P. I. Mackenzie, cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily, Biochem. Biophys. Res. Commun., 194, 496 (1993).
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 496
    • Jin, C.1    Miners, J.O.2    Lillywhite, K.J.3    Mackenzie, P.I.4
  • 59
    • 0020586942 scopus 로고
    • Ethynylestradiol-17β D-ring glucuronide conjugates are potent cholestatic agents in the rat
    • M. Vore, H. Hadd, and W. Slikker, Jr., Ethynylestradiol-17β D-ring glucuronide conjugates are potent cholestatic agents in the rat, Life. Sci., 32, 2989 (1983).
    • (1983) Life. Sci. , vol.32 , pp. 2989
    • Vore, M.1    Hadd, H.2    Slikker W., Jr.3
  • 60
    • 0027242397 scopus 로고
    • Validation and use of cloned, expressed human drug-metabolizing enzymes in heterologous cells for analysis of drug metabolism and drug-drug interactions
    • R. P. Remmel and B. Burchell, Validation and use of cloned, expressed human drug-metabolizing enzymes in heterologous cells for analysis of drug metabolism and drug-drug interactions, Biochem. Pharmacol., 46, 559 (1993).
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 559
    • Remmel, R.P.1    Burchell, B.2
  • 62
    • 0015523047 scopus 로고
    • Regulation of microsomal enzymes by phospholipids. V. Kinetic studies of hepatic uridine diphosphate-glucuronyltransferase
    • D. A. Vessey and D. Zakim, Regulation of microsomal enzymes by phospholipids. V. Kinetic studies of hepatic uridine diphosphate-glucuronyltransferase, J. Biol. Chem., 247, 3023 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 3023
    • Vessey, D.A.1    Zakim, D.2
  • 63
    • 0023146762 scopus 로고
    • The enzymatic mechanism of glucuronidation catalyzed by two purified rat liver steroid UDP-glucuronosyltransferases
    • C. N. Falany, M. D. Green, and T. R. Tephly, The enzymatic mechanism of glucuronidation catalyzed by two purified rat liver steroid UDP-glucuronosyltransferases, J. Biol. Chem., 262, 1218 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 1218
    • Falany, C.N.1    Green, M.D.2    Tephly, T.R.3
  • 64
    • 0021061756 scopus 로고
    • Kinetic properties of the rat intestinal microsomal 1-naphthol:UDP-glucuronosyl transferase. Inhibition by UDP and UDP-N-acetylglucosamine
    • A. S. Koster and J. Noordhoek, Kinetic properties of the rat intestinal microsomal 1-naphthol:UDP-glucuronosyl transferase. Inhibition by UDP and UDP-N-acetylglucosamine, Biochim. Biophys. Acta, 761, 76 (1983).
    • (1983) Biochim. Biophys. Acta , vol.761 , pp. 76
    • Koster, A.S.1    Noordhoek, J.2
  • 65
    • 0015523747 scopus 로고
    • A study on the enzymatic mechanism of guinea-pig hepatic-microsomal bilirubin glucuronyl transferase
    • R. F. Potrepka and J. L. Spratt, A study on the enzymatic mechanism of guinea-pig hepatic-microsomal bilirubin glucuronyl transferase, Eur. J. Biochem., 29, 433 (1972).
    • (1972) Eur. J. Biochem. , vol.29 , pp. 433
    • Potrepka, R.F.1    Spratt, J.L.2
  • 66
    • 0016554213 scopus 로고
    • Morphine metabolism. IV. Studies on the mechanism of morphine: Uridine diphosphoglucuronyltransferase and its activation by bilirubin
    • E. Sanchez and T. R. Tephly, Morphine metabolism. IV. Studies on the mechanism of morphine: Uridine diphosphoglucuronyltransferase and its activation by bilirubin, Mol. Pharmacol., 11, 613 (1975).
    • (1975) Mol. Pharmacol. , vol.11 , pp. 613
    • Sanchez, E.1    Tephly, T.R.2
  • 67
    • 0017106709 scopus 로고
    • Kinetics of steroid transport through cell membranes: Comparison of the uptake of cortisol by isolated rat liver cells with binding of cortisol to rat liver cytosol
    • M. L. Rao, G. S. Rao, and H. Breuer, Kinetics of steroid transport through cell membranes: Comparison of the uptake of cortisol by isolated rat liver cells with binding of cortisol to rat liver cytosol, Biochim. Biophys. Acta, 452, 89 (1976).
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 89
    • Rao, M.L.1    Rao, G.S.2    Breuer, H.3
  • 68
    • 0020491333 scopus 로고
    • Factors modulating the catalytic specificity of a pure form of UDP-glucuronyltransferase
    • J. Magdalou, Y. Hochman, and D. Zakim, Factors modulating the catalytic specificity of a pure form of UDP-glucuronyltransferase, J. Biol. Chem., 257, 13,624 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 13624
    • Magdalou, J.1    Hochman, Y.2    Zakim, D.3
  • 69
    • 0021338808 scopus 로고
    • Studies of the catalytic mechanism of microsomal UDP-glucuronyltransferase. Alpha-glucuronidase activity and its stimulation by phospholipids
    • Y. Hochman and D. Zakim, Studies of the catalytic mechanism of microsomal UDP-glucuronyltransferase. Alpha-glucuronidase activity and its stimulation by phospholipids, J. Biol. Chem., 259, 5521 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 5521
    • Hochman, Y.1    Zakim, D.2
  • 70
    • 0021112015 scopus 로고
    • Evidence for an active site arginine in UDP-glucuronyltransferase
    • D. Zakim, Y. Hochman, and W. C. Kenney, Evidence for an active site arginine in UDP-glucuronyltransferase, J. Biol. Chem., 258, 6430 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 6430
    • Zakim, D.1    Hochman, Y.2    Kenney, W.C.3
  • 71
    • 0030989680 scopus 로고    scopus 로고
    • Photoaffinity labeling studies of the human recombinant UDP-glucuronosyltransferase, UGT1*6, with 5-azido-UDP-glucuronic acid
    • E. Battaglia, S. Nowell, R. R. Drake, J. Magdalou, S. Fournel-Gigleux, C. Senay, and A. Radominska, Photoaffinity labeling studies of the human recombinant UDP-glucuronosyltransferase, UGT1*6, with 5-azido-UDP-glucuronic acid., Drug Metab. Disp., 25, 406 (1997).
    • (1997) Drug Metab. Disp. , vol.25 , pp. 406
    • Battaglia, E.1    Nowell, S.2    Drake, R.R.3    Magdalou, J.4    Fournel-Gigleux, S.5    Senay, C.6    Radominska, A.7
  • 72
    • 0027991904 scopus 로고
    • Investigation of the substrate specificity of a cloned expressed human bilirubin UDP-glucuronosyltrans-ferase: UDP-sugar specificity and involvement in steroid and xenobiotic glucuronidation
    • S. B. Senafi, D. J. Clarke, and B. Burchell, Investigation of the substrate specificity of a cloned expressed human bilirubin UDP-glucuronosyltrans-ferase: UDP-sugar specificity and involvement in steroid and xenobiotic glucuronidation, Biochem. J., 303, 233 (1994).
    • (1994) Biochem. J. , vol.303 , pp. 233
    • Senafi, S.B.1    Clarke, D.J.2    Burchell, B.3
  • 73
    • 0016853644 scopus 로고
    • Commentary: Control of UDP-glucuronyltransferase activity
    • G. J. Dutton, Commentary: Control of UDP-glucuronyltransferase activity, Biochem. Pharmacol., 24, 1835 (1975).
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 1835
    • Dutton, G.J.1
  • 74
    • 0013958571 scopus 로고
    • The competitive inhibition of p-nitrophenyl-beta-D-glucopyranosiduronic acid synthesis by aliphatic alcohols in vitro
    • O. Hanninen and K. Alanen, The competitive inhibition of p-nitrophenyl-beta-D-glucopyranosiduronic acid synthesis by aliphatic alcohols in vitro, Biochem. Pharmacol., 15, 1465 (1966).
    • (1966) Biochem. Pharmacol. , vol.15 , pp. 1465
    • Hanninen, O.1    Alanen, K.2
  • 75
    • 0018865574 scopus 로고
    • Lipophilicity of acceptor substrate as a factor in "late foetal" microsomal UDP-glucuronosyltransferase activity
    • H. P. A. Illing, Lipophilicity of acceptor substrate as a factor in "late foetal" microsomal UDP-glucuronosyltransferase activity, Biochem. Pharmacol., 29, 99 (1980).
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 99
    • Illing, H.P.A.1
  • 76
    • 0016187530 scopus 로고
    • "Coupled transglucuronidation": A new tool for studying the latency of UDP-glucuronyl transferase
    • C. Berry and T. Hallinan, "Coupled transglucuronidation": A new tool for studying the latency of UDP-glucuronyl transferase., FEBS Lett., 42, 73 (1974).
    • (1974) FEBS Lett. , vol.42 , pp. 73
    • Berry, C.1    Hallinan, T.2
  • 77
    • 0016817805 scopus 로고
    • Guinea pig liver microsomal UDP-glucuronyltransferase: Compartmented or phospholipid-constrained
    • C. Berry, A. Stellon, and T. Hallinan, Guinea pig liver microsomal UDP-glucuronyltransferase: Compartmented or phospholipid-constrained, Biochim. Biophys. Acta, 403, 335 (1975).
    • (1975) Biochim. Biophys. Acta , vol.403 , pp. 335
    • Berry, C.1    Stellon, A.2    Hallinan, T.3
  • 78
    • 0017142383 scopus 로고
    • Summary of a novel, three-component regulatory model for uridine diphosphate glucuronyltransferase
    • C. Berry and T. Hallinan, Summary of a novel, three-component regulatory model for uridine diphosphate glucuronyltransferase, Biochem. Soc. Trans., 4, 650 (1976).
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 650
    • Berry, C.1    Hallinan, T.2
  • 79
    • 0023923099 scopus 로고
    • Phospholipids and UDP-glucuronosyltransferase. Structure/function relationships
    • D. Zakim, M. Cantor, and H. Eibl, Phospholipids and UDP-glucuronosyltransferase. Structure/function relationships, J. Biol. Chem., 263, 5164 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 5164
    • Zakim, D.1    Cantor, M.2    Eibl, H.3
  • 80
    • 84886639236 scopus 로고
    • Cloning of cDNAs coding for rat hepatic microsomal UDP-glucuronyltransferases
    • M. R. Jackson, L. R. McCarthy, R. B. Corser, G. C. Barr, and B. Burchell, Cloning of cDNAs coding for rat hepatic microsomal UDP-glucuronyltransferases, Gene, 34, 147 (1985).
    • (1985) Gene , vol.34 , pp. 147
    • Jackson, M.R.1    McCarthy, L.R.2    Corser, R.B.3    Barr, G.C.4    Burchell, B.5
  • 81
    • 0021205484 scopus 로고
    • Cloning and characterization of DNA complementary to rat liver UDP-glucuronosyltransferase mRNA
    • P. I. Mackenzie, F. J. Gonzalez, and I. S. Owens, Cloning and characterization of DNA complementary to rat liver UDP-glucuronosyltransferase mRNA, J. Biol. Chem., 259, 12,153 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 12153
    • Mackenzie, P.I.1    Gonzalez, F.J.2    Owens, I.S.3
  • 82
    • 0021765496 scopus 로고
    • Cleavage of nascent UDP-glucuronosyltransferase from rat liver by dog pancreatic microsomes
    • P. I. Mackenzie and I. S. Owens, Cleavage of nascent UDP-glucuronosyltransferase from rat liver by dog pancreatic microsomes, Biochem. Biophys. Res. Commun., 122, 1441 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1441
    • Mackenzie, P.I.1    Owens, I.S.2
  • 84
    • 0023035858 scopus 로고
    • Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA encoding a phenobarbital-inducible form
    • P. I. Mackenzie, Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA encoding a phenobarbital-inducible form, J. Biol. Chem., 267, 6119 (1986).
    • (1986) J. Biol. Chem. , vol.267 , pp. 6119
    • Mackenzie, P.I.1
  • 85
    • 0023655381 scopus 로고
    • Rat liver UDP-glucuronosyltransferase. Identification of cDNAs encoding two enzymes which glucuronidate testosterone, dihydrotestosterone, and β-estradiol
    • P. I. Mackenzie, Rat liver UDP-glucuronosyltransferase. Identification of cDNAs encoding two enzymes which glucuronidate testosterone, dihydrotestosterone, and β-estradiol, J. Biol. Chem., 262, 9744 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 9744
    • Mackenzie, P.I.1
  • 86
    • 0023019287 scopus 로고
    • Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase
    • T. Iyanagi, M. Haniu, K. Sogawa, Y. Fujii-Kuriyama, S. Watanabe, J. E. Shively, and K. F. Anan, Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase, J. Biol. Chem., 261, 15,607 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 15607
    • Iyanagi, T.1    Haniu, M.2    Sogawa, K.3    Fujii-Kuriyama, Y.4    Watanabe, S.5    Shively, J.E.6    Anan, K.F.7
  • 87
    • 0030846868 scopus 로고    scopus 로고
    • UDP-Glucuronosyltransferase, the role of the amino terminus in dimerization
    • R. Meech and P. I. Mackenzie, UDP-Glucuronosyltransferase, the role of the amino terminus in dimerization, J. Biol. Chem., 272, 26,913 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26913
    • Meech, R.1    Mackenzie, P.I.2
  • 88
    • 0029956992 scopus 로고    scopus 로고
    • Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1
    • R. Meech, G. Yogalingam, and P. Mackenzie, Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1, DNA Cell Biol., 15, 489 (1996).
    • (1996) DNA Cell Biol. , vol.15 , pp. 489
    • Meech, R.1    Yogalingam, G.2    Mackenzie, P.3
  • 89
    • 0024566868 scopus 로고
    • An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum
    • S. R. P. Shepherd, S. J. Baird, T. Hallinan, and B. Burchell, An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum, Biochem. J., 259, 617 (1989).
    • (1989) Biochem. J. , vol.259 , pp. 617
    • Shepherd, S.R.P.1    Baird, S.J.2    Hallinan, T.3    Burchell, B.4
  • 90
    • 0023909231 scopus 로고
    • Topology and regulation of bilirubin UDP-glucuronosyltransferase in sealed native microsomes from rat liver
    • F. Vanstapel and N. Blanckaert, Topology and regulation of bilirubin UDP-glucuronosyltransferase in sealed native microsomes from rat liver, Arch. Biochem. Biophys., 263, 216 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 216
    • Vanstapel, F.1    Blanckaert, N.2
  • 91
    • 0026699309 scopus 로고
    • Topological disposition of UDP-glucuronyltransferase in rat liver microsomes
    • H. Yokota, A. Yuasa, and R. Sato, Topological disposition of UDP-glucuronyltransferase in rat liver microsomes, J. Biochem., 112, 192 (1992).
    • (1992) J. Biochem. , vol.112 , pp. 192
    • Yokota, H.1    Yuasa, A.2    Sato, R.3
  • 92
    • 0021430832 scopus 로고
    • Cell-free translation of mouse liver mRNA coding for two forms of UDP glucuronosyltransferase
    • P. I. Mackenzie, F. J. Gonzalez, and I. S. Owens, Cell-free translation of mouse liver mRNA coding for two forms of UDP glucuronosyltransferase, Arch. Biochem. Biophys., 230, 676 (1984).
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 676
    • Mackenzie, P.I.1    Gonzalez, F.J.2    Owens, I.S.3
  • 93
    • 0031010059 scopus 로고    scopus 로고
    • Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes
    • S. Ikushiro, Y. Emi, and T. Iyanagi, Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes, Biochemistry, 36, 7154 (1997).
    • (1997) Biochemistry , vol.36 , pp. 7154
    • Ikushiro, S.1    Emi, Y.2    Iyanagi, T.3
  • 95
    • 0028116221 scopus 로고
    • Radiation inactivation analysis of microsomal UDP-glucuronosyltransferases catalysing mono-and diglucuronide formation of 3,6-dihydroxybenzo(a)pyrene and 3,6-dihydroxychrysene
    • H. Gschaidmeier and K. W. Bock, Radiation inactivation analysis of microsomal UDP-glucuronosyltransferases catalysing mono-and diglucuronide formation of 3,6-dihydroxybenzo(a)pyrene and 3,6-dihydroxychrysene, Biochem. Pharmacol., 48, 545 (1994).
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 545
    • Gschaidmeier, H.1    Bock, K.W.2
  • 96
    • 0021133988 scopus 로고
    • The molecular weights of UDP-glucuronyltransferase determined with radiation-inactivation analysis. A molecular model of bilirubin UDP-glucuronyltransferase
    • W. H. Peters, P. L. Jansen, and H. Nauta, The molecular weights of UDP-glucuronyltransferase determined with radiation-inactivation analysis. A molecular model of bilirubin UDP-glucuronyltransferase, J. Biol. Chem., 259, 11,701 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 11701
    • Peters, W.H.1    Jansen, P.L.2    Nauta, H.3
  • 97
    • 0024521003 scopus 로고
    • In situ structural analysis of microsomal UDP-glucuronyltransferases by radiation inactivation
    • D. A. Vessey and E. S. Kempner, In situ structural analysis of microsomal UDP-glucuronyltransferases by radiation inactivation, J. Biol. Chem., 264, 6334 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 6334
    • Vessey, D.A.1    Kempner, E.S.2
  • 98
    • 0028873814 scopus 로고
    • Mechanism of stimulation of microsomal UDP-glucuronosyltransferase by UDP-N-acetylglucusamine
    • X. Bossuyt and N. Blanckaert, Mechanism of stimulation of microsomal UDP-glucuronosyltransferase by UDP-N-acetylglucusamine, Biochem. J., 305, 321 (1995).
    • (1995) Biochem. J. , vol.305 , pp. 321
    • Bossuyt, X.1    Blanckaert, N.2
  • 99
    • 0029913593 scopus 로고    scopus 로고
    • Uridine diphosphoxylose enhances hepatic microsomal UDP-glucuronic glucuronosyltransferase activity by stimulating transport of UDP-glucuronic acid across the endoplasmic reticulum membrane
    • X. Bossuyt and N. Blanckaert, Uridine diphosphoxylose enhances hepatic microsomal UDP-glucuronic glucuronosyltransferase activity by stimulating transport of UDP-glucuronic acid across the endoplasmic reticulum membrane, Biochem. J., 315, 189 (1996).
    • (1996) Biochem. J. , vol.315 , pp. 189
    • Bossuyt, X.1    Blanckaert, N.2
  • 100
    • 0027935783 scopus 로고
    • Hepatobiliary elimination of the peroxisome proliferator nafenopin by conjugation and subsequent ATP-dependent transport across the canlicular membrane
    • G. Jedlitschky, I. Leier, M. Bohme, U. Buchholz, J. Bar-Tana, and D. Keppler, Hepatobiliary elimination of the peroxisome proliferator nafenopin by conjugation and subsequent ATP-dependent transport across the canlicular membrane, Biochem. Pharmacol., 48, 1113 (1994).
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1113
    • Jedlitschky, G.1    Leier, I.2    Bohme, M.3    Buchholz, U.4    Bar-Tana, J.5    Keppler, D.6
  • 101
    • 0030668526 scopus 로고    scopus 로고
    • ATP-dependent transport of bilirubin glucuronides by the multidrug resistance protein MRP1 and its hepatocyte canalicular isoform MRP2
    • G. Jedlitschky, I. Leier, U. Buchholz, J. Hummel-Eisenbeiss, B. Burchell, and D. Keppler, ATP-dependent transport of bilirubin glucuronides by the multidrug resistance protein MRP1 and its hepatocyte canalicular isoform MRP2, Biochem. J., 327, 305 (1997).
    • (1997) Biochem. J. , vol.327 , pp. 305
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Hummel-Eisenbeiss, J.4    Burchell, B.5    Keppler, D.6
  • 102
    • 0030063480 scopus 로고    scopus 로고
    • Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump
    • G. Jedlitschky, I. Leier, U. Buchholz, K. Barnouin, G. Kurz, and D. Keppler, Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump, Cancer Res., 56, 988 (1996).
    • (1996) Cancer Res. , vol.56 , pp. 988
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Barnouin, K.4    Kurz, G.5    Keppler, D.6
  • 103
    • 0029986408 scopus 로고    scopus 로고
    • Absence of the canalicular isoform of the MRP gene-encoded conjugate export pump from the hepatocytes in Dubin-Johnson syndrome
    • J. Kartenbeck, U. Leuschner, R. Mayer, and D. Keppler, Absence of the canalicular isoform of the MRP gene-encoded conjugate export pump from the hepatocytes in Dubin-Johnson syndrome, Hepatology, 23, 1061 (1996).
    • (1996) Hepatology , vol.23 , pp. 1061
    • Kartenbeck, J.1    Leuschner, U.2    Mayer, R.3    Keppler, D.4
  • 104
    • 0031715907 scopus 로고    scopus 로고
    • Human mast cells secreting leukotriene C4 express the MRP1 gene-encoded conjugate export pump
    • G. Bartosz, J. Konig, D. Keppler, and W. Hagmann, Human mast cells secreting leukotriene C4 express the MRP1 gene-encoded conjugate export pump, Biol. Chem., 379, 1121 (1998).
    • (1998) Biol. Chem. , vol.379 , pp. 1121
    • Bartosz, G.1    Konig, J.2    Keppler, D.3    Hagmann, W.4
  • 105
    • 0031758818 scopus 로고    scopus 로고
    • Expression of the apical conjugate export pump, Mrp2, in the polarized hepatoma cell line, WIF-B
    • A. T. Nies, T. Cantz, M. Brom, I. Leier, and D. Keppler, Expression of the apical conjugate export pump, Mrp2, in the polarized hepatoma cell line, WIF-B, Hepatology, 28, 1332 (1998).
    • (1998) Hepatology , vol.28 , pp. 1332
    • Nies, A.T.1    Cantz, T.2    Brom, M.3    Leier, I.4    Keppler, D.5
  • 106
    • 0029862844 scopus 로고    scopus 로고
    • Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles
    • G. Banhegyi, L. Braun, P. Marcolongo, M. Csala, R. Fulceri, J. Mandl, and A. Benedetti, Evidence for an UDP-glucuronic acid/phenol glucuronide antiport in rat liver microsomal vesicles, Biochem. J., 315, 171 (1996).
    • (1996) Biochem. J. , vol.315 , pp. 171
    • Banhegyi, G.1    Braun, L.2    Marcolongo, P.3    Csala, M.4    Fulceri, R.5    Mandl, J.6    Benedetti, A.7
  • 109
    • 0019879365 scopus 로고
    • Modification of functional arginine residues in purified bovine testicular hyaluronidase with butane-2,3-dione
    • P. Gacesa, M. J. Savitsky, K. S. Dodgson, and A. H. Olavesen, Modification of functional arginine residues in purified bovine testicular hyaluronidase with butane-2,3-dione, Biochim. Biophys. Acta, 661, 205 (1981).
    • (1981) Biochim. Biophys. Acta , vol.661 , pp. 205
    • Gacesa, P.1    Savitsky, M.J.2    Dodgson, K.S.3    Olavesen, A.H.4
  • 110
    • 0021262685 scopus 로고
    • Specific inactivation of the phosphohydrolase component of the hepatic microsomal glucose-6-phosphatase system by diethyl pyrocarbonate
    • W. J. Arion, B. Burchell, and A. Burchell, Specific inactivation of the phosphohydrolase component of the hepatic microsomal glucose-6-phosphatase system by diethyl pyrocarbonate, Biochem. J., 220, 342 (1984).
    • (1984) Biochem. J. , vol.220 , pp. 342
    • Arion, W.J.1    Burchell, B.2    Burchell, A.3
  • 111
    • 0032522255 scopus 로고    scopus 로고
    • Bilirubin is an effective antioxidant of peroxynitrite-mediated protein oxidation in human blood plasma
    • M. Minetti, C. Mallozzi, A. M. Di Stasi, and D. Pietraforte, Bilirubin is an effective antioxidant of peroxynitrite-mediated protein oxidation in human blood plasma, Arch. Biochem. Biophys., 352, 165 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 165
    • Minetti, M.1    Mallozzi, C.2    Di Stasi, A.M.3    Pietraforte, D.4
  • 116
    • 0029853289 scopus 로고    scopus 로고
    • Inhibition of bilirubin UDP-glucuronosyltransferase: A comparative molecular field analysis (CoMFA)
    • M. Said, A. Elass, J. C. Ziegler, B. Vergoten, and J. Magdalou, Inhibition of bilirubin UDP-glucuronosyltransferase: A comparative molecular field analysis (CoMFA), Quant. Structure Activity Relation, 15, 382 (1996).
    • (1996) Quant. Structure Activity Relation , vol.15 , pp. 382
    • Said, M.1    Elass, A.2    Ziegler, J.C.3    Vergoten, B.4    Magdalou, J.5
  • 120
    • 0028349889 scopus 로고
    • Photoaffinity labeling for evaluation of uridinyl analogs as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases
    • A. Radominska, P. Paul, S. Treat, H. Towbin, C. Pratt, J. Little, J. Magdalou, R. Lester, and R. R. Drake, Photoaffinity labeling for evaluation of uridinyl analogs as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases, Biochim. Biophys. Acta, 1205, 336 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 336
    • Radominska, A.1    Paul, P.2    Treat, S.3    Towbin, H.4    Pratt, C.5    Little, J.6    Magdalou, J.7    Lester, R.8    Drake, R.R.9
  • 121
  • 122
    • 0032031994 scopus 로고    scopus 로고
    • Inhibition of UDP-glucuronosyltransferase by 5′-O-amino acid and oligopeptide derivatives of uridine: Structure-activity relationships
    • Z. G. Naydenova, K. C. Grancharov, D. K. Alargov, E. V. Golovinsky, I. M. Stanoeva, L. D. Shalamanova, and I. K. Pajeva, Inhibition of UDP-glucuronosyltransferase by 5′-O-amino acid and oligopeptide derivatives of uridine: Structure-activity relationships, Z. Naturforsch., 53, 173 (1998).
    • (1998) Z. Naturforsch. , vol.53 , pp. 173
    • Naydenova, Z.G.1    Grancharov, K.C.2    Alargov, D.K.3    Golovinsky, E.V.4    Stanoeva, I.M.5    Shalamanova, L.D.6    Pajeva, I.K.7
  • 123
    • 0029593658 scopus 로고
    • Inhibition of UDP-glucuronyltransferase activity in rat liver microsomes by pyrimidine derivatives
    • Z. Naydenova, K. Grancharov, M. Shopova, and E. Golovinsky, Inhibition of UDP-glucuronyltransferase activity in rat liver microsomes by pyrimidine derivatives, Compar. Biochem. Physiol., 112C, 321 (1995).
    • (1995) Compar. Biochem. Physiol. , vol.112 C , pp. 321
    • Naydenova, Z.1    Grancharov, K.2    Shopova, M.3    Golovinsky, E.4
  • 124
    • 0343488688 scopus 로고    scopus 로고
    • Monometoxytrityl derivatives of uridine as inhibitors of a human recombinant UDP-glucuronosyltransferase: UGT*6
    • V. Cano, C. Lorentz, J. Magdalou, V. Loppinet, G. Siest, and J. C. Ziegler, Monometoxytrityl derivatives of uridine as inhibitors of a human recombinant UDP-glucuronosyltransferase: UGT*6, Life Sci., 6, PL1 (1997).
    • (1997) Life Sci. , vol.6 PL1
    • Cano, V.1    Lorentz, C.2    Magdalou, J.3    Loppinet, V.4    Siest, G.5    Ziegler, J.C.6
  • 125
    • 0032476086 scopus 로고    scopus 로고
    • Inhibitory effects of uridine diphosphate on UDP-glucuronosyltransferase
    • H. Yokota, F. Ando, H. Iwano, and A. Yuasa, Inhibitory effects of uridine diphosphate on UDP-glucuronosyltransferase, Life Sci., 63, 1693 (1998).
    • (1998) Life Sci. , vol.63 , pp. 1693
    • Yokota, H.1    Ando, F.2    Iwano, H.3    Yuasa, A.4
  • 126
    • 0029981211 scopus 로고    scopus 로고
    • Enzyme inhibition in open systems. Superiority of uncompetitive agents
    • A. M. Westley and J. Westley, Enzyme inhibition in open systems. Superiority of uncompetitive agents, J. Biol. Chem., 271, 5347 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 5347
    • Westley, A.M.1    Westley, J.2
  • 127
    • 0031688282 scopus 로고    scopus 로고
    • Enzymatic transition states and transition state analog design
    • V. L. Schramm, Enzymatic transition states and transition state analog design, Annu. Rev. Biochem., 67, 693 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 693
    • Schramm, V.L.1
  • 128
    • 0028287938 scopus 로고
    • Transition state analysis and inhibitor design for enzymatic reactions
    • V. L. Schramm, Transition state analysis and inhibitor design for enzymatic reactions, J. Biol. Chem., 269, 18,259 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18259
    • Schramm, V.L.1
  • 129
    • 0023137126 scopus 로고
    • Isolation and purification of two human liver UDP-glucuronosyltransferases
    • Y. M. Irshaid and T. R. Tephly, Isolation and purification of two human liver UDP-glucuronosyltransferases, Mol. Pharmacol., 31, 21 (1987).
    • (1987) Mol. Pharmacol. , vol.31 , pp. 21
    • Irshaid, Y.M.1    Tephly, T.R.2
  • 130
    • 0025824215 scopus 로고
    • Isolation and characterization of hyodeoxycholic acid:UDP-glucuronosyltransferase from human liver
    • H. Matern, N. Lappas, and S. Matern, Isolation and characterization of hyodeoxycholic acid:UDP-glucuronosyltransferase from human liver, Eur. J. Biochem., 200, 393 (1991).
    • (1991) Eur. J. Biochem. , vol.200 , pp. 393
    • Matern, H.1    Lappas, N.2    Matern, S.3
  • 131
    • 0026756613 scopus 로고
    • Photoaffinity labeling of glycosyltransferases
    • R. R. Drake and A. D. Elbein, Photoaffinity labeling of glycosyltransferases, Glycobiology, 2, 279 (1992).
    • (1992) Glycobiology , vol.2 , pp. 279
    • Drake, R.R.1    Elbein, A.D.2
  • 132
    • 0028203281 scopus 로고
    • Synthesis and uses of azido-nucleoside diphosphate sugar photoaffinity analogs
    • A. Radominska and R. Drake, Synthesis and uses of azido-nucleoside diphosphate sugar photoaffinity analogs, Methods Enzymol., 230, 330 (1994).
    • (1994) Methods Enzymol. , vol.230 , pp. 330
    • Radominska, A.1    Drake, R.2
  • 133
    • 0022400351 scopus 로고
    • Furosemide 1-o-acyl glucuronide. In vitro biosynthesis and pH-dependent isomerization to β-glucuronidase-resistant forms
    • A. Rachmel, G. A. Hazelton, A. L. Yergey, and D. J. Liberate, Furosemide 1-O-acyl glucuronide. In vitro biosynthesis and pH-dependent isomerization to β-glucuronidase-resistant forms, Drug Metab. Disp., 13, 705 (1985).
    • (1985) Drug Metab. Disp. , vol.13 , pp. 705
    • Rachmel, A.1    Hazelton, G.A.2    Yergey, A.L.3    Liberate, D.J.4
  • 134
    • 0026327990 scopus 로고
    • Radominska, synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins
    • R. R. Drake, P. Zimniak, B. E. Haley, R. Lester, A. D. Elbein, and A. Radominska, Synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins, J. Biol. Chem., 266, 23,257 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 23257
    • Drake, R.R.1    Zimniak, P.2    Haley, B.E.3    Lester, R.4    Elbein, A.D.5
  • 135
    • 0000811210 scopus 로고
    • Purification, photoaffinity labeling and properties of plant UDP-glucose: Phosphoryldolichol glucosyltransferase
    • R. R. Drake, G. P. Kaushal, I. Pastuszak, and A. D. Elbein, Purification, photoaffinity labeling and properties of plant UDP-glucose: Phosphoryldolichol glucosyltransferase, Plant Physiol., 97, 396 (1991).
    • (1991) Plant Physiol. , vol.97 , pp. 396
    • Drake, R.R.1    Kaushal, G.P.2    Pastuszak, I.3    Elbein, A.D.4
  • 136
    • 0028314103 scopus 로고
    • Bile acid glucuronidation by rat liver microsomes and cDNA-expressed UDP-glucuronosyltransferases
    • A. Radominska, J. M. Little, R. Lester, and P. I. Mackenzie, Bile acid glucuronidation by rat liver microsomes and cDNA-expressed UDP-glucuronosyltransferases, Biochim. Biophys. Acta, 1205, 75 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 75
    • Radominska, A.1    Little, J.M.2    Lester, R.3    Mackenzie, P.I.4
  • 137
    • 0028036952 scopus 로고
    • Characterization of UDP-glucuronic acid transport in rat liver microsomal vesicles with photoaffinity analogs
    • A. Radominska, C. Berg, S. Treat, J. M. Little, J. Gollan, R. Lester, and R. Drake, Characterization of UDP-glucuronic acid transport in rat liver microsomal vesicles with photoaffinity analogs, Biochim. Biophys. Acta, 1195, 63 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1195 , pp. 63
    • Radominska, A.1    Berg, C.2    Treat, S.3    Little, J.M.4    Gollan, J.5    Lester, R.6    Drake, R.7
  • 138
    • 0024381187 scopus 로고
    • Synthesis and properties of 5-azido-UDP-glucose: Development of photoaffinity probes for nucleotide diphospate sugar binding sites
    • R. R. Drake, R. K. Evans, M. J. Wolf, and B. E. Haley, Synthesis and properties of 5-azido-UDP-glucose: Development of photoaffinity probes for nucleotide diphospate sugar binding sites, J. Biol. Chem., 264, 11,928 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 11928
    • Drake, R.R.1    Evans, R.K.2    Wolf, M.J.3    Haley, B.E.4
  • 140
    • 0026349175 scopus 로고
    • Nucleotide photoaffinity labeling of protein kinase subunits
    • B. E. Haley, Nucleotide photoaffinity labeling of protein kinase subunits, Methods Emzymol., 200, 477 (1991).
    • (1991) Methods Emzymol. , vol.200 , pp. 477
    • Haley, B.E.1
  • 141
    • 0026667310 scopus 로고
    • Application of 5-azido-UDP-glucose and 5-azido-UDP-glucuronic acid photoaffinity probes for the determination of the active site orientation of microsomal UDP-glucosyltransferases and UDP-glucuronosyltransferases
    • R. Drake, I. Igari, R. Lester, A. Elbein, and A. Radominska, Application of 5-azido-UDP-glucose and 5-azido-UDP-glucuronic acid photoaffinity probes for the determination of the active site orientation of microsomal UDP-glucosyltransferases and UDP-glucuronosyltransferases, J. Biol. Chem., 267, 11,360 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 11360
    • Drake, R.1    Igari, I.2    Lester, R.3    Elbein, A.4    Radominska, A.5
  • 143
    • 0031021739 scopus 로고    scopus 로고
    • Glucuronidation of all trans-retinoic acid and 5,6-epoxy-all trans-retinoic acid: Activation of rat liver microsomal UDP-glucuronosyltranferase activity by alamethicin
    • J. M. Little, P. A. Lehman, S. Nowell, V. Samokyszyn, and A. Radominska, Glucuronidation of all trans-retinoic acid and 5,6-epoxy-all trans-retinoic acid: Activation of rat liver microsomal UDP-glucuronosyltranferase activity by alamethicin, Drug Metab. Disp., 25, 5 (1997).
    • (1997) Drug Metab. Disp. , vol.25 , pp. 5
    • Little, J.M.1    Lehman, P.A.2    Nowell, S.3    Samokyszyn, V.4    Radominska, A.5
  • 145
    • 0344505956 scopus 로고    scopus 로고
    • Synthesis and characterization of a new fluorescent photoaffinity probe, 7-azido-4-methylcoumarin. Application to labeling the aglycon binding site of human liver recombinant UGT1A6
    • in press
    • C. Senay, E. Battaglia, S. Fournel-Gigleux, J. Magdalou, and A. Radominska-Pandya, Synthesis and characterization of a new fluorescent photoaffinity probe, 7-azido-4-methylcoumarin. Application to labeling the aglycon binding site of human liver recombinant UGT1A6, Arch. Biochem. Biophys. (in press).
    • Arch. Biochem. Biophys.
    • Senay, C.1    Battaglia, E.2    Fournel-Gigleux, S.3    Magdalou, J.4    Radominska-Pandya, A.5
  • 146
  • 147
    • 0015171336 scopus 로고
    • Formation of bilirubin glucoside
    • K. P. Wong, Formation of bilirubin glucoside, Biochem. J., 125, 929 (1971).
    • (1971) Biochem. J. , vol.125 , pp. 929
    • Wong, K.P.1
  • 148
    • 0021225545 scopus 로고
    • Bilirubin mono-and di-glucuronide formation by purified rat liver microsomal bilirubin UDP-glucuronyltransferase
    • B. Burchell and N. Blanckaert, Bilirubin mono-and di-glucuronide formation by purified rat liver microsomal bilirubin UDP-glucuronyltransferase, Biochem. J., 223, 461 (1984).
    • (1984) Biochem. J. , vol.223 , pp. 461
    • Burchell, B.1    Blanckaert, N.2
  • 150
    • 0015584212 scopus 로고
    • Studies of mammalian glucoside conjugation
    • T. Gessner, A. Jacknowitz, and C. A. Vollmer, Studies of mammalian glucoside conjugation, Biochem. J., 132, 249 (1973).
    • (1973) Biochem. J. , vol.132 , pp. 249
    • Gessner, T.1    Jacknowitz, A.2    Vollmer, C.A.3
  • 151
    • 0020094818 scopus 로고
    • Bile acid and bile salt disrupt gastric mucosal barrier in the dog by different mechanisms
    • W. C. Duane, D. M. Wiegand, and C. E. Sievert, Bile acid and bile salt disrupt gastric mucosal barrier in the dog by different mechanisms, Am. J. Physiol., 242, G95 (1982).
    • (1982) Am. J. Physiol. , vol.242
    • Duane, W.C.1    Wiegand, D.M.2    Sievert, C.E.3
  • 152
    • 0022529717 scopus 로고
    • Induction of UDP-glucuronyl transferase mRNA in embryonic chick livers by phenobarbital
    • M. R. Jackson, S. M. Kennedy, G. Lown, and B. Burchell, Induction of UDP-glucuronyl transferase mRNA in embryonic chick livers by phenobarbital, Biochem. Pharmacol., 35, 1191 (1986).
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1191
    • Jackson, M.R.1    Kennedy, S.M.2    Lown, G.3    Burchell, B.4
  • 153
    • 0023031991 scopus 로고
    • Rat liver UDP-glucuronosyltransferase. CDNA sequence and expression of a form glucuronidating 3-hydroxyandrogens
    • P. I. Mackenzie, Rat liver UDP-glucuronosyltransferase. cDNA sequence and expression of a form glucuronidating 3-hydroxyandrogens, J. Biol. Chem., 261, 14,112 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 14112
    • Mackenzie, P.I.1
  • 154
    • 0000614010 scopus 로고
    • Enzymatic oxidation of undine diphosphate glucose to uridine diphosphate glucuronic acid
    • J. L. Strominger, H. M. Kalckar, J. Axelrod, and E. S. Maxwell, Enzymatic oxidation of undine diphosphate glucose to uridine diphosphate glucuronic acid, J. Am. Chem. Soc., 76, 6411 (1954).
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 6411
    • Strominger, J.L.1    Kalckar, H.M.2    Axelrod, J.3    Maxwell, E.S.4
  • 155
    • 0023763078 scopus 로고
    • A membrane transporter mediates access of uridine 5′-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implications for glucuronidation reaction
    • S. C. Hauser, J. C. Ziurys, and J. L. Gollan, A membrane transporter mediates access of uridine 5′-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implications for glucuronidation reaction, Biochim. Biophys. Acta, 967, 149 (1988).
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 149
    • Hauser, S.C.1    Ziurys, J.C.2    Gollan, J.L.3
  • 156
    • 0026517062 scopus 로고
    • New developments in glucuronidation research: Report of a workshop on "glucuronidation, its role in health and disease,"
    • P. L. M. Jansen, G. J. Mulder, and B. Burchell, New developments in glucuronidation research: Report of a workshop on "Glucuronidation, Its Role in Health and Disease," Hepatology, 15, 532 (1992).
    • (1992) Hepatology , vol.15 , pp. 532
    • Jansen, P.L.M.1    Mulder, G.J.2    Burchell, B.3
  • 157
    • 0028796027 scopus 로고
    • Membrane translocation and regulation of uridine diphosphate-glucuronic acid uptake in rat liver microsomal vesicles
    • C. Berg, A. Radominska, R. Lester, and J. Gollan, Membrane translocation and regulation of uridine diphosphate-glucuronic acid uptake in rat liver microsomal vesicles, Gastroenterology, 108, 183-192 (1995).
    • (1995) Gastroenterology , vol.108 , pp. 183192
    • Berg, C.1    Radominska, A.2    Lester, R.3    Gollan, J.4
  • 159
    • 0027216130 scopus 로고
    • Synthesis and characterization of a new class of inhibitors of membrane-associated UDP-glycosyltransferases
    • P. Paul, T. Lutz, C. Osborn, S. Kyosseva, A. Elbein, H. Towbin. A. Radominska, and R. Drake, Synthesis and characterization of a new class of inhibitors of membrane-associated UDP-glycosyltransferases, J. Biol. Chem., 268, 12,933 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 12933
    • Paul, P.1    Lutz, T.2    Osborn, C.3    Kyosseva, S.4    Elbein, A.5    Towbin, H.6    Radominska, A.7    Drake, R.8
  • 160
    • 0023904909 scopus 로고
    • Biosynthesis of hydroxyl-linked glucuronides of short-chain bile acids by rat liver 3-hydroxysteroid UDP-glucuronosyltransferase
    • A. Radominska, M. D. Green, P. Zimniak, and R. Lester, Biosynthesis of hydroxyl-linked glucuronides of short-chain bile acids by rat liver 3-hydroxysteroid UDP-glucuronosyltransferase, J. Lipid Res., 29, 501 (1988).
    • (1988) J. Lipid Res. , vol.29 , pp. 501
    • Radominska, A.1    Green, M.D.2    Zimniak, P.3    Lester, R.4
  • 161
    • 0032488649 scopus 로고    scopus 로고
    • A functional role for histidyl residues of the UDP-glucuronic acid carrier in rat endoplasmic reticulum membranes
    • E. Battaglia and A. Radominska-Pandya, A functional role for histidyl residues of the UDP-glucuronic acid carrier in rat endoplasmic reticulum
    • (1998) Biochemistry , vol.37 , pp. 258
    • Battaglia, E.1    Radominska-Pandya, A.2
  • 163
    • 0026644417 scopus 로고
    • Functional expression of zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site
    • B. S. Bundle, D. A. O'Brien, M. Alberti, P. Beyer, and J. E. Hearst, Functional expression of zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site, Proc. Natl. Acad. Sci. USA, 89, 9321 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9321
    • Bundle, B.S.1    O'Brien, D.A.2    Alberti, M.3    Beyer, P.4    Hearst, J.E.5
  • 164
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP, glucuronosyltransferase involved in substrate selection
    • P. I. Mackenzie, Expression of chimeric cDNAs in cell culture defines a region of UDP, glucuronosyltransferase involved in substrate selection, J. Biol. Chem., 265, 3432 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 3432
    • Mackenzie, P.I.1
  • 165
    • 0027749498 scopus 로고
    • Determination of the human liver UDP-glucuronosyltransferase 2B4 domains involved in the binding of UDP-glucuronic acid using photoaftinity labeling of fusion proteins
    • T. Pillot, M. Ouzzine, S. Fournel-Gigleux, C. LaFaurie, D. Tebbi, S. Treat, A. Radominska, R. Lester, G. Siest, and J. Magdalou, Determination of the human liver UDP-glucuronosyltransferase 2B4 domains involved in the binding of UDP-glucuronic acid using photoaftinity labeling of fusion proteins, Biochem. Biophys. Res. Commun, 197, 785 (1993).
    • (1993) Biochem. Biophys. Res. Commun , vol.197 , pp. 785
    • Pillot, T.1    Ouzzine, M.2    Fournel-Gigleux, S.3    LaFaurie, C.4    D Tebbi, S.T.5    Radominska, A.6    Lester, R.7    Siest, G.8    Magdalou, J.9
  • 166
    • 0029884743 scopus 로고    scopus 로고
    • Proteolytic mapping of the thymidine/thymidylate binding site of herpes simplex virus type 1 thymidine kinase: A general photoaffinity labeling method for identifying active-site peptides
    • T. M. Rechtin, M. E. Black, and R. R. Drake, Proteolytic mapping of the thymidine/thymidylate binding site of herpes simplex virus type 1 thymidine kinase: A general photoaffinity labeling method for identifying active-site peptides, Anal. Biochem., 237, 135 (1996).
    • (1996) Anal. Biochem. , vol.237 , pp. 135
    • Rechtin, T.M.1    Black, M.E.2    Drake, R.R.3
  • 167
    • 0020696906 scopus 로고
    • Affinity labeling of purine nucleotide sites in proteins
    • R. F. Colman, Affinity labeling of purine nucleotide sites in proteins, Anna. Rev. Biochem., 52, 67 (1983).
    • (1983) Anna. Rev. Biochem. , vol.52 , pp. 67
    • Colman, R.F.1
  • 168
    • 0020485888 scopus 로고
    • Interactions between the mitochondrial adenosinetriphosphatase and periodate-oxidized adenosine 5′-triphosphate, an affinity label for adenosine 5′-triphosphate binding sites
    • P. N. Lowe and R. B. Beechey, Interactions between the mitochondrial adenosinetriphosphatase and periodate-oxidized adenosine 5′-triphosphate, an affinity label for adenosine 5′-triphosphate binding sites, Biochemistry, 21, 4073 (1982).
    • (1982) Biochemistry , vol.21 , pp. 4073
    • Lowe, P.N.1    Beechey, R.B.2
  • 169
    • 0028805697 scopus 로고
    • Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2′,3′-dialdehyde affinity labeling
    • J. Kanaani, D. Maltby, P. Focia, and C. C. Wang, Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2′,3′-dialdehyde affinity labeling, Biochemistry, 34, 14,987 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14987
    • Kanaani, J.1    Maltby, D.2    Focia, P.3    Wang, C.C.4
  • 170
    • 0022005917 scopus 로고
    • Inhibition of hyaluronate synthesis
    • P. Prehm, Inhibition of hyaluronate synthesis, Biochem. J., 225, 699 (1985).
    • (1985) Biochem. J. , vol.225 , pp. 699
    • Prehm, P.1
  • 171
    • 0026051566 scopus 로고
    • Modification of the ATP inhibitory site of the Ascaris suun phosphofructokinase results in the stabilization of an inactive T state
    • G. S. J. Rao, P. F. Cook, and B. G. Harris, Modification of the ATP inhibitory site of the Ascaris suun phosphofructokinase results in the stabilization of an inactive T state, Biochemistry, 30, 9998 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9998
    • Rao, G.S.J.1    Cook, P.F.2    Harris, B.G.3
  • 172
    • 0029132172 scopus 로고
    • Inactivation of escherichia coli phosphoribosylpyrophosphate synthetase by the 2′,3′-dialdehyde derivative of ATP
    • I. Hilden, B. Hove-Jensen, and K. W. Harlow, Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by the 2′,3′-dialdehyde derivative of ATP, J. Biol. Chem., 270, 20,730 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20730
    • Hilden, I.1    Hove-Jensen, B.2    Harlow, K.W.3
  • 173
    • 0001036382 scopus 로고
    • Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells
    • D. Harding, S. Fournel-Gigleux, M. R. Jackson, and B. Burchell, Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells, Proc. Natl. Acad. Sci. USA, 85, 8381 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8381
    • Harding, D.1    Fournel-Gigleux, S.2    Jackson, M.R.3    Burchell, B.4
  • 174
    • 0027530118 scopus 로고
    • Substrate specificities of two stably expressed human liver UDP-glucuronosyltransferases of the UGT1 gene family
    • T. Ebner and B. Burchell, Substrate specificities of two stably expressed human liver UDP-glucuronosyltransferases of the UGT1 gene family, Drug Metab. Disp., 21, 50 (1993).
    • (1993) Drug Metab. Disp. , vol.21 , pp. 50
    • Ebner, T.1    Burchell, B.2
  • 176
    • 0031584094 scopus 로고    scopus 로고
    • 3H]all trans-retenoic acid to characterization of rat liver microsomal UP-glucuronosyltransferase(s) with activity toward retinoic acid
    • 3H]all trans-retenoic acid to characterization of rat liver microsomal UP-glucuronosyltransferase(s) with activity toward retinoic acid, Biochem. Biophys. Res. Commun., 230, 497 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 497
    • Little, J.M.1    Radominska, A.2
  • 178
    • 0029113143 scopus 로고
    • Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A
    • J. E. Wedekind, P. A. Frey, and I. Rayment, Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A. Biochemistry, 34, 11,049 (1995).
    • (1995) Biochemistry , vol.34 , pp. 11049
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 179
    • 0029895408 scopus 로고    scopus 로고
    • The human gene CGT encoding the UDP-galactose ceramide galactosyl transferase (cerebroside synthase): Cloning, characterization, and assignment to human chromosome 4, band q26
    • A. Bosio, E. Binczek, M. M. Lebeau, A. A. Fernald, and W. Stoffel, The human gene CGT encoding the UDP-galactose ceramide galactosyl transferase (cerebroside synthase): Cloning, characterization, and assignment to human chromosome 4, band q26, Genomics, 34, 69 (1996).
    • (1996) Genomics , vol.34 , pp. 69
    • Bosio, A.1    Binczek, E.2    Lebeau, M.M.3    Fernald, A.A.4    Stoffel, W.5
  • 180
    • 0024003767 scopus 로고
    • Sequence of three bronze alleles of maize and correlation with the genetic fine structure
    • E. J. Ralston, J. J. English, and H. K. Dooner, Sequence of three bronze alleles of maize and correlation with the genetic fine structure, Genetics, 119, 55 (1988).
    • (1988) Genetics , vol.119 , pp. 55
    • Ralston, E.J.1    English, J.J.2    Dooner, H.K.3
  • 181
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • M. D. Ayres, S. C. Howard, J. Kuzio, M. Lopez-Ferber, and R. D. Possee, The complete DNA sequence of Autographa californica nuclear polyhedrosis virus, Virology, 202, 586 (1994).
    • (1994) Virology , vol.202 , pp. 586
    • Ayres, M.D.1    Howard, S.C.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 182
    • 0025719224 scopus 로고
    • Cloning and characterization of two genes from Streptomyces lividans that confer inducible resistance to lincomycin and macrolide antibiotics
    • G. Jenkins and E. Cundliffe, Cloning and characterization of two genes from Streptomyces lividans that confer inducible resistance to lincomycin and macrolide antibiotics, Gene, 108, 55 (1991).
    • (1991) Gene , vol.108 , pp. 55
    • Jenkins, G.1    Cundliffe, E.2
  • 184
    • 0032513046 scopus 로고    scopus 로고
    • Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases
    • Y. Sakakibara, Y. Takami, T. Nakayama, M. Suiko, and M. C. Liu, Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases, J. Biol. Chem., 273, 6242 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6242
    • Sakakibara, Y.1    Takami, Y.2    Nakayama, T.3    Suiko, M.4    Liu, M.C.5
  • 185
    • 0032437886 scopus 로고    scopus 로고
    • A single amino acid, glu 146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3
    • R. Dajani, A. M. Hood, and M. W. H. Coughtrie, A single amino acid, glu 146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3, Mol. Pharmacol., 54, 942 (1998).
    • (1998) Mol. Pharmacol. , vol.54 , pp. 942
    • Dajani, R.1    Hood, A.M.2    Coughtrie, M.W.H.3
  • 187
    • 0030443993 scopus 로고    scopus 로고
    • Computer modeling of 3D structures of cytochrome P450s
    • Y. Chang, O. Stiffelman, and G. Loew, Computer modeling of 3D structures of cytochrome P450s, Biochimie, 78, 771 (1996).
    • (1996) Biochimie , vol.78 , pp. 771
    • Chang, Y.1    Stiffelman, O.2    Loew, G.3
  • 188
    • 0028774713 scopus 로고
    • Crystal structure of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • G. J. Kleywegt, T. Bergfors, H. Senn, P. LeMotte, B. Gsell, K. Shudo, and T. A. Jone, Crystal structure of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid, Structure, 2, 1241 (1994).
    • (1994) Structure , vol.2 , pp. 1241
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    LeMotte, P.4    Gsell, B.5    Shudo, K.6    Jone, T.A.7
  • 189
    • 44949272730 scopus 로고
    • A time-efficient, linear-space local similarity algorithm
    • X. Huang and W. Miller, A time-efficient, linear-space local similarity algorithm, Adv. Appl. Math., 12, 337 (1991).
    • (1991) Adv. Appl. Math. , vol.12 , pp. 337
    • Huang, X.1    Miller, W.2
  • 190
    • 0025861217 scopus 로고
    • Cloning and stable expression of a new member of the human liver phenol/bilirubin:UDP-glucuronosyltransferase cDNA family
    • R. Wooster, L. Sutherland, T. Ebner, D. Clarke, O. da Cruz e Silva, and B. Burchell, Cloning and stable expression of a new member of the human liver phenol/bilirubin:UDP-glucuronosyltransferase cDNA family, Biochem. J., 278, 465 (1991).
    • (1991) Biochem. J. , vol.278 , pp. 465
    • Wooster, R.1    Sutherland, L.2    Ebner, T.3    Clarke, D.4    Da Cruz E Silva, O.5    Burchell, B.6
  • 191
    • 0027469416 scopus 로고
    • Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase
    • T. W. Wilborn, K. A. Comer, T. P. Dooley, I. M. Reardon, R. L. Heinrikson, and C. N. Falany, Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase, Mol. Pharmacol., 43, 70 (1993).
    • (1993) Mol. Pharmacol. , vol.43 , pp. 70
    • Wilborn, T.W.1    Comer, K.A.2    Dooley, T.P.3    Reardon, I.M.4    Heinrikson, R.L.5    Falany, C.N.6
  • 194
    • 0026775534 scopus 로고
    • Characterization of a complementary DNA for rat liver aryl sulfotransferase IV and use in evaluating the hepatic gene transcript levels of rats at various stages of 2-acetylaminofluoreneinduced hepatocarcinogenesis
    • T. Yerokun, J. L. Etheredge, T. R. Norton, H. A. Carter, K. H. Chung, P. J. Birckbichler, and D. P. Ringer, Characterization of a complementary DNA for rat liver aryl sulfotransferase IV and use in evaluating the hepatic gene transcript levels of rats at various stages of 2-acetylaminofluoreneinduced hepatocarcinogenesis, Cancer Res., 52, 4779 (1992).
    • (1992) Cancer Res. , vol.52 , pp. 4779
    • Yerokun, T.1    Etheredge, J.L.2    Norton, T.R.3    Carter, H.A.4    Chung, K.H.5    Birckbichler, P.J.6    Ringer, D.P.7
  • 195
    • 0029122101 scopus 로고
    • Characterization and prevalence of a polymorphism in the 3′ untranslated region of cytochrome P4501Al in cancer-prone Atlantic tomcod
    • N. K. Roy, G. L. Kreamer, B. Konkle, C. Grunwald, and I. Wirgin, Characterization and prevalence of a polymorphism in the 3′ untranslated region of cytochrome P4501Al in cancer-prone Atlantic tomcod, Arch. Biochem. Biophys., 322, 204 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 204
    • Roy, N.K.1    Kreamer, G.L.2    Konkle, B.3    Grunwald, C.4    Wirgin, I.5
  • 197
    • 0025022689 scopus 로고
    • The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes
    • S. Yamano, J. Tatsuno, and F. J. Gonzalez, The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes, Biochemistry, 29, 1322 (1990).
    • (1990) Biochemistry , vol.29 , pp. 1322
    • Yamano, S.1    Tatsuno, J.2    Gonzalez, F.J.3
  • 198
    • 0025763625 scopus 로고
    • Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily
    • J. A. Goldstein, J. L. Raucy, J. A. Blaisdell, M. B. Faletto, and M. Romkes, Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily, Biochemistry, 30, 3247 (1991).
    • (1991) Biochemistry , vol.30 , pp. 3247
    • Goldstein, J.A.1    Raucy, J.L.2    Blaisdell, J.A.3    Faletto, M.B.4    Romkes, M.5
  • 200
    • 0041725049 scopus 로고    scopus 로고
    • The structure and function of the UDP-glucuronosyltransferase gene family
    • B. Burchell, C. H. Brierley, G. Managhan, and D. J. Clarke, The structure and function of the UDP-glucuronosyltransferase gene family, Adv. Pharmacol., 42, 335-338 (1998).
    • (1998) Adv. Pharmacol. , vol.42 , pp. 335-338
    • Burchell, B.1    Brierley, C.H.2    Managhan, G.3    Clarke, D.J.4
  • 202
    • 0029962074 scopus 로고    scopus 로고
    • Glucuronidation of amines and hydroxylated xenobiotics and endobiotics catalyzed by expressed human UGT1.4 protein
    • M. D. Green and T. R. Tephly, Glucuronidation of amines and hydroxylated xenobiotics and endobiotics catalyzed by expressed human UGT1.4 protein, Drug Metab. Disp., 24, 356 (1996).
    • (1996) Drug Metab. Disp. , vol.24 , pp. 356
    • Green, M.D.1    Tephly, T.R.2
  • 204
    • 0031570313 scopus 로고    scopus 로고
    • The regio-and stereo-selectivity of C19 and C21 hydroxysteroid glucuronidation by UGT2B7 and UGT2B11
    • C.-J. Jin, P. I. Mackenzie, and J. O. Miners, The regio-and stereo-selectivity of C19 and C21 hydroxysteroid glucuronidation by UGT2B7 and UGT2B11, Arch. Biochem. Biophy., 341, 207 (1997).
    • (1997) Arch. Biochem. Biophy. , vol.341 , pp. 207
    • Jin, C.-J.1    Mackenzie, P.I.2    Miners, J.O.3
  • 205
    • 0025321169 scopus 로고
    • Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells
    • J. K. Ritter, Y. Y. Sheen, and I. S. Owens, Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells, J. Biol. Chem., 265, 7900 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 7900
    • Ritter, J.K.1    Sheen, Y.Y.2    Owens, I.S.3
  • 206
    • 0344784391 scopus 로고    scopus 로고
    • Isolation and characterization of a human orphan UDP-glucuronosyltransferase, UGT2B11
    • M. Beaulieu, E. Lévesque, D. W. Hum, and A. Belanger, Isolation and characterization of a human orphan UDP-glucuronosyltransferase, UGT2B11, Biochem. Biophys. Res. Commun., 248, 44 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 44
    • Beaulieu, M.1    Lévesque, E.2    Hum, D.W.3    A Belanger4
  • 207
    • 0028031001 scopus 로고
    • Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) with activity toward steroid and xenobiotic substrates
    • M. D. Green, E. M. Oturu, and T. R. Tephly, Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) with activity toward steroid and xenobiotic substrates, Drug Metab. Disp., 22, 799 (1994).
    • (1994) Drug Metab. Disp. , vol.22 , pp. 799
    • Green, M.D.1    Oturu, E.M.2    Tephly, T.R.3
  • 209
    • 0031765698 scopus 로고    scopus 로고
    • Glucuronidation of amines and other xenobiotics catalyzed by expressed human UDP-glucuronosyltransferase 1A3
    • M. D. Green, C. D. King, B. Mojarrabi, P. I. Mackenzie, and T. R. Tephly, Glucuronidation of amines and other xenobiotics catalyzed by expressed human UDP-glucuronosyltransferase 1A3, Drug Metab. Disp., 26, 507 (1998).
    • (1998) Drug Metab. Disp. , vol.26 , pp. 507
    • Green, M.D.1    King, C.D.2    Mojarrabi, B.3    Mackenzie, P.I.4    Tephly, T.R.5
  • 210
    • 0030699360 scopus 로고    scopus 로고
    • Genetic polymorphism in the human UGT1A6 (planar phenol) UDP-glucuronosyltransferase: Pharmacological implications
    • M. Ciotti, A. Marrone, C. Potter, and I. S. Owens, Genetic polymorphism in the human UGT1A6 (planar phenol) UDP-glucuronosyltransferase: Pharmacological implications, Pharmacogenetics, 7, 485 (1997).
    • (1997) Pharmacogenetics , vol.7 , pp. 485
    • Ciotti, M.1    Marrone, A.2    Potter, C.3    Owens, I.S.4
  • 212
    • 0027484631 scopus 로고
    • Drug and xenobiotic glucuronidation catalysed by cloned human liver UDP-glucuronosyltransferases stably expressed in tissue culture cell lines
    • R. Wooster, T. Ebner, L. Sutherland, D. Clarke, and B. Burchell, Drug and xenobiotic glucuronidation catalysed by cloned human liver UDP-glucuronosyltransferases stably expressed in tissue culture cell lines, Toxicology, 82, 119 (1993).
    • (1993) Toxicology , vol.82 , pp. 119
    • Wooster, R.1    Ebner, T.2    Sutherland, L.3    Clarke, D.4    Burchell, B.5
  • 213
    • 0031590285 scopus 로고    scopus 로고
    • The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid
    • B. Mojarrabi and P. I. Mackenzie, The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid, Biochem. Biophys. Res. Commun., 238, 775 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 775
    • Mojarrabi, B.1    Mackenzie, P.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.