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Volumn 45, Issue 4, 2013, Pages 401-414

Interactions of cytosolic sulfotransferases with xenobiotics

Author keywords

Dietary sulfotransferase inhibitors; Enhancement of sulfonation; Inhibition of sulfotransferases

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; CELECOXIB; FLAVONOID; ISOENZYME; KYNURENIC ACID; SULFOTRANSFERASE; SULFOTRANSFERASE 1A1; SULFOTRANSFERASE 1A3; SULFOTRANSFERASE 1B1; SULFOTRANSFERASE 1E1; SULFOTRANSFERASE 2A1; TRANSFERASE; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 84887361225     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.3109/03602532.2013.835613     Document Type: Review
Times cited : (96)

References (117)
  • 1
    • 79952068588 scopus 로고    scopus 로고
    • Liquorice and glycyrrhetinic acid increase DHEA and deoxycorticosterone levels in vivo and in vitro by inhibiting adrenal SULT2A1 activity
    • Al-Dujaili EA, Kenyon CJ, Nicol MR, Mason JI. (2011). Liquorice and glycyrrhetinic acid increase DHEA and deoxycorticosterone levels in vivo and in vitro by inhibiting adrenal SULT2A1 activity. Mol Cell Endocrinol 336:102-109.
    • (2011) Mol Cell Endocrinol , vol.336 , pp. 102-109
    • Al-Dujaili, E.A.1    Kenyon, C.J.2    Nicol, M.R.3    Mason, J.I.4
  • 2
    • 33750976355 scopus 로고    scopus 로고
    • Triclosan in plasma and milk from Swedish nursing mothers and their exposure via personal care products
    • DOI 10.1016/j.scitotenv.2006.08.007, PII S0048969706006267
    • Allmyr M, Adolfsson-Erici M, Mclachlan MS, Sandborgh-Englund G. (2006). Triclosan in plasma and milk from Swedish nursing mothers and their exposure via personal care products. Sci Total Environ 372: 87-93. (Pubitemid 44751071)
    • (2006) Science of the Total Environment , vol.372 , Issue.1 , pp. 87-93
    • Allmyr, M.1    Adolfsson-Erici, M.2    McLachlan, M.S.3    Sandborgh-Englund, G.4
  • 3
    • 70350003592 scopus 로고    scopus 로고
    • Human exposure to triclosan via toothpaste does not change CYP3A4 activity or plasma concentrations of thyroid hormones
    • Allmyr M, Panagiotidis G, Sparve E, et al. (2009). Human exposure to triclosan via toothpaste does not change CYP3A4 activity or plasma concentrations of thyroid hormones. Basic Clin Pharmacol Toxicol 105:339-344.
    • (2009) Basic Clin Pharmacol Toxicol , vol.105 , pp. 339-344
    • Allmyr, M.1    Panagiotidis, G.2    Sparve, E.3
  • 5
    • 0032549060 scopus 로고    scopus 로고
    • Sulfation of minoxidil by multiple human cytosolic sulfotransferases
    • DOI 10.1016/S0009-2797(97)00120-8, PII S0009279797001208
    • Anderson RJ, Kudlacek PE, Clemens DL. (1998). Sulfation of minoxidil by multiple human cytosolic sulfotransferases. Chem Biol Interact 109:53-67. (Pubitemid 28161101)
    • (1998) Chemico-Biological Interactions , vol.109 , Issue.1-3 , pp. 53-67
    • Anderson, R.J.1    Kudlacek, P.E.2    Clemens, D.L.3
  • 6
    • 0033608416 scopus 로고    scopus 로고
    • Dietary heterocyclic amines and cancer of the colon, rectum, bladder, and kidney: A population-based study
    • DOI 10.1016/S0140-6736(98)06099-1
    • Augustsson K, Skog K, Jagerstad M, et al. (1999). Dietary heterocyclic amines and cancer of the colon, rectum, bladder, and kidney: A population-based study. Lancet 353:703-707. (Pubitemid 29103803)
    • (1999) Lancet , vol.353 , Issue.9154 , pp. 703-707
    • Augustsson, K.1    Skog, K.2    Jagerstad, M.3    Dickman, P.W.4    Steineck, G.5
  • 7
    • 0026729330 scopus 로고
    • Inhibition of human liver steroid sulfotransferase activities by drugs: A novel mechanism of drug toxicity
    • Bamforth KJ, Dalgliesh K, Coughtrie MW. (1992). Inhibition of human liver steroid sulfotransferase activities by drugs: A novel mechanism of drug toxicity Eur J Pharmacol 228:15-21.
    • (1992) Eur J Pharmacol , vol.228 , pp. 15-21
    • Bamforth, K.J.1    Dalgliesh, K.2    Coughtrie, M.W.3
  • 8
    • 0027494035 scopus 로고
    • Common food additives are potent inhibitors of human liver 17α-ethinyloestradiol and dopamine sulphotransferases
    • DOI 10.1016/0006-2952(93)90575-H
    • Bamforth KJ, Jones AL, Roberts RC, Coughtrie MW. (1993). Common food additives are potent inhibitors of human liver 17 alphaethinyloestradiol and dopamine sulphotransferases. Biochem Pharmacol 46:1713-1720. (Pubitemid 23349018)
    • (1993) Biochemical Pharmacology , vol.46 , Issue.10 , pp. 1713-1720
    • Bamforth, K.J.1    Jones, A.L.2    Roberts, R.C.3    Coughtrie, M.W.H.4
  • 9
    • 80055109953 scopus 로고    scopus 로고
    • The molecular basis for the broad substrate specificity of human sulfotransferase 1A1
    • Berger I, Guttman C, Amar D, et al. (2011). The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. PLoS One 6:e26794.
    • (2011) PLoS One , vol.6
    • Berger, I.1    Guttman, C.2    Amar, D.3
  • 11
    • 67849103759 scopus 로고    scopus 로고
    • IC50-to-Ki: A web-based tool for converting IC50 to Ki values for inhibitors of enzyme activity and ligand binding
    • Cer RZ, Mudunuri U, Stephens R, Lebeda FJ. (2009). IC50-to-Ki: A web-based tool for converting IC50 to Ki values for inhibitors of enzyme activity and ligand binding. Nucleic Acids Res 37:W441-5.
    • (2009) Nucleic Acids Res , vol.37
    • Cer, R.Z.1    Mudunuri, U.2    Stephens, R.3    Lebeda, F.J.4
  • 15
    • 0027051110 scopus 로고
    • Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal
    • Comer KA, Falany CN. (1992). Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal. Mol Pharmacol 41:645-651. (Pubitemid 23021450)
    • (1992) Molecular Pharmacology , vol.41 , Issue.4 , pp. 645-651
    • Comer, K.A.1    Falany, C.N.2
  • 17
    • 0035056401 scopus 로고    scopus 로고
    • Interactions between dietary chemicals and human sulfotransferases - Molecular mechanisms and clinical significance
    • Coughtrie MW, Johnston LE. (2001). Interactions between dietary chemicals and human sulfotransferases-molecular mechanisms and clinical significance. Drug Metab Dispos 29:522-528. (Pubitemid 32275528)
    • (2001) Drug Metabolism and Disposition , vol.29 , Issue.II4 , pp. 522-528
    • Coughtrie, M.W.H.1    Johnston, L.E.2
  • 18
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases
    • DOI 10.1016/S0009-2797(97)00117-8, PII S0009279797001178
    • Coughtrie MW, Sharp S, Maxwell K, Innes NP. (1998). Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem Biol Interact 109:3-27. (Pubitemid 28161098)
    • (1998) Chemico-Biological Interactions , vol.109 , Issue.1-3 , pp. 3-27
    • Coughtrie, M.W.H.1    Sharp, S.2    Maxwell, K.3    Innes, N.P.4
  • 19
    • 40349101820 scopus 로고    scopus 로고
    • Thyroid disrupting chemicals: Mechanisms and mixtures
    • DOI 10.1111/j.1365-2605.2007.00857.x
    • Crofton KM. (2008). Thyroid disrupting chemicals: Mechanisms and mixtures. Int J Androl 31:209-222. (Pubitemid 351341380)
    • (2008) International Journal of Andrology , vol.31 , Issue.2 , pp. 209-222
    • Crofton, K.M.1
  • 20
    • 6944222745 scopus 로고    scopus 로고
    • Heterotropic modulation of sulfotransferase 2A1 activity by celecoxib: Product ratio switching of ethynylestradiol sulfation
    • DOI 10.1124/dmd.32.11.
    • Cui D, Booth-Genthe CL, Carlini E, et al. (2004). Heterotropic modulation of sulfotransferase 2A1 activity by celecoxib: Product ratio switching of ethynylestradiol sulfation. Drug Metab Dispos 32: 1260-1264. (Pubitemid 39410910)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.11 , pp. 1260-1264
    • Cui, D.1    Booth-Genthe, C.L.2    Carlini, E.3    Carr, B.4    Schrag, M.L.5
  • 22
    • 0032437886 scopus 로고    scopus 로고
    • A single amino acid, Glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3
    • Dajani R, Hood AM, Coughtrie MWH. (1998). A single amino acid, Glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3. Mol Pharmacol 54:942-948. (Pubitemid 29002035)
    • (1998) Molecular Pharmacology , vol.54 , Issue.6 , pp. 942-948
    • Dajani, R.1    Hood, A.M.2    Coughtrie, M.W.H.3
  • 23
    • 0036269922 scopus 로고    scopus 로고
    • Inhibition of phenol sulfotransferase (SULT1A1) by quercetin in human adult and foetal livers
    • DOI 10.1080/00498250110119108
    • De Santi C, Pietrabissa A, Mosca F, et al. (2002). Inhibition of phenol sulfotransferase (SULT1A1) by quercetin in human adult and foetal livers. Xenobiotica 32:363-368. (Pubitemid 34620942)
    • (2002) Xenobiotica , vol.32 , Issue.5 , pp. 363-368
    • De Santi, C.1    Pietrabissa, A.2    Mosca, F.3    Rane, A.4    Pacifici, G.M.5
  • 24
    • 0033777342 scopus 로고    scopus 로고
    • Sulphation of resveratrol, a natural compound present in wine, and its inhibition by natural flavonoids
    • De Santi C, Pietrabissa A, Spisni R, et al. (2000). Sulphation of resveratrol, a natural compound present in wine, and its inhibition by natural flavonoids. Xenobiotica 30:857-866.
    • (2000) Xenobiotica , vol.30 , pp. 857-866
    • De Santi, C.1    Pietrabissa, A.2    Spisni, R.3
  • 25
    • 84879465621 scopus 로고    scopus 로고
    • Biomarkers of human exposure to personal care products: Results from the Flemish Environment and Health Study (FLEHS 2007-2011)
    • Den Hond E, Paulussen M, Geens T, et al. (2013). Biomarkers of human exposure to personal care products: Results from the Flemish Environment and Health Study (FLEHS 2007-2011). Sci Total Environ 463-464C:102-110.
    • (2013) Sci Total Environ , vol.463-464 , Issue.C , pp. 102-110
    • Den Hond, E.1    Paulussen, M.2    Geens, T.3
  • 26
    • 84859763830 scopus 로고    scopus 로고
    • Association of dietary quercetin with reduced risk of proximal colon cancer
    • Djuric Z, Severson RK, Kato I. (2012). Association of dietary quercetin with reduced risk of proximal colon cancer. Nutr Cancer 64:351-360.
    • (2012) Nutr Cancer , vol.64 , pp. 351-360
    • Djuric, Z.1    Severson, R.K.2    Kato, I.3
  • 28
    • 84865837155 scopus 로고    scopus 로고
    • SULT1A inhibition and how a migraine stops
    • Eagle K. (2012a). SULT1A inhibition and how a migraine stops. Headache 52:1321.
    • (2012) Headache , vol.52 , pp. 1321
    • Eagle, K.1
  • 29
    • 84861456557 scopus 로고    scopus 로고
    • Toxicological effects of red wine, orange juice, and other dietary SULT1A inhibitors via excess catecholamines
    • Eagle K. (2012b). Toxicological effects of red wine, orange juice, and other dietary SULT1A inhibitors via excess catecholamines. Food Chem Toxicol 50:2243-2249.
    • (2012) Food Chem Toxicol , vol.50 , pp. 2243-2249
    • Eagle, K.1
  • 30
    • 0030022005 scopus 로고    scopus 로고
    • Flavonoids, potent inhibitors of the human P-form phenolsulfotransferase: Potential role in drug metabolism and chemoprevention
    • Eaton EA, Walle UK, Lewis AJ, et al. (1996). Flavonoids, potent inhibitors of the human P-form phenolsulfotransferase. Potential role in drug metabolism and chemoprevention. Drug Metab Dispos 24: 232-237. (Pubitemid 26063910)
    • (1996) Drug Metabolism and Disposition , vol.24 , Issue.2 , pp. 232-237
    • Eaton, E.A.1    Walle, U.K.2    Lewis, A.J.3    Hudson, T.4    Wilson, A.A.5    Walle, T.6
  • 32
    • 80054762464 scopus 로고    scopus 로고
    • Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1
    • Ekuase EJ, Liu Y, Lehmler HJ, et al. (2011). Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1. Chem Res Toxicol 24: 1720-1728.
    • (2011) Chem Res Toxicol , vol.24 , pp. 1720-1728
    • Ekuase, E.J.1    Liu, Y.2    Lehmler, H.J.3
  • 33
    • 0025869349 scopus 로고
    • Molecular enzymology of human liver cytosolic sulfotransferases
    • Falany CN. (1991). Molecular enzymology of human liver cytosolic sulfotransferases. Trends Pharmacol Sci 12:255-259.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 255-259
    • Falany, C.N.1
  • 34
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany CN. (1997). Enzymology of human cytosolic sulfotransferases.FASEB J 11:206-216. (Pubitemid 27118321)
    • (1997) FASEB Journal , vol.11 , Issue.4 , pp. 206-216
    • Falany, C.N.1
  • 35
    • 37549003662 scopus 로고    scopus 로고
    • Effect of resveratrol on 17beta-estradiol sulfation by human hepatic and jejunal S9 and recombinant sulfotransferase 1E1
    • Furimsky AM, Green CE, Sharp LE, et al. (2008). Effect of resveratrol on 17beta-estradiol sulfation by human hepatic and jejunal S9 and recombinant sulfotransferase 1E1. Drug Metab Dispos 36: 129-136.
    • (2008) Drug Metab Dispos , vol.36 , pp. 129-136
    • Furimsky, A.M.1    Green, C.E.2    Sharp, L.E.3
  • 36
    • 29244470499 scopus 로고    scopus 로고
    • The structure of human SULT1A1 crystallized with estradiol: An insight into active site plasticity and substrate inhibition with multi-ring substrates
    • DOI 10.1074/jbc.M508289200
    • Gamage NU, Tsvetanov S, Duggleby RG, et al. (2005). The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem 280:41482-41486. (Pubitemid 41832208)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41482-41486
    • Gamage, N.U.1    Tsvetanov, S.2    Duggleby, R.G.3    McManus, M.E.4    Martin, J.L.5
  • 37
    • 0023224612 scopus 로고
    • In vitro inhibition of phenolsulphotransferase by food and drink constituents
    • DOI 10.1016/0006-2952(87)90598-3
    • Gibb C, Glover V, Sandler M. (1987). In vitro inhibition of phenolsulphotransferase by food and drink constituents. Biochem Pharmacol 36:2325-2330. (Pubitemid 17097408)
    • (1987) Biochemical Pharmacology , vol.36 , Issue.14 , pp. 2325-2330
    • Gibb, C.1    Glover, V.2    Sandler, M.3
  • 39
    • 30144435525 scopus 로고    scopus 로고
    • Activation and inactivation of carcinogens and mutagens by human sulfotransferases
    • Pacifici GM, Coughtrie MWH Boca Raton, Taylor and Francis
    • Glatt H. (2005). Activation and inactivation of carcinogens and mutagens by human sulfotransferases. In: Pacifici GM, Coughtrie MWH, eds. Human Cytosolic Sulfotransferases. Boca Raton, Taylor and Francis.
    • (2005) Human Cytosolic Sulfotransferases
    • Glatt, H.1
  • 42
    • 0031899371 scopus 로고    scopus 로고
    • Inhibition of phenolsulphotransferase by salicylic acid: A possible mechanism by which aspirin may reduce carcinogenesis
    • Harris RM, Hawker RJ, Langman MJ, et al. (1998). Inhibition of phenolsulphotransferase by salicylic acid: A possible mechanism by which aspirin may reduce carcinogenesis. Gut 42:272-275. (Pubitemid 28212184)
    • (1998) Gut , vol.42 , Issue.2 , pp. 272-275
    • Harris, R.M.1    Hawker, R.J.2    Langman, M.J.S.3    Singh, S.4    Waring, R.H.5
  • 43
    • 27744599111 scopus 로고    scopus 로고
    • Non-genomic effects of endocrine disrupters: Inhibition of estrogen sulfotransferase by phenols and chlorinated phenols
    • DOI 10.1016/j.mce.2005.05.013, PII S0303720705003114, Endocrine Mimicry and Disruption: Plasticisers and other Environmental Chemicals
    • Harris RM, Kirk CJ, Waring RH. (2005). Non-genomic effects of endocrine disrupters: Inhibition of estrogen sulfotransferase by phenols and chlorinated phenols. Mol Cell Endocrinol 244:72-74. (Pubitemid 41628231)
    • (2005) Molecular and Cellular Endocrinology , vol.244 , Issue.1-2 , pp. 72-74
    • Harris, R.M.1    Kirk, C.J.2    Waring, R.H.3
  • 44
    • 45249123185 scopus 로고    scopus 로고
    • Sulfotransferase inhibition: Potential impact of diet and environmental chemicals on steroid metabolism and drug detoxification
    • DOI 10.2174/138920008784220637
    • Harris RM, Waring RH. (2008). Sulfotransferase inhibition: Potential impact of diet and environmental chemicals on steroid metabolism and drug detoxification. Curr Drug Metab 9:269-275. (Pubitemid 351836415)
    • (2008) Current Drug Metabolism , vol.9 , Issue.4 , pp. 269-275
    • Harris, R.M.1    Waring, R.H.2
  • 45
    • 0030469590 scopus 로고    scopus 로고
    • Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: Immunochemical characterization of individual variation
    • Her C, Szumlanski C, Aksoy IA, Weinshilboum RM. (1996). Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: Immunochemical characterization of individual variation.Drug Metab Dispos 24:1328-1335.
    • (1996) Drug Metab Dispos , vol.24 , pp. 1328-1335
    • Her, C.1    Szumlanski, C.2    Aksoy, I.A.3    Weinshilboum, R.M.4
  • 46
    • 0024340713 scopus 로고
    • Immunological characterization of human phenol sulfotransferase
    • Heroux JA, Falany CN, Roth JA. (1989). Immunological characterization of human phenol sulfotransferase. Mol Pharmacol 36:29-33. (Pubitemid 19191255)
    • (1989) Molecular Pharmacology , vol.36 , Issue.1 , pp. 29-33
    • Heroux, J.A.1    Falany, C.N.2    Roth, J.A.3
  • 47
    • 41949089207 scopus 로고    scopus 로고
    • Consumption of Brussels sprouts protects peripheral human lymphocytes against 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) and oxidative DNAdamage: Results of a controlled human intervention trial
    • Hoelzl C, Glatt H, Meinl W, et al. (2008). Consumption of Brussels sprouts protects peripheral human lymphocytes against 2-amino-1-methyl-6- phenylimidazo[4,5-b]pyridine (PhIP) and oxidative DNAdamage: Results of a controlled human intervention trial. Mol Nutr Food Res 52:330-341.
    • (2008) Mol Nutr Food Res , vol.52 , pp. 330-341
    • Hoelzl, C.1    Glatt, H.2    Meinl, W.3
  • 48
    • 66149158179 scopus 로고    scopus 로고
    • Sulfation of dietary flavonoids by human sulfotransferases
    • Huang C, Chen Y, Zhou T, Chen G. (2009). Sulfation of dietary flavonoids by human sulfotransferases. Xenobiotica 39: 312-322.
    • (2009) Xenobiotica , vol.39 , pp. 312-322
    • Huang, C.1    Chen, Y.2    Zhou, T.3    Chen, G.4
  • 49
    • 77955865306 scopus 로고    scopus 로고
    • Triclosan is a potent inhibitor of estradiol and estrone sulfonation in sheep placenta
    • James MO, Li W, Summerlot DP, et al. (2010). Triclosan is a potent inhibitor of estradiol and estrone sulfonation in sheep placenta.Environ Int 36:942-949.
    • (2010) Environ Int , vol.36 , pp. 942-949
    • James, M.O.1    Li, W.2    Summerlot, D.P.3
  • 50
    • 0028808265 scopus 로고
    • Reduced platelet phenolsulphotransferase activity towards dopamine and 5-hydroxytryptamine in migraine
    • Jones AL, Roberts RC, Colvin DW, et al. (1995). Reduced platelet phenolsulphotransferase activity towards dopamine and 5-hydroxytryptamine in migraine. Eur J Clin Pharmacol 49:109-114.
    • (1995) Eur J Clin Pharmacol , vol.49 , pp. 109-114
    • Jones, A.L.1    Roberts, R.C.2    Colvin, D.W.3
  • 53
    • 33749449061 scopus 로고    scopus 로고
    • Inhibition of human phenol and estrogen sulfotransferase by certain non-steroidal anti-inflammatory agents
    • DOI 10.2174/138920006778520615
    • King RS, Ghosh AA, Wu J. (2006). Inhibition of human phenol and estrogen sulfotransferase by certain non-steroidal anti-inflammatory agents. Curr Drug Metab 7:745-753. (Pubitemid 44509680)
    • (2006) Current Drug Metabolism , vol.7 , Issue.7 , pp. 745-753
    • King, R.S.1    Ghosh, A.A.2    Wu, J.3
  • 54
    • 84865766898 scopus 로고    scopus 로고
    • Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases
    • Ko K, Kurogi K, Davidson G, et al. (2012). Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases. J Biochem 152: 275-283.
    • (2012) J Biochem , vol.152 , pp. 275-283
    • Ko, K.1    Kurogi, K.2    Davidson, G.3
  • 55
    • 84858258974 scopus 로고    scopus 로고
    • Standardized LC-MS/MS based steroid hormone profile-analysis
    • Koal T, Schmiederer D, Pham-Tuan H, et al. (2012). Standardized LC-MS/MS based steroid hormone profile-analysis. J Steroid Biochem Mol Biol 129:129-138.
    • (2012) J Steroid Biochem Mol Biol , vol.129 , pp. 129-138
    • Koal, T.1    Schmiederer, D.2    Pham-Tuan, H.3
  • 57
    • 33845276999 scopus 로고    scopus 로고
    • Hydroxylated polychlorinated biphenyls are substrates and inhibitors of human hydroxysteroid sulfotransferase SULT2A1
    • DOI 10.1021/tx060160+
    • Liu Y, Apak TI, Lehmler HJ, et al. (2006). Hydroxylated polychlorinated biphenyls are substrates and inhibitors of human hydroxysteroid sulfotransferase SULT2A1. Chem Res Toxicol 19:1420-1425. (Pubitemid 44863483)
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.11 , pp. 1420-1425
    • Liu, Y.1    Idil Apak, T.2    Lehmler, H.-J.3    Robertson, L.W.4    Duffel, M.W.5
  • 58
    • 79551541627 scopus 로고    scopus 로고
    • Physicochemical properties of hydroxylated polychlorinated biphenyls aid in predicting their interactions with rat sulfotransferase 1A1 (rSULT1A1)
    • Liu Y, Lehmler HJ, Robertson LW, Duffel MW. (2011). Physicochemical properties of hydroxylated polychlorinated biphenyls aid in predicting their interactions with rat sulfotransferase 1A1 (rSULT1A1). Chem Biol Interact 189:153-160.
    • (2011) Chem Biol Interact , vol.189 , pp. 153-160
    • Liu, Y.1    Lehmler, H.J.2    Robertson, L.W.3    Duffel, M.W.4
  • 59
    • 66449092829 scopus 로고    scopus 로고
    • Structure-activity relationships for hydroxylated polychlorinated biphenyls as substrates and inhibitors of rat sulfotransferases and modification of these relationships by changes in thiol status
    • Liu Y, Smart JT, Song Y, et al. (2009). Structure-activity relationships for hydroxylated polychlorinated biphenyls as substrates and inhibitors of rat sulfotransferases and modification of these relationships by changes in thiol status. Drug Metab Dispos 37:1065-1072.
    • (2009) Drug Metab Dispos , vol.37 , pp. 1065-1072
    • Liu, Y.1    Smart, J.T.2    Song, Y.3
  • 60
    • 0142212157 scopus 로고    scopus 로고
    • Solvent effect on cDNA-expressed human sulfotransferase (SULT) activities in vitro
    • DOI 10.1124/dmd.31.11.1300
    • Ma B, Shou M, Schrag ML. (2003). Solvent effect on cDNA-expressed human sulfotransferase (SULT) activities in vitro. Drug Metab Dispos 31:1300-1305. (Pubitemid 37310316)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.11 , pp. 1300-1305
    • Ma, B.1    Shou, M.2    Schrag, M.L.3
  • 61
    • 0035689972 scopus 로고    scopus 로고
    • Differential inhibition of human liver and duodenum sulphotransferase activities by quercetin, a flavonoid present in vegetables, fruit and wine
    • DOI 10.1080/00498250110069159
    • Marchetti F, De Santi C, Vietri M, et al. (2001). Differential inhibition of human liver and duodenum sulphotransferase activities by quercetin, a flavonoid present in vegetables, fruit and wine. Xenobiotica 31: 841-847. (Pubitemid 34074787)
    • (2001) Xenobiotica , vol.31 , Issue.12 , pp. 841-847
    • Marchetti, F.1    De Santi, C.2    Vietri, M.3    Pietrabissa, A.4    Spisni, R.5    Mosca, F.6    Pacifici, G.M.7
  • 62
    • 9144251959 scopus 로고    scopus 로고
    • Inhibition of rat liver sulfotransferases SULT1A1 and SULT2A1 and glucuronosyltransferase by dietary flavonoids
    • DOI 10.1080/00498250310001615762
    • Mesia-Vela S, Kauffman FC. (2003). Inhibition of rat liver sulfotransferases SULT1A1 and SULT2A1 and glucuronosyltransferase by dietary flavonoids. Xenobiotica 33:1211-1220. (Pubitemid 38122243)
    • (2003) Xenobiotica , vol.33 , Issue.12 , pp. 1211-1220
    • Mesia-Vela, S.1    Kauffman, F.C.2
  • 64
    • 76849101780 scopus 로고    scopus 로고
    • Expression of sulfotransferases and sulfatases in human breast cancer: Impact on resveratrol metabolism
    • Miksits M, Wlcek K, Svoboda M, et al. (2010). Expression of sulfotransferases and sulfatases in human breast cancer: Impact on resveratrol metabolism. Cancer Lett 289:237-245.
    • (2010) Cancer Lett , vol.289 , pp. 237-245
    • Miksits, M.1    Wlcek, K.2    Svoboda, M.3
  • 65
    • 0025316424 scopus 로고
    • Characterization of paracetamol UDP-glucuronosyltransferase activity in human liver microsomes
    • DOI 10.1016/0006-2952(90)90561-X
    • Miners JO, Lillywhite KJ, Yoovathaworn K, et al. (1990).Characterization of paracetamol UDP-glucuronosyltransferase activity in human liver-microsomes. Biochem Pharmacol 40:595-600. (Pubitemid 20241126)
    • (1990) Biochemical Pharmacology , vol.40 , Issue.3 , pp. 595-600
    • Miners, J.O.1    Lillywhite, K.J.2    Yoovathaworn, K.3    Pongmarutai, M.4    Birkett, D.J.5
  • 66
    • 16644374972 scopus 로고    scopus 로고
    • Inhibitory effect of flavonoids on sulfo- and glucurono-conjugation of acetaminophen in rat cultured hepatocytes and liver subcellular preparations
    • DOI 10.1248/bpb.27.714
    • Morimitsu Y, Sugihara N, Furuno K. (2004). Inhibitory effect of flavonoids on sulfo-and glucurono-conjugation of acetaminophen in rat cultured hepatocytes and liver subcellular preparations. Biol Pharm Bull 27:714-717. (Pubitemid 41694678)
    • (2004) Biological and Pharmaceutical Bulletin , vol.27 , Issue.5 , pp. 714-717
    • Morimitsu, Y.1    Sugihara, N.2    Furuno, K.3
  • 67
    • 59949090346 scopus 로고    scopus 로고
    • Inhibitory effects of herbal extracts on the activity of human sulfotransferase isoform sulfotransferase 1A3 (SULT1A3)
    • Nagai M, Fukamachi T, Tsujimoto M, et al. (2009). Inhibitory effects of herbal extracts on the activity of human sulfotransferase isoform sulfotransferase 1A3 (SULT1A3). Biol Pharm Bull 32:105-109.
    • (2009) Biol Pharm Bull , vol.32 , pp. 105-109
    • Nagai, M.1    Fukamachi, T.2    Tsujimoto, M.3
  • 68
    • 33745177369 scopus 로고    scopus 로고
    • Sulfotransferase (SULT) 1A1 polymorphic variants1,2, and3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation
    • DOI 10.1124/mol.105.019240
    • Nagar S, Walther S, Blanchard RL. (2006). Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation. Mol Pharmacol 69:2084-2092. (Pubitemid 43894328)
    • (2006) Molecular Pharmacology , vol.69 , Issue.6 , pp. 2084-2092
    • Nagar, S.1    Walther, S.2    Blanchard, R.L.3
  • 70
    • 23844543826 scopus 로고    scopus 로고
    • Inhibitory effects of various beverages on ritodrine sulfation by recombinant human sulfotransferase isoforms SULT1A1 and SULT1A3
    • DOI 10.1007/s11095-005-5263-y
    • Nishimuta H, Tsujimoto M, Ogura K, et al. (2005). Inhibitory effects of various beverages on ritodrine sulfation by recombinant human sulfotransferase isoforms SULT1A1 and SULT1A3. Pharm Res 22: 1406-1410. (Pubitemid 41176045)
    • (2005) Pharmaceutical Research , vol.22 , Issue.8 , pp. 1406-1410
    • Nishimuta, H.1    Tsujimoto, M.2    Ogura, K.3    Hiratsuka, A.4    Ohtani, H.5    Sawada, Y.6
  • 71
    • 0346024012 scopus 로고    scopus 로고
    • Characterization of a zebrafish estrogen-sulfating cytosolic sulfotransferase: Inhibitory effects and mechanism of action of phytoestrogens
    • DOI 10.1016/j.cbi.2003.09.001
    • Ohkimoto K, Liu MY, Suiko M, et al. (2004). Characterization of a zebrafish estrogen-sulfating cytosolic sulfotransferase: Inhibitory effects and mechanism of action of phytoestrogens. Chem Biol Interact 147:1-7. (Pubitemid 38076845)
    • (2004) Chemico-Biological Interactions , vol.147 , Issue.1 , pp. 1-7
    • Ohkimoto, K.1    Liu, M.-Y.2    Suiko, M.3    Sakakibara, Y.4    Liu, M.-C.5
  • 72
    • 0033750995 scopus 로고    scopus 로고
    • Quercetin and resveratrol potently reduce estrogen sulfotransferase activity in normal human mammary epithelial cells
    • Otake Y, Nolan AL, Walle UK, Walle T. (2000). Quercetin and resveratrol potently reduce estrogen sulfotransferase activity in normal human mammary epithelial cells. J Steroid Biochem Mol Biol 73: 265-270.
    • (2000) J Steroid Biochem Mol Biol , vol.73 , pp. 265-270
    • Otake, Y.1    Nolan, A.L.2    Walle, U.K.3    Walle, T.4
  • 73
    • 18044372636 scopus 로고    scopus 로고
    • Recent insight on the control of enzymes involved in estrogen formation and transformation in human breast cancer
    • DOI 10.1016/j.jsbmb.2005.02.007, Proceedings of the 16th Internatioanl Symposium of the Journal of Steroid Biochemistry and Molecular Biology
    • Pasqualini JR, Chetrite GS. (2005). Recent insight on the control of enzymes involved in estrogen formation and transformation in human breast cancer. J Steroid Biochem Mol Biol 93:221-236. (Pubitemid 40602495)
    • (2005) Journal of Steroid Biochemistry and Molecular Biology , vol.93 , Issue.2-5 , pp. 221-236
    • Pasqualini, J.R.1    Chetrite, G.S.2
  • 74
    • 0021257308 scopus 로고
    • Platelet monoamine oxidase and phenolsulphotransferase M and P in cancer
    • DOI 10.1016/0009-8981(84)90276-6
    • Rampling RP, Bonham Carter SM, Glover V, Sandler M. (1984). Platelet monoamine oxidase and phenolsulphotransferase M and P in cancer.Clin Chim Acta 139:303-312. (Pubitemid 14111449)
    • (1984) Clinica Chimica Acta , vol.139 , Issue.3 , pp. 303-312
    • Rampling, R.P.1    Bonham Carter, S.M.2    Glover, V.3    Sandler, M.4
  • 75
    • 0022446184 scopus 로고
    • Plasma free and conjugated catecholamines in clinical disorders
    • Ratge D, Knoll E, Wisser H. (1986). Plasma free and conjugated catecholamines in clinical disorders. Life Sci 39:557-564. (Pubitemid 16076233)
    • (1986) Life Sciences , vol.39 , Issue.4 , pp. 557-564
    • Ratge, D.1    Knoll, E.2    Wisser, H.3
  • 76
    • 0037093546 scopus 로고    scopus 로고
    • Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate
    • Rehse PH, Zhou M, Lin SX. (2002). Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate.Biochem J 364:165-171. (Pubitemid 34538959)
    • (2002) Biochemical Journal , vol.364 , Issue.1 , pp. 165-171
    • Rehse, P.H.1    Zhou, M.2    Lin, S.-X.3
  • 77
    • 58549104390 scopus 로고    scopus 로고
    • Simultaneous modelling of the Michaelis-Menten kinetics of paracetamol sulphation and glucuronidation
    • Reith D, Medlicott NJ, Kumara De Silva R, et al. (2009). Simultaneous modelling of the Michaelis-Menten kinetics of paracetamol sulphation and glucuronidation. Clin Exp Pharmacol Physiol 36:35-42.
    • (2009) Clin Exp Pharmacol Physiol , vol.36 , pp. 35-42
    • Reith, D.1    Medlicott, N.J.2    Kumara De Silva, R.3
  • 78
    • 0034967098 scopus 로고    scopus 로고
    • Sulfation of thyroid hormone and dopamine during human development: Ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain
    • DOI 10.1210/jc.86.6.2734
    • Richard K, Hume R, Kaptein E, et al. (2001). Sulfation of thyroid hormone and dopamine during human development: Ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain.J Clin Endocrinol Metab 86:2734-2742. (Pubitemid 32545731)
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , Issue.6 , pp. 2734-2742
    • Richard, K.1    Hume, R.2    Kaptein, E.3    Stanley, E.L.4    Visser, T.J.5    Coughtrie, M.W.H.6
  • 79
    • 70350319524 scopus 로고    scopus 로고
    • Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: The SULT pie
    • Riches Z, Stanley EL, Bloomer JC, Coughtrie MW. (2009). Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: The SULT "pie". Drug Metab Dispos 37:2255-2261.
    • (2009) Drug Metab Dispos , vol.37 , pp. 2255-2261
    • Riches, Z.1    Stanley, E.L.2    Bloomer, J.C.3    Coughtrie, M.W.4
  • 80
    • 84863889483 scopus 로고    scopus 로고
    • Potent inhibition of human sulfotransferase 1A1 by 17alpha- ethinylestradiol: Role of 30-phosphoadenosine 50-phosphosulfate binding and structural rearrangements in regulating inhibition and activity
    • Rohn KJ, Cook IT, Leyh TS, et al. (2012). Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: Role of 30-phosphoadenosine 50-phosphosulfate binding and structural rearrangements in regulating inhibition and activity. Drug Metab Dispos 40:1588-1595.
    • (2012) Drug Metab Dispos , vol.40 , pp. 1588-1595
    • Rohn, K.J.1    Cook, I.T.2    Leyh, T.S.3
  • 81
    • 84872742547 scopus 로고    scopus 로고
    • Regulation of the cytosolic sulfotransferases by nuclear receptors
    • Runge-Morris M, Kocarek TA, Falany CN. (2013). Regulation of the cytosolic sulfotransferases by nuclear receptors. Drug Metab Rev 45: 15-33.
    • (2013) Drug Metab Rev , vol.45 , pp. 15-33
    • Runge-Morris, M.1    Kocarek, T.A.2    Falany, C.N.3
  • 82
    • 0033842043 scopus 로고    scopus 로고
    • Analysis of hydroxylated metabolites of PCBs (OH-PCBs) and other chlorinated phenolic compounds in whole blood from Canadian Inuit
    • Sandau CD, Ayotte P, Dewailly E, et al. (2000). Analysis of hydroxylated metabolites of PCBs (OH-PCBs) and other chlorinated phenolic compounds in whole blood from Canadian inuit. Environ Health Perspect 108:611-616. (Pubitemid 30657866)
    • (2000) Environmental Health Perspectives , vol.108 , Issue.7 , pp. 611-616
    • Sandau, C.D.1    Ayotte, P.2    Dewailly, E.3    Duffe, J.4    Norstrom, R.J.5
  • 83
    • 0036230329 scopus 로고    scopus 로고
    • Pentachlorophenol and hydroxylated polychlorinated biphenyl metabolites in umbilical cord plasma of neonates from coastal populations in Québec
    • Sandau CD, Ayotte P, Dewailly E, et al. (2002). Pentachlorophenol and hydroxylated polychlorinated biphenyl metabolites in umbilical cord plasma of neonates from coastal populations in Quebec. Environ Health Perspect 110:411-417. (Pubitemid 34308606)
    • (2002) Environmental Health Perspectives , vol.110 , Issue.4 , pp. 411-417
    • Sandau, C.D.1    Ayotte, P.2    Dewailly, E.3    Duffe, J.4    Norstrom, R.J.5
  • 84
    • 57349144983 scopus 로고    scopus 로고
    • Pomegranate juice inhibits sulfoconjugation in Caco-2 human colon carcinoma cells
    • Saruwatari A, Okamura S, Nakajima Y, et al. (2008). Pomegranate juice inhibits sulfoconjugation in Caco-2 human colon carcinoma cells.J Med Food 11:623-628.
    • (2008) J Med Food , vol.11 , pp. 623-628
    • Saruwatari, A.1    Okamura, S.2    Nakajima, Y.3
  • 86
    • 0032865121 scopus 로고    scopus 로고
    • Effects of pentachlorophenol and hydroxylated polychlorinated biphenyls on thyroid hormone conjugation in a rat and a human hepatoma cell line
    • DOI 10.1016/S0887-2333(99)00005-3, PII S0887233399000053
    • Schuur AG, Bergman A, Brouwer A, Visser TJ. (1999). Effects of pentachlorophenol and hydroxylated polychlorinated biphenyls on thyroid hormone conjugation in a rat and a human hepatoma cell line.Toxicol in Vitro 13:417-425. (Pubitemid 29354226)
    • (1999) Toxicology in Vitro , vol.13 , Issue.3 , pp. 417-425
    • Schuur, A.G.1    Bergman, A.2    Brouwer, A.3    Visser, T.J.4
  • 89
    • 79952616759 scopus 로고    scopus 로고
    • Sulfation of the 3,4-methylenedioxymethamphetamine (MDMA) metabolites 3,4-dihydroxymethamphetamine (DHMA) and 4-hydroxy-3-methoxymethamphetamine (HMMA) and their capability to inhibit human sulfotransferases
    • Schwaninger AE, Meyer MR, Zapp J, Maurer HH. (2011). Sulfation of the 3,4-methylenedioxymethamphetamine (MDMA) metabolites 3,4- dihydroxymethamphetamine (DHMA) and 4-hydroxy-3-methoxymethamphetamine (HMMA) and their capability to inhibit human sulfotransferases. Toxicol Lett 202:120-128.
    • (2011) Toxicol Lett , vol.202 , pp. 120-128
    • Schwaninger, A.E.1    Meyer, M.R.2    Zapp, J.3    Maurer, H.H.4
  • 90
    • 70249095602 scopus 로고    scopus 로고
    • Inhibitory effects of kynurenic acid, a tryptophan metabolite, and its derivatives on cytosolic sulfotransferases
    • Senggunprai L, Yoshinari K, Yamazoe Y. (2009). Inhibitory effects of kynurenic acid, a tryptophan metabolite, and its derivatives on cytosolic sulfotransferases. Biochem J 422:455-462.
    • (2009) Biochem J , vol.422 , pp. 455-462
    • Senggunprai, L.1    Yoshinari, K.2    Yamazoe, Y.3
  • 91
    • 0037745545 scopus 로고    scopus 로고
    • Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase
    • Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M. (2003). Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect 111:884-888. (Pubitemid 36790381)
    • (2003) Environmental Health Perspectives , vol.111 , Issue.7 , pp. 884-888
    • Shevtsov, S.1    Petrochenko, E.V.2    Pedersen, L.C.3    Negishi, M.4
  • 92
    • 23644432067 scopus 로고    scopus 로고
    • Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification
    • DOI 10.1016/j.mce.2005.06.003, PII S0303720705002303
    • Stanley EL, Hume R, Coughtrie MW. (2005). Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification. Mol Cell Endocrinol 240: 32-42. (Pubitemid 41133369)
    • (2005) Molecular and Cellular Endocrinology , vol.240 , Issue.1-2 , pp. 32-42
    • Stanley, E.L.1    Hume, R.2    Coughtrie, M.W.H.3
  • 93
    • 0036796816 scopus 로고    scopus 로고
    • Sulfonation and molecular action
    • DOI 10.1210/er.2001-0040
    • Strott CA. (2002). Sulfonation and molecular action. Endocr Rev 23: 703-732. (Pubitemid 35203256)
    • (2002) Endocrine Reviews , vol.23 , Issue.5 , pp. 703-732
    • Strott, C.A.1
  • 94
    • 0027215866 scopus 로고
    • Chemoprevention of diethylnitrosamine-induced hepatocarcinogenesis by a simple phenolic acid protocatechuic acid in rats
    • Tanaka T, Kojima T, Kawamori T, et al. (1993). Chemoprevention of diethylnitrosamine-induced hepatocarcinogenesis by a simple phenolic acid protocatechuic acid in rats. Cancer Res 53:2775-2779. (Pubitemid 23180514)
    • (1993) Cancer Research , vol.53 , Issue.12 , pp. 2775-2779
    • Tanaka, T.1    Kojima, T.2    Kawamori, T.3    Yoshimi, N.4    Mori, H.5
  • 95
    • 34249799590 scopus 로고    scopus 로고
    • Identification and localization of soluble sulfotransferases in the human gastrointestinal tract
    • DOI 10.1042/BJ20061431
    • Teubner W, Meinl W, Florian S, et al. (2007). Identification and localization of soluble sulfotransferases in the human gastrointestinal tract. Biochem J 404:207-215. (Pubitemid 46849592)
    • (2007) Biochemical Journal , vol.404 , Issue.2 , pp. 207-215
    • Teubner, W.1    Meinl, W.2    Florian, S.3    Kretzschmar, M.4    Glatt, H.5
  • 97
    • 84855816521 scopus 로고    scopus 로고
    • Triclosan in individual human milk samples from Australi
    • Toms LM, Allmyr M, Mueller JF, et al. (2011). Triclosan in individual human milk samples from Australia. Chemosphere 85:1682-1686.
    • (2011) Chemosphere , vol.85 , pp. 1682-1686
    • Toms, L.M.1    Allmyr, M.2    Mueller, J.F.3
  • 98
    • 61649084453 scopus 로고    scopus 로고
    • Trans-resveratrol-mediated inhibition of betaoestradiol conjugation in MCF-7 cells stably expressing human sulfotransferases SULT1A1 or SULT1E1, and human liver microsomes
    • Ung D, Nagar S. (2009). Trans-resveratrol-mediated inhibition of betaoestradiol conjugation in MCF-7 cells stably expressing human sulfotransferases SULT1A1 or SULT1E1, and human liver microsomes.Xenobiotica 39:72-79.
    • (2009) Xenobiotica , vol.39 , pp. 72-79
    • Ung, D.1    Nagar, S.2
  • 99
    • 0034002230 scopus 로고    scopus 로고
    • Fenamates and the potent inhibition of human liver phenol sulphotransferase
    • Vietri M, De Santi C, Pietrabissa A, et al. (2000a). Fenamates and the potent inhibition of human liver phenol sulphotransferase.Xenobiotica 30:111-116. (Pubitemid 30125112)
    • (2000) Xenobiotica , vol.30 , Issue.2 , pp. 111-116
    • Vietri, M.1    De Santi, C.2    Pietrabissa, A.3    Mosca, F.4    Pacifici, G.M.5
  • 101
    • 0034939706 scopus 로고    scopus 로고
    • Human adult and foetal liver sulphotransferases: Inhibition by mefenamic acid and salicylic acid
    • DOI 10.1080/00498250110043481
    • Vietri M, Pietrabissa A, Mosca F, et al. (2001). Human adult and foetal liver sulphotransferases: Inhibition by mefenamic acid and salicylic acid. Xenobiotica 31:153-161. (Pubitemid 32635343)
    • (2001) Xenobiotica , vol.31 , Issue.3 , pp. 153-161
    • Vietri, M.1    Pietrabissa, A.2    Mosca, F.3    Rane, A.4    Pacifici, G.M.5
  • 102
    • 0033820716 scopus 로고    scopus 로고
    • Differential inhibition of hepatic and duodenal sulfation of ()-salbutamol and minoxidil by mefenamic acid
    • Vietri M, Pietrabissa A, Spisni R, et al. (2000c). Differential inhibition of hepatic and duodenal sulfation of (-)-salbutamol and minoxidil by mefenamic acid. Eur J Clin Pharmacol 56:477-479.
    • (2000) Eur J Clin Pharmacol , vol.56 , pp. 477-479
    • Vietri, M.1    Pietrabissa, A.2    Spisni, R.3
  • 103
    • 0036066850 scopus 로고    scopus 로고
    • Sulfation of R(-)-apomorphine in the human liver and duodenum, and its inhibition by mefenamic acid, salicylic acid and quercetin
    • Vietri M, Vaglini F, Pietrabissa A, et al. (2002). Sulfation of R(-)-apomorphine in the human liver and duodenum, and its inhibition by mefenamic acid, salicylic acid and quercetin.Xenobiotica 32:587-594.
    • (2002) Xenobiotica , vol.32 , pp. 587-594
    • Vietri, M.1    Vaglini, F.2    Pietrabissa, A.3
  • 104
    • 0029092127 scopus 로고
    • Quercetin, a potent and specific inhibitor of the human P-form phenosulfotransferase
    • Walle T, Eaton EA, Walle UK. (1995). Quercetin, a potent and specific inhibitor of the human P-form phenosulfotransferase. Biochem Pharmacol 50:731-734.
    • (1995) Biochem Pharmacol , vol.50 , pp. 731-734
    • Walle, T.1    Eaton, E.A.2    Walle, U.K.3
  • 105
    • 4644322855 scopus 로고    scopus 로고
    • Triclosan as a substrate and inhibitor of 3′-phosphoadenosine 5′-phosphosulfate-sulfotransferase and UDP-glucuronosyl transferase in human liver fractions
    • DOI 10.1124/dmd.104.000273
    • Wang LQ, Falany CN, James MO. (2004). Triclosan as a substrate and inhibitor of 30-phosphoadenosine 50-phosphosulfate-sulfotransferase and UDP-glucuronosyl transferase in human liver fractions. Drug Metab Dispos 32:1162-1169. (Pubitemid 39287591)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.10 , pp. 1162-1169
    • Wang, L.-Q.1    Falany, C.N.2    James, M.O.3
  • 106
    • 25644456179 scopus 로고    scopus 로고
    • Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate
    • DOI 10.1016/j.jsbmb.2005.05.002, PII S0960076005002116
    • Wang LQ, James MO. (2005). Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate. J Steroid Biochem Mol Biol 96: 367-374. (Pubitemid 41384138)
    • (2005) Journal of Steroid Biochemistry and Molecular Biology , vol.96 , Issue.5 , pp. 367-374
    • Wang, L.-Q.1    James, M.O.2
  • 107
    • 30944444047 scopus 로고    scopus 로고
    • Inhibition of sulfotransferases by xenobiotics
    • Wang LQ, James MO. (2006). Inhibition of sulfotransferases by xenobiotics. Curr Drug Metab 7:83-104.
    • (2006) Curr Drug Metab , vol.7 , pp. 83-104
    • Wang, L.Q.1    James, M.O.2
  • 108
    • 20844446830 scopus 로고    scopus 로고
    • In vitro inhibition of human hepatic and cDNA-expressed sulfotransferase activity with 3-hydroxybenzo[a]pyrene by polychlorobiphenylols
    • DOI 10.1289/ehp.7837
    • Wang LQ, Lehmler HJ, Robertson LW, et al. (2005). In vitro inhibition of human hepatic and cDNA-expressed sulfotransferase activity with 3-hydroxybenzo[a]pyrene by polychlorobiphenylols. Environ Health Perspect 113:680-687. (Pubitemid 40862178)
    • (2005) Environmental Health Perspectives , vol.113 , Issue.6 , pp. 680-687
    • Wang, L.-Q.1    Lehmler, H.-J.2    Robertson, L.W.3    Falany, C.N.4    James, M.O.5
  • 109
    • 30944434189 scopus 로고    scopus 로고
    • Polychlorobiphenylols are selective inhibitors of human phenol sulfotransferase 1A1 with 4-nitrophenol as a substrate
    • DOI 10.1016/j.cbi.2005.12.004, PII S0009279705004230
    • Wang LQ, Lehmler HJ, Robertson LW, James MO. (2006).Polychlorobiphenylols are selective inhibitors of human phenol sulfotransferase 1A1 with 4-nitrophenol as a substrate. Chem Biol Interact 159:235-246. (Pubitemid 43112434)
    • (2006) Chemico-Biological Interactions , vol.159 , Issue.3 , pp. 235-246
    • Wang, L.-Q.1    Lehmler, H.-J.2    Robertson, L.W.3    James, M.O.4
  • 111
    • 0021828106 scopus 로고
    • Purification and kinetic characterization of a dopamine-sulfating form of phenol sulfotransferase from human brain
    • DOI 10.1021/bi00331a013
    • Whittemore RM, Pearce LB, Roth JA. (1985). Purification and kinetic characterization of a dopamine-sulfating form of phenol sulfotransferase from human brain. Biochemistry 24:2477-2482. (Pubitemid 15015753)
    • (1985) Biochemistry , vol.24 , Issue.10 , pp. 2477-2482
    • Whittemore, R.M.1    Pearce, L.B.2    Roth, J.A.3
  • 112
    • 53749096477 scopus 로고    scopus 로고
    • Allosteric modulation of SULT2A1 by celecoxib and nimesulide: Computational analyses
    • Yalcin EB, Struzik SM, King RS. (2008). Allosteric modulation of SULT2A1 by celecoxib and nimesulide: Computational analyses.Drug Metab Lett 2:198-204.
    • (2008) Drug Metab Lett , vol.2 , pp. 198-204
    • Yalcin, E.B.1    Struzik, S.M.2    King, R.S.3
  • 113
    • 34247857329 scopus 로고    scopus 로고
    • Cigarette smoke toxicants as substrates and inhibitors for human cytosolic SULTs
    • DOI 10.1016/j.taap.2007.02.013, PII S0041008X07000853
    • Yasuda S, Idell S, Fu J, et al. (2007). Cigarette smoke toxicants as substrates and inhibitors for human cytosolic SULTs. Toxicol Appl Pharmacol 221:13-20. (Pubitemid 46702277)
    • (2007) Toxicology and Applied Pharmacology , vol.221 , Issue.1 , pp. 13-20
    • Yasuda, S.1    Idell, S.2    Fu, J.3    Carter, G.4    Snow, R.5    Liu, M.-C.6
  • 114
    • 18244393185 scopus 로고    scopus 로고
    • Oral contraceptives as substrates and inhibitors for human cytosolic SULTs
    • DOI 10.1093/jb/mvi047
    • Yasuda S, Suiko M, Liu MC. (2005). Oral contraceptives as substrates and inhibitors for human cytosolic SULTs. J Biochem 137:401-406. (Pubitemid 40628448)
    • (2005) Journal of Biochemistry , vol.137 , Issue.3 , pp. 401-406
    • Yasuda, S.1    Suiko, M.2    Liu, M.-C.3
  • 115
    • 0037467073 scopus 로고    scopus 로고
    • Effects of phenolic acids on human phenolsulfotransferases in relation to their antioxidant activity
    • Yeh CT, Yen GC. (2003). Effects of phenolic acids on human phenolsulfotransferases in relation to their antioxidant activity.J Agric Food Chem 51:1474-1479.
    • (2003) J Agric Food Chem , vol.51 , pp. 1474-1479
    • Yeh, C.T.1    Yen, G.C.2
  • 116
    • 0021960624 scopus 로고
    • Human phenol sulfotransferase: Correlation of brain and platelet activities
    • DOI 10.1111/j.1471-4159.1985.tb08734.x
    • Young Jr WF, Laws Jr ER, Sharbrough FW, Weinshilboum RM. (1985).Human phenol sulfotransferase: Correlation of brain and platelet activities. J Neurochem 44:1131-1137. (Pubitemid 15105765)
    • (1985) Journal of Neurochemistry , vol.44 , Issue.4 , pp. 1131-1137
    • Young Jr., W.F.1    Laws Jr., E.R.2    Sharbrough, F.W.3    Weinshilboum, R.M.4
  • 117


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