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Volumn 45, Issue 7, 2006, Pages 2322-2332

Phenylalanine 90 and 93 are localized within the phenol binding site of human UDP-glucuronosyltransferase 1A10 as determined by photoaffinity labeling, mass spectrometry, and site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; BENZENE; DESORPTION; IONIZATION; MASS SPECTROMETRY; PHENOLS; SYNTHESIS (CHEMICAL);

EID: 33144483681     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0519001     Document Type: Article
Times cited : (38)

References (59)
  • 1
    • 0021765496 scopus 로고
    • Cleavage of nascent UDP-glucuronosyltransferase from rat liver by dog pancreatic microsomes
    • Mackenzie, P. I., and Owens, I. S. (1984) Cleavage of nascent UDP-glucuronosyltransferase from rat liver by dog pancreatic microsomes, Biochem. Biophys. Res. Commun. 122, 1441-1449.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1441-1449
    • Mackenzie, P.I.1    Owens, I.S.2
  • 2
    • 0032973964 scopus 로고    scopus 로고
    • Expression of a functionally active human hepatic UDP- glucuronosyltransferase (UGT1A6) lacking the N-terminal signal sequence in the endoplasmic reticulum
    • Ouzzine, M., Magdalou, J., Burchell, B., and Fournel-Gigleux, S. (1999) Expression of a functionally active human hepatic UDP-glucuronosyltransferase (UGT1A6) lacking the N-terminal signal sequence in the endoplasmic reticulum, FEBS Lett. 454, 187-91.
    • (1999) FEBS Lett. , vol.454 , pp. 187-191
    • Ouzzine, M.1    Magdalou, J.2    Burchell, B.3    Fournel-Gigleux, S.4
  • 3
    • 0033615624 scopus 로고    scopus 로고
    • An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum
    • Ouzzine, M., Magdalou, J., Burchell, B., and Fournel-Gigleux, S. (1999) An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum, J. Biol. Chem. 274, 31401-31409.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31401-31409
    • Ouzzine, M.1    Magdalou, J.2    Burchell, B.3    Fournel-Gigleux, S.4
  • 4
    • 0032147023 scopus 로고    scopus 로고
    • Determinants of UDP glucuronosyltransferase membrane association and residency in the endoplasmic reticulum
    • Meech, R., and Mackenzie, P. I. (1998) Determinants of UDP glucuronosyltransferase membrane association and residency in the endoplasmic reticulum, Arch. Biochem. Biophys. 356, 77-85.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 77-85
    • Meech, R.1    Mackenzie, P.I.2
  • 5
    • 0023035858 scopus 로고
    • Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA encoding a phenobarbital -inducible form
    • Mackenzie, P. I. (1986) Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA encoding a phenobarbital -inducible form, J. Biol. Chem. 261, 6119-6125.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6119-6125
    • Mackenzie, P.I.1
  • 6
    • 0023655381 scopus 로고
    • Rat liver UDP-glucuronosyltransferase. Identification of cDNAs encoding two enzymes which glucuronidate testosterone, dihydrotestosterone, and b-estradiol
    • Mackenzie, P. I. (1987) Rat liver UDP-glucuronosyltransferase. Identification of cDNAs encoding two enzymes which glucuronidate testosterone, dihydrotestosterone, and b-estradiol, J. Biol. Chem. 262, 9744-9749.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9744-9749
    • Mackenzie, P.I.1
  • 11
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP-glucuronosyltransferase involved in substrate selection
    • Mackenzie, P. I. (1990) Expression of chimeric cDNAs in cell culture defines a region of UDP-glucuronosyltransferase involved in substrate selection, J. Biol. Chem. 265, 3432-3435.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3432-3435
    • Mackenzie, P.I.1
  • 12
    • 0033675536 scopus 로고    scopus 로고
    • Importance of histidine residues for the function of the human liver UDP-glucuronosyltransferase UGT1A6: Evidence for the catalytic role of histidine 370
    • Ouzzine, M., Antonio, L., Burchell, B., Netter, P., Fournel-Gigleux, S., and Magdalou, J. (2000) Importance of histidine residues for the function of the human liver UDP-glucuronosyltransferase UGT1A6: evidence for the catalytic role of histidine 370, Mol. Pharmacol. 58, 1609-1615.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1609-1615
    • Ouzzine, M.1    Antonio, L.2    Burchell, B.3    Netter, P.4    Fournel-Gigleux, S.5    Magdalou, J.6
  • 13
    • 0030889553 scopus 로고    scopus 로고
    • Arginine 52 and histidine 54 located in a conserved amino-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
    • Senay, C., Ouzzine, M., Battaglia, E., Pless, D., Cano, V., Burchell, B., Radominska, A., Magdalou, J., and Fournel-Gigleux, S. (1997) Arginine 52 and histidine 54 located in a conserved amino-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, 406-13.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 406-413
    • 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
  • 14
    • 0037310081 scopus 로고    scopus 로고
    • Opioids bind to the amino acids 84 to 118 of UDP-glucuronosyltransferase UGT2B7
    • Coffman, B. L., Kearney, W. R., Goldsmith, S., Knosp, B. M., and Tephly, T. R. (2003) Opioids bind to the amino acids 84 to 118 of UDP- glucuronosyltransferase UGT2B7, Mol. Pharmacol. 63, 283-8.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 283-288
    • Coffman, B.L.1    Kearney, W.R.2    Goldsmith, S.3    Knosp, B.M.4    Tephly, T.R.5
  • 15
    • 0031079999 scopus 로고    scopus 로고
    • Cloning and expression of solanidine UDP-glucose glucosyltransferase from potato
    • Moehs, C. P., Allen, P. V., Friedman, M., and Belknap, W. R. (1997) Cloning and expression of solanidine UDP-glucose glucosyltransferase from potato, Plant J. 11, 227-236.
    • (1997) Plant J. , vol.11 , pp. 227-236
    • Moehs, C.P.1    Allen, P.V.2    Friedman, M.3    Belknap, W.R.4
  • 16
    • 0034990314 scopus 로고    scopus 로고
    • Analysis of opiod binding to UDP-glucuronosyltransferase 2B7 fusion proteins using nuclear magnetic resonance spectroscopy
    • Coffman, B. L., Kearney, W. R., Green, M. D., Lowery, R. G., and Tephly, T. R. (2001) Analysis of opiod binding to UDP-glucuronosyltransferase 2B7 fusion proteins using nuclear magnetic resonance spectroscopy, Mol. Pharmacol. 59, 1464-1469.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1464-1469
    • Coffman, B.L.1    Kearney, W.R.2    Green, M.D.3    Lowery, R.G.4    Tephly, T.R.5
  • 17
    • 0030879658 scopus 로고    scopus 로고
    • A critical amino acid residue, asp446, in UDP-glucuronosyltransferase
    • Iwano, H., Yokota, H., Ohgiya, S., Yotumoto, N., and Yuasa, A. (1997) A critical amino acid residue, asp446, in UDP-glucuronosyltransferase, Biochem. J. 325, 587-591.
    • (1997) Biochem. J. , vol.325 , pp. 587-591
    • Iwano, H.1    Yokota, H.2    Ohgiya, S.3    Yotumoto, N.4    Yuasa, A.5
  • 18
    • 0033102535 scopus 로고    scopus 로고
    • The significance of amino acid residue Asp446 for enzymatic stability of rat UDP-glucuronosyltransferase UGT1A6
    • Iwano, H., Yokota, H., Ohgiya, S., and Yuasa, A. (1999) The significance of amino acid residue Asp446 for enzymatic stability of rat UDP- glucuronosyltransferase UGT1A6, Arch. Biochem. Biophys. 363, 116-20.
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 116-120
    • Iwano, H.1    Yokota, H.2    Ohgiya, S.3    Yuasa, A.4
  • 19
    • 0034718452 scopus 로고    scopus 로고
    • N-glycosylation and residue 96 are involved in the functional properties of UDP-glucuronosyltransferase enzymes
    • Barbier, O., Girard, C., Breton, R., Belanger, A., and Hum, D. W. (2000) N-glycosylation and residue 96 are involved in the functional properties of UDP-glucuronosyltransferase enzymes, Biochemistry 39, 11540-52.
    • (2000) Biochemistry , vol.39 , pp. 11540-11552
    • Barbier, O.1    Girard, C.2    Breton, R.3    Belanger, A.4    Hum, D.W.5
  • 20
    • 0031894377 scopus 로고    scopus 로고
    • The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268)
    • Coffman, B. L., King, C. D., Rios, G. R., and Tephly, T. R. (1998) The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268), Drug Metab. Dispos. 26, 73-77.
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 73-77
    • Coffman, B.L.1    King, C.D.2    Rios, G.R.3    Tephly, T.R.4
  • 21
    • 0033951038 scopus 로고    scopus 로고
    • Using photolabile ligands in drug discovery and development
    • Dorman, G., and Pestwich, G. D. (2000) Using photolabile ligands in drug discovery and development, Trends Biotechnol. 18, 64-77.
    • (2000) Trends Biotechnol. , vol.18 , pp. 64-77
    • Dorman, G.1    Pestwich, G.D.2
  • 22
    • 0032881708 scopus 로고    scopus 로고
    • Photoaffinity labeling probe for the substrate binding site of human phenol sulfotransferase (SULT1A1): 7-Azido-4-methylcoumarin
    • Chen, G., Battaglia, E., Senay, C., Falany, C. N., and Radominska-Pandya, A. (1999) Photoaffinity labeling probe for the substrate binding site of human phenol sulfotransferase (SULT1A1): 7-azido-4-methylcoumarin, Protein Sci. 8, 2151-7.
    • (1999) Protein Sci. , vol.8 , pp. 2151-2157
    • Chen, G.1    Battaglia, E.2    Senay, C.3    Falany, C.N.4    Radominska-Pandya, A.5
  • 24
    • 0034680357 scopus 로고    scopus 로고
    • Direct photoaffinity labeling of cellular retinoic acid-binding protein I (CRABP-I) with all-trans-retinoic acid: Identification of amino acids in the ligand binding site
    • Chen, G., and Radominska-Pandya, A. (2000) Direct photoaffinity labeling of cellular retinoic acid-binding protein I (CRABP-I) with all-trans-retinoic acid: identification of amino acids in the ligand binding site, Biochemistry 39, 12568-74.
    • (2000) Biochemistry , vol.39 , pp. 12568-12574
    • Chen, G.1    Radominska-Pandya, A.2
  • 25
    • 0035104033 scopus 로고    scopus 로고
    • Application of photoaffinity labeling with [(3)H] all trans- and 9-cis-retinoic acids for characterization of cellular retinoic acid-binding proteins I and II
    • Radominska-Pandya, A., Chen, G., Samokyszyn, V. M., Little, J. M., Gall, W. E., Zawada, G., Terrier, N., Magdalou, J., and Czernik, P. (2001) Application of photoaffinity labeling with [(3)H] all trans- and 9-cis-retinoic acids for characterization of cellular retinoic acid-binding proteins I and II, Protein Sci. 10, 200-11.
    • (2001) Protein Sci. , vol.10 , pp. 200-211
    • Radominska-Pandya, A.1    Chen, G.2    Samokyszyn, V.M.3    Little, J.M.4    Gall, W.E.5    Zawada, G.6    Terrier, N.7    Magdalou, J.8    Czernik, P.9
  • 26
    • 0034698126 scopus 로고    scopus 로고
    • Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy
    • Radominska-Pandya, A., Chen, G., Czernik, P. J., Little, J. M., Samokyszyn, V. M., Carter, C. A., and Nowak, G. (2000) Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy, J. Biol. Chem. 275, 22324-30.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22324-22330
    • Radominska-Pandya, A.1    Chen, G.2    Czernik, P.J.3    Little, J.M.4    Samokyszyn, V.M.5    Carter, C.A.6    Nowak, G.7
  • 27
    • 0037117716 scopus 로고    scopus 로고
    • Photoaffinity labeling of human retinoid X receptor beta (RXRbeta) with 9-cis-retinoic acid: Identification of phytanic acid, docosahexaenoic acid, and lithocholic acid as ligands for RXRbeta
    • Radominska-Pandya, A., and Chen, G. (2002) Photoaffinity labeling of human retinoid X receptor beta (RXRbeta) with 9-cis-retinoic acid: identification of phytanic acid, docosahexaenoic acid, and lithocholic acid as ligands for RXRbeta, Biochemistry 41, 4883-90.
    • (2002) Biochemistry , vol.41 , pp. 4883-4890
    • Radominska-Pandya, A.1    Chen, G.2
  • 28
    • 0033179447 scopus 로고    scopus 로고
    • Photoaffinity labeling of the aglycon binding site of the recombinant human liver UDP-glucuronosyltransferase UGT1A6 with 7-azido-4-methylcoumarin
    • Senay, C., Battaglia, E., Chen, G., Breton, R., Fournel-Gigleux, S., Magdalou, J., and Radominska-Pandya, A. (1999) Photoaffinity labeling of the aglycon binding site of the recombinant human liver UDP-glucuronosyltransferase UGT1A6 with 7-azido-4-methylcoumarin, Arch. Biochem. Biophys. 368, 75-84.
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 75-84
    • Senay, C.1    Battaglia, E.2    Chen, G.3    Breton, R.4    Fournel-Gigleux, S.5    Magdalou, J.6    Radominska-Pandya, A.7
  • 30
    • 0031584094 scopus 로고    scopus 로고
    • Application of photoaffinity labeling with [11,12-3H]all-trans-retinoic acid to characterization of rat liver microsomal UDP-glucuronosyltransferase(s) with activity toward retinoic acid
    • Little, J. M., and Radominska, A. (1997) Application of photoaffinity labeling with [11,12-3H]all-trans-retinoic acid to characterization of rat liver microsomal UDP-glucuronosyltransferase(s) with activity toward retinoic acid, Biochem. Biophys. Res. Commun. 230, 497-500.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 497-500
    • Little, J.M.1    Radominska, A.2
  • 31
    • 0030989680 scopus 로고    scopus 로고
    • Photoaffinity labeling studies of the human recombinant UDP-glucuronosyltransferase, UGT1*6, with 5-azido-UDP-glucuronic acid
    • Battaglia, E., Nowell, S., Drake, R. R., Magdalou, J., Fournel-Gigleux, S., Senay, C., and Radominska, A. (1997) Photoaffinity labeling studies of the human recombinant UDP-glucuronosyltransferase, UGT1*6, with 5-azido-UDP-glucuronic acid, Drug Metab. Dispos. 25, 406-11.
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 406-411
    • Battaglia, E.1    Nowell, S.2    Drake, R.R.3    Magdalou, J.4    Fournel-Gigleux, S.5    Senay, C.6    Radominska, A.7
  • 32
    • 0028349889 scopus 로고
    • Photoaffinity labeling for evaluation of uridinyl analogues as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases
    • Radominska, A., Paul, P., Treat, S., Towbin, H., Pratt, C., Little, J., Magdalou, J., Lester, R., and Drake, R. (1994) Photoaffinity labeling for evaluation of uridinyl analogues as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases, Biochim. Biophys. Acta 1205, 336-45.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 336-345
    • 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.9
  • 35
    • 0026327990 scopus 로고
    • Synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins
    • Drake, R. R., Zimniak, P., Haley, B. E., Lester, R., Elbein, A. D., and Radominska, A. (1991) Synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins, J. Biol. Chem. 266, 23257-60.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23257-23260
    • Drake, R.R.1    Zimniak, P.2    Haley, B.E.3    Lester, R.4    Elbein, A.D.5    Radominska, A.6
  • 36
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP- glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme
    • Kurkela, M., Garcia-Horsman, J. A., Luukkanen, L., Morsky, S., Taskinen, J., Baumann, M., Kostiainen, R., Hirvonen, J., and Finel, M. (2003) Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme, J. Biol. Chem. 278, 3536-44.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3536-3544
    • Kurkela, M.1    Garcia-Horsman, J.A.2    Luukkanen, L.3    Morsky, S.4    Taskinen, J.5    Baumann, M.6    Kostiainen, R.7    Hirvonen, J.8    Finel, M.9
  • 37
    • 0013588037 scopus 로고    scopus 로고
    • cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3
    • Mojarrabi, B., Butler, R., and Mackenzie, P. I. (1996) cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3, Biochem. Biophys. Res. Commun. 225, 785-790.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 785-790
    • Mojarrabi, B.1    Butler, R.2    Mackenzie, P.I.3
  • 38
    • 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
    • Strassburg, C. P., Oldhaffer, K., Manns, M. P., and Tukey, R. H. (1997) 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, 212-220.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 212-220
    • Strassburg, C.P.1    Oldhaffer, K.2    Manns, M.P.3    Tukey, R.H.4
  • 39
    • 0032502764 scopus 로고    scopus 로고
    • Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8
    • Strassburg, C. P., Manns, M. P., and Tukey, R. H. (1998) Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8, J. Biol. Chem. 273, 8719-26.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8719-8726
    • Strassburg, C.P.1    Manns, M.P.2    Tukey, R.H.3
  • 40
    • 0036204296 scopus 로고    scopus 로고
    • Glucuronidation: An important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues
    • Zheng, Z., Fang, J.-L., and Lazarus, P. (2002) glucuronidation: an important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues, Drug Metab. Dispos. 30, 397-403.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 397-403
    • Zheng, Z.1    Fang, J.-L.2    Lazarus, P.3
  • 42
    • 1842536798 scopus 로고    scopus 로고
    • Amino acid residue ILE211 is essential for the enzymatic activity of human UDP-glucuronosyltransferase 1A10 (UGT1A10)
    • Martineau, I., Tchernof, A., and Belanger, A. (2004) Amino acid residue ILE211 is essential for the enzymatic activity of human UDP- glucuronosyltransferase 1A10 (UGT1A10), Drug Metab. Dispos. 32, 455-459.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 455-459
    • Martineau, I.1    Tchernof, A.2    Belanger, A.3
  • 43
    • 1842536833 scopus 로고    scopus 로고
    • Human udp-glucuronosyltransferases: Isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • Uchaipichat, V., Mackenzie, P. I., Guo, X. H., Gardner-Stephen, D., Galetin, A., Houston, J. B., and Miners, J. O. (2004) Human udp- glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid, Drug Metab. Dispos. 32, 413-23.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6    Miners, J.O.7
  • 44
    • 3142652041 scopus 로고    scopus 로고
    • Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteridal antiinflammatory drugs, depends on phosphorylation
    • Basu, N. K., Kubota, S., Meselhy, M. R., Ciotti, M., Chowdhury, B., Hartori, M., and Owens, I. S. (2004) Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteridal antiinflammatory drugs, depends on phosphorylation, J. Biol. Chem. 279, 28320-28329.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28320-28329
    • Basu, N.K.1    Kubota, S.2    Meselhy, M.R.3    Ciotti, M.4    Chowdhury, B.5    Hartori, M.6    Owens, I.S.7
  • 45
    • 20044388593 scopus 로고    scopus 로고
    • Glucuronidation of bioflavonoids by human UGT1A10: Structure-function relationships
    • Lewinsky, R. H., Smith, P. A., and Mackenzie, P. I. (2005) Glucuronidation of bioflavonoids by human UGT1A10: structure-function relationships, Xenobiotica 35, 117-129.
    • (2005) Xenobiotica , vol.35 , pp. 117-129
    • Lewinsky, R.H.1    Smith, P.A.2    Mackenzie, P.I.3
  • 46
    • 4644315738 scopus 로고    scopus 로고
    • Glucuronidation of oxidized fatty acids and prostaglandins B1 and E2 by human hepatic and recombinant UDP-glucuronosyltransferases
    • Little, J. M., Kurkela, M., Sonka, J., Jantti, S., Ketola, R., Bratton, S., Finel, M., and Radominska-Pandya, A. (2004) Glucuronidation of oxidized fatty acids and prostaglandins B1 and E2 by human hepatic and recombinant UDP-glucuronosyltransferases, J. Lipid Res. 45, 1694-703.
    • (2004) J. Lipid Res. , vol.45 , pp. 1694-1703
    • Little, J.M.1    Kurkela, M.2    Sonka, J.3    Jantti, S.4    Ketola, R.5    Bratton, S.6    Finel, M.7    Radominska-Pandya, A.8
  • 47
    • 0042071532 scopus 로고    scopus 로고
    • Detection of UGT1A10 polymorphisms and their association with orolaryngeal carcinoma risk
    • Elahi, A., Bendaly, J., Zheng, Z., Muscat, J. E., Richie, J. P., Jr., Schantz, S. P., and Lazarus, P. (2003) Detection of UGT1A10 polymorphisms and their association with orolaryngeal carcinoma risk, Cancer 98, 872-80.
    • (2003) Cancer , vol.98 , pp. 872-880
    • Elahi, A.1    Bendaly, J.2    Zheng, Z.3    Muscat, J.E.4    Richie Jr., J.P.5    Schantz, S.P.6    Lazarus, P.7
  • 48
    • 0031590285 scopus 로고    scopus 로고
    • The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid
    • Mojarrabi, B., and Mackenzie, P. I. (1997) The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid, Biochem. Biophys. Res. Commun. 238, 775-778.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 775-778
    • Mojarrabi, B.1    Mackenzie, P.I.2
  • 49
    • 0032864111 scopus 로고    scopus 로고
    • Studies on the substrate specificity of human intestinal UDP-lucuronosyltransferases 1A8 and 1A10
    • Cheng, Z., Radominska-Pandya, A., and Tephly, T. R. (1999) Studies on the substrate specificity of human intestinal UDP-lucuronosyltransferases 1A8 and 1A10, Drug Metab. Dispos. 27, 1165-70.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 1165-1170
    • Cheng, Z.1    Radominska-Pandya, A.2    Tephly, T.R.3
  • 50
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression and disease
    • Tukey, R. H., and Strassburg, C. P. (2000) Human UDP- glucuronosyltransferases: metabolism, expression and disease, Annu. Rev. Pharmacol. Toxicol. 40, 581-616.
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 52
    • 0041856580 scopus 로고    scopus 로고
    • Glucuronidation of anabolic androgenic steroids by recombinant human UDP-glucuronosyltransferases
    • Kuuranne, T., Kurkela, M., Thevis, M., Schanzer, W., Finel, M., and Kostiainen, R. (2003) Glucuronidation of anabolic androgenic steroids by recombinant human UDP-glucuronosyltransferases, Drug Metab. Dispos. 31, 1117-24.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1117-1124
    • Kuuranne, T.1    Kurkela, M.2    Thevis, M.3    Schanzer, W.4    Finel, M.5    Kostiainen, R.6
  • 55
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence database using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence database using mass spectrometry data, Electrophoresis 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 56
    • 8844283291 scopus 로고    scopus 로고
    • The interactions between the N-terminal and C-terminal domains of the human UDP-glucuronosyltransferases are partly isoform-specific, and may involve both monomers
    • Kurkela, M., Hirvonen, J., Kostiainen, R., and Finel, M. (2004) The interactions between the N-terminal and C-terminal domains of the human UDP-glucuronosyltransferases are partly isoform-specific, and may involve both monomers, Biochem. Pharmacol. 68, 2443-50.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 2443-2450
    • Kurkela, M.1    Hirvonen, J.2    Kostiainen, R.3    Finel, M.4
  • 57
    • 6344248683 scopus 로고    scopus 로고
    • Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphospho-glucuronosyltransferases expressed in endometrium
    • Lepine, J., Bernard, O., Plante, M., Têtu, B., Pelletier, G., Labrie, F., and Bêlanger, A. (2004) Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphospho-glucuronosyltransferases expressed in endometrium, J. Clin. Endocrinol. Metab. 89, 5222-5232.
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 5222-5232
    • Lepine, J.1    Bernard, O.2    Plante, M.3    Têtu, B.4    Pelletier, G.5    Labrie, F.6    Bêlanger, A.7
  • 58
    • 0031866592 scopus 로고    scopus 로고
    • Photoaffinity labeling as an approach to study supramolecular nucleoprotein complexes
    • Knorre, D. G., and Godovikova, T. S. (1998) Photoaffinity labeling as an approach to study supramolecular nucleoprotein complexes, FEBS Lett. 433, 9-14.
    • (1998) FEBS Lett. , vol.433 , pp. 9-14
    • Knorre, D.G.1    Godovikova, T.S.2
  • 59
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano, J. K., Hsu, M. H., Griffin, K. J., Stout, C. D., and Johnson, E. F. (2005) Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen, Nat. Struct. Mol. Biol. 12, 822-3.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 822-823
    • Yano, J.K.1    Hsu, M.H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5


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