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Volumn 30, Issue 1, 2015, Pages 3-20

Structural plasticity in the human cytosolic sulfotransferase dimer and its role in substrate selectivity and catalysis

Author keywords

3 diphosphoadenosine; 3 phosphoadenosine 5 phosphosulfate; Cytosolic sulfotransferase; Metabolism; PAP; PAPS; Structure; Sulfation; SULT

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; CYTOSOLIC SULFOTRANSFERASE; SULFOTRANSFERASE; UNCLASSIFIED DRUG; DRUG; ISOENZYME; PROTEIN BINDING;

EID: 84925014270     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.1016/j.dmpk.2014.10.004     Document Type: Review
Times cited : (62)

References (191)
  • 1
    • 0033051051 scopus 로고    scopus 로고
    • Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells
    • A. Kotov, J.L. Falany, J. Wang, and C.N. Falany Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells J Steroid Biochem Mol Biol 3-4 1999 137 144
    • (1999) J Steroid Biochem Mol Biol , vol.3-4 , pp. 137-144
    • Kotov, A.1    Falany, J.L.2    Wang, J.3    Falany, C.N.4
  • 2
    • 70349280717 scopus 로고    scopus 로고
    • 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: Formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver x receptor activation
    • I.T. Cook, Z. Duniec-Dmuchowski, T.A. Kocarek, M. Runge-Morris, and C.N. Falany 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver x receptor activation Drug Metab Dispos Biol Fate Chem 10 2009 2069 2078
    • (2009) Drug Metab Dispos Biol Fate Chem , vol.10 , pp. 2069-2078
    • Cook, I.T.1    Duniec-Dmuchowski, Z.2    Kocarek, T.A.3    Runge-Morris, M.4    Falany, C.N.5
  • 3
    • 79151476474 scopus 로고    scopus 로고
    • Sulfation of 25-hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells
    • Q. Bai, L. Xu, G. Kakiyama, M.A. Runge-Morris, P.B. Hylemon, and L. Yin Sulfation of 25-hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells Atherosclerosis 2 2011 350 356
    • (2011) Atherosclerosis , vol.2 , pp. 350-356
    • Bai, Q.1    Xu, L.2    Kakiyama, G.3    Runge-Morris, M.A.4    Hylemon, P.B.5    Yin, L.6
  • 5
    • 0019760160 scopus 로고
    • Increased cholesterol sulfate in plasma and red blood cell membranes of steroid sulfatase deficient patients
    • E.A. Bergner, and L.J. Shapiro Increased cholesterol sulfate in plasma and red blood cell membranes of steroid sulfatase deficient patients J Clin Endocrinol Metab 1 1981 221 223
    • (1981) J Clin Endocrinol Metab , vol.1 , pp. 221-223
    • Bergner, E.A.1    Shapiro, L.J.2
  • 8
    • 0029705444 scopus 로고    scopus 로고
    • Pathways of thyroid hormone metabolism
    • T.J. Visser pathways of thyroid hormone metabolism Acta Med Austriaca 1-2 1996 10 16
    • (1996) Acta Med Austriaca , vol.1-2 , pp. 10-16
    • Visser, T.J.1
  • 10
    • 84862073598 scopus 로고    scopus 로고
    • Crystal structures of human sulfotransferases: Insights into the mechanisms of action and substrate selectivity
    • D. Dong, R. Ako, and B. Wu Crystal structures of human sulfotransferases: insights into the mechanisms of action and substrate selectivity Expert Opin Drug Metab Toxicol 6 2012 635 646
    • (2012) Expert Opin Drug Metab Toxicol , vol.6 , pp. 635-646
    • Dong, D.1    Ako, R.2    Wu, B.3
  • 11
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • C.N. Falany enzymology of human cytosolic sulfotransferases FASEB J Off Publ Fed Am Soc Exp Biol 4 1997 206 216
    • (1997) FASEB J off Publ Fed Am Soc Exp Biol , vol.4 , pp. 206-216
    • Falany, C.N.1
  • 12
    • 0033569516 scopus 로고    scopus 로고
    • Pharmacogenomics: Translating functional genomics into rational therapeutics
    • W.E. Evans, and M.V. Relling Pharmacogenomics: translating functional genomics into rational therapeutics Science 5439 1999 487 491
    • (1999) Science , vol.5439 , pp. 487-491
    • Evans, W.E.1    Relling, M.V.2
  • 13
    • 31844448260 scopus 로고    scopus 로고
    • Human sulphotransferases are involved in the activation of aristolochic acids and are expressed in renal target tissue
    • W. Meinl, U. Pabel, M. Osterloh-Quiroz, J.G. Hengstler, and H. Glatt Human sulphotransferases are involved in the activation of aristolochic acids and are expressed in renal target tissue Int J Cancer J Int du cancer 5 2006 1090 1097
    • (2006) Int J Cancer J Int du Cancer , vol.5 , pp. 1090-1097
    • Meinl, W.1    Pabel, U.2    Osterloh-Quiroz, M.3    Hengstler, J.G.4    Glatt, H.5
  • 14
    • 84882769868 scopus 로고    scopus 로고
    • Highly selective bioactivation of 1- and 2-hydroxy-3-methylcholanthrene to mutagens by individual human and other mammalian sulphotransferases expressed in Salmonella typhimurium
    • W. Meinl, C. Tsoi, S. Swedmark, Z.E. Tibbs, C.N. Falany, and H. Glatt Highly selective bioactivation of 1- and 2-hydroxy-3-methylcholanthrene to mutagens by individual human and other mammalian sulphotransferases expressed in Salmonella typhimurium Mutagenesis 5 2013 609 619
    • (2013) Mutagenesis , vol.5 , pp. 609-619
    • Meinl, W.1    Tsoi, C.2    Swedmark, S.3    Tibbs, Z.E.4    Falany, C.N.5    Glatt, H.6
  • 15
    • 0025202686 scopus 로고
    • Minoxidil sulfate is the active metabolite that stimulates hair follicles
    • A.E. Buhl, D.J. Waldon, C.A. Baker, and G.A. Johnson Minoxidil sulfate is the active metabolite that stimulates hair follicles J Investig Dermatol 5 1990 553 557
    • (1990) J Investig Dermatol , vol.5 , pp. 553-557
    • Buhl, A.E.1    Waldon, D.J.2    Baker, C.A.3    Johnson, G.A.4
  • 16
    • 84863931141 scopus 로고    scopus 로고
    • A nucleotide-gated molecular pore selects sulfotransferase substrates
    • I. Cook, T. Wang, C.N. Falany, and T.S. Leyh A nucleotide-gated molecular pore selects sulfotransferase substrates Biochemistry 28 2012 5674 5683
    • (2012) Biochemistry , vol.28 , pp. 5674-5683
    • Cook, I.1    Wang, T.2    Falany, C.N.3    Leyh, T.S.4
  • 18
    • 0036796816 scopus 로고    scopus 로고
    • Sulfonation and molecular action
    • C.A. Strott Sulfonation and molecular action Endocr Rev 5 2002 703 732
    • (2002) Endocr Rev , vol.5 , pp. 703-732
    • Strott, C.A.1
  • 19
    • 4544226091 scopus 로고    scopus 로고
    • Sulfotransferases: Structure, mechanism, biological activity, inhibition, and synthetic utility
    • E. Chapman, M.D. Best, S.R. Hanson, and C.H. Wong Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility Angew Chem 27 2004 3526 3548
    • (2004) Angew Chem , vol.27 , pp. 3526-3548
    • Chapman, E.1    Best, M.D.2    Hanson, S.R.3    Wong, C.H.4
  • 22
    • 84924983670 scopus 로고
    • Concerning the occurrence of brenzcatechin in the urine
    • E. Baumann Concerning the occurrence of brenzcatechin in the urine Pflügers Archiv Eur J Physiol 69 1876
    • (1876) Pflügers Archiv Eur J Physiol , vol.69
    • Baumann, E.1
  • 23
    • 0025869349 scopus 로고
    • Molecular enzymology of human liver cytosolic sulfotransferases
    • C.N. Falany Molecular enzymology of human liver cytosolic sulfotransferases Trends Pharmacol Sci 7 1991 255 259
    • (1991) Trends Pharmacol Sci , vol.7 , pp. 255-259
    • Falany, C.N.1
  • 24
    • 0034534841 scopus 로고    scopus 로고
    • Sulfotransferases in the bioactivation of xenobiotics
    • H. Glatt Sulfotransferases in the bioactivation of xenobiotics Chem Biol Interact 1-2 2000 141 170
    • (2000) Chem Biol Interact , vol.1-2 , pp. 141-170
    • Glatt, H.1
  • 25
    • 0023094378 scopus 로고
    • Molecular cloning and characterization of cDNA for androgen-repressible rat liver protein, SMP-2
    • B. Chatterjee, D. Majumdar, O. Ozbilen, C.V. Murty, and A.K. Roy Molecular cloning and characterization of cDNA for androgen-repressible rat liver protein, SMP-2 J Biol Chem 2 1987 822 825
    • (1987) J Biol Chem , vol.2 , pp. 822-825
    • Chatterjee, B.1    Majumdar, D.2    Ozbilen, O.3    Murty, C.V.4    Roy, A.K.5
  • 26
    • 0024149024 scopus 로고
    • Oestrogen sulfotransferase: Molecular cloning and sequencing of cDNA for the bovine placental enzyme
    • A.R. Nash, W.K. Glenn, S.S. Moore, J. Kerr, A.R. Thompson, and E.O. Thompson Oestrogen sulfotransferase: molecular cloning and sequencing of cDNA for the bovine placental enzyme Aust J Biol Sci 4 1988 507 516
    • (1988) Aust J Biol Sci , vol.4 , pp. 507-516
    • Nash, A.R.1    Glenn, W.K.2    Moore, S.S.3    Kerr, J.4    Thompson, A.R.5    Thompson, E.O.6
  • 27
    • 0028206389 scopus 로고
    • Human dehydroepiandrosterone sulfotransferase: Molecular cloning of cDNA and genomic DNA
    • D.M. Otterness, and R. Weinshilboum Human dehydroepiandrosterone sulfotransferase: molecular cloning of cDNA and genomic DNA Chem Biol Interact 1-3 1994 145 159
    • (1994) Chem Biol Interact , vol.1-3 , pp. 145-159
    • Otterness, D.M.1    Weinshilboum, R.2
  • 30
    • 0035834560 scopus 로고    scopus 로고
    • Structure and localization of the human SULT1B1 gene: Neighborhood to SULT1E1 and a SULT1D pseudogene
    • W. Meinl, and H. Glatt Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene Biochem Biophys Res Commun 4 2001 855 862
    • (2001) Biochem Biophys Res Commun , vol.4 , pp. 855-862
    • Meinl, W.1    Glatt, H.2
  • 31
    • 0031887611 scopus 로고    scopus 로고
    • Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver
    • J. Wang, J.L. Falany, and C.N. Falany Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver Mol Pharmacol 2 1998 274 282
    • (1998) Mol Pharmacol , vol.2 , pp. 274-282
    • Wang, J.1    Falany, J.L.2    Falany, C.N.3
  • 32
    • 0029053067 scopus 로고
    • Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
    • C.N. Falany, V. Krasnykh, and J.L. Falany Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase J Steroid Biochem Mol Biol 6 1995 529 539
    • (1995) J Steroid Biochem Mol Biol , vol.6 , pp. 529-539
    • Falany, C.N.1    Krasnykh, V.2    Falany, J.L.3
  • 34
    • 63849173713 scopus 로고    scopus 로고
    • Expression and localization of cytosolic sulfotransferase (SULT) 1A1 and SULT1A3 in normal human brain
    • E.D. Salman, S.A. Kadlubar, and C.N. Falany Expression and localization of cytosolic sulfotransferase (SULT) 1A1 and SULT1A3 in normal human brain Drug Metab Dispos Biol Fate Chem 4 2009 706 709
    • (2009) Drug Metab Dispos Biol Fate Chem , vol.4 , pp. 706-709
    • Salman, E.D.1    Kadlubar, S.A.2    Falany, C.N.3
  • 35
    • 0034654571 scopus 로고    scopus 로고
    • Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain
    • C.N. Falany, X. Xie, J. Wang, J. Ferrer, and J.L. Falany Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain Biochem J 857-864 2000
    • (2000) Biochem J , vol.857-864
    • Falany, C.N.1    Xie, X.2    Wang, J.3    Ferrer, J.4    Falany, J.L.5
  • 36
    • 0031149235 scopus 로고    scopus 로고
    • Human sulfotransferase SULT1C1: CDNA cloning, tissue-specific expression, and chromosomal localization
    • C. Her, G.P. Kaur, R.S. Athwal, and R.M. Weinshilboum Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization Genomics 3 1997 467 470
    • (1997) Genomics , vol.3 , pp. 467-470
    • Her, C.1    Kaur, G.P.2    Athwal, R.S.3    Weinshilboum, R.M.4
  • 37
    • 0032545405 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene
    • Y. Sakakibara, K. Yanagisawa, J. Katafuchi, D.P. Ringer, Y. Takami, and T. Nakayama Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene J Biol Chem 51 1998 33929 33935
    • (1998) J Biol Chem , vol.51 , pp. 33929-33935
    • Sakakibara, Y.1    Yanagisawa, K.2    Katafuchi, J.3    Ringer, D.P.4    Takami, Y.5    Nakayama, T.6
  • 38
    • 23644432067 scopus 로고    scopus 로고
    • Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification
    • E.L. Stanley, R. Hume, and M.W. Coughtrie Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification Mol Cell Endocrinol 1-2 2005 32 42
    • (2005) Mol Cell Endocrinol , vol.1-2 , pp. 32-42
    • Stanley, E.L.1    Hume, R.2    Coughtrie, M.W.3
  • 39
    • 39149086046 scopus 로고    scopus 로고
    • SULT1C3, an orphan sequence of the human genome, encodes an enzyme activating various promutagens. Food and chemical toxicology
    • W. Meinl, C. Donath, H. Schneider, Y. Sommer, and H. Glatt SULT1C3, an orphan sequence of the human genome, encodes an enzyme activating various promutagens. Food and chemical toxicology Int J Publ Br Ind Biol Res Assoc 4 2008 1249 1256
    • (2008) Int J Publ Br Ind Biol Res Assoc , vol.4 , pp. 1249-1256
    • Meinl, W.1    Donath, C.2    Schneider, H.3    Sommer, Y.4    Glatt, H.5
  • 40
    • 84893852024 scopus 로고    scopus 로고
    • Expression of the orphan cytosolic sulfotransferase SULT1C3 in human intestine: Characterization of the transcript variant and implications for function
    • Z. Duniec-Dmuchowski, E.A. Rondini, Z.E. Tibbs, C.N. Falany, M. Runge-Morris, and T.A. Kocarek Expression of the orphan cytosolic sulfotransferase SULT1C3 in human intestine: characterization of the transcript variant and implications for function Drug Metab Dispos Biol Fate Chem 3 2014 352 360
    • (2014) Drug Metab Dispos Biol Fate Chem , vol.3 , pp. 352-360
    • Duniec-Dmuchowski, Z.1    Rondini, E.A.2    Tibbs, Z.E.3    Falany, C.N.4    Runge-Morris, M.5    Kocarek, T.A.6
  • 41
    • 0034895787 scopus 로고    scopus 로고
    • Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b)
    • C.A. Meloche, and C.N. Falany Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b) J Steroid Biochem Mol Biol 4-5 2001 261 269
    • (2001) J Steroid Biochem Mol Biol , vol.4-5 , pp. 261-269
    • Meloche, C.A.1    Falany, C.N.2
  • 42
    • 33751015135 scopus 로고    scopus 로고
    • Human cytosolic sulfotransferase 2B1: Isoform expression, tissue specificity and subcellular localization
    • C.N. Falany, D. He, N. Dumas, A.R. Frost, and J.L. Falany Human cytosolic sulfotransferase 2B1: isoform expression, tissue specificity and subcellular localization J Steroid Biochem Mol Biol 1-5 2006 214 221
    • (2006) J Steroid Biochem Mol Biol , vol.1-5 , pp. 214-221
    • Falany, C.N.1    He, D.2    Dumas, N.3    Frost, A.R.4    Falany, J.L.5
  • 43
    • 2542597642 scopus 로고    scopus 로고
    • Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate
    • D. He, C.A. Meloche, N.A. Dumas, A.R. Frost, and C.N. Falany Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate Biochem J Pt 3 2004 533 540
    • (2004) Biochem J Pt , vol.3 , pp. 533-540
    • He, D.1    Meloche, C.A.2    Dumas, N.A.3    Frost, A.R.4    Falany, C.N.5
  • 44
    • 2442421716 scopus 로고    scopus 로고
    • Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes
    • Y. Higashi, H. Fuda, H. Yanai, Y. Lee, T. Fukushige, and T. Kanzaki Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes J Investig Dermatol 5 2004 1207 1213
    • (2004) J Investig Dermatol , vol.5 , pp. 1207-1213
    • Higashi, Y.1    Fuda, H.2    Yanai, H.3    Lee, Y.4    Fukushige, T.5    Kanzaki, T.6
  • 45
    • 0031136606 scopus 로고    scopus 로고
    • Sulfation and sulfotransferases 5: The importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB journal
    • C.D. Klaassen, and J.W. Boles Sulfation and sulfotransferases 5: the importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB journal Off Publ Fed Am Soc Exp Biol 6 1997 404 418
    • (1997) Off Publ Fed Am Soc Exp Biol , vol.6 , pp. 404-418
    • Klaassen, C.D.1    Boles, J.W.2
  • 46
    • 0019452651 scopus 로고
    • An evaluation of methods to decrease the availability of inorganic sulphate for sulphate conjugation in the rat in vivo
    • K.R. Krujgsheld, E. Scholtens, and G.J. Mulder An evaluation of methods to decrease the availability of inorganic sulphate for sulphate conjugation in the rat in vivo Biochem Pharmacol 14 1981 1973 1979
    • (1981) Biochem Pharmacol , vol.14 , pp. 1973-1979
    • Krujgsheld, K.R.1    Scholtens, E.2    Mulder, G.J.3
  • 47
    • 0024447657 scopus 로고
    • Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3′-phosphate 5′-phosphosulphate in human tissues
    • M. Cappiello, M. Franchi, L. Giuliani, and G.M. Pacifici Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3′-phosphate 5′-phosphosulphate in human tissues Eur J Clin Pharmacol 3 1989 317 320
    • (1989) Eur J Clin Pharmacol , vol.3 , pp. 317-320
    • Cappiello, M.1    Franchi, M.2    Giuliani, L.3    Pacifici, G.M.4
  • 48
    • 84886588118 scopus 로고    scopus 로고
    • Structural rearrangement of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation
    • I.T. Cook, T.S. Leyh, S.A. Kadlubar, and C.N. Falany Structural rearrangement of SULT2A1: effects on dehydroepiandrosterone and raloxifene sulfation Hormone Mol Biol Clin Investig 2 2010 81 87
    • (2010) Hormone Mol Biol Clin Investig , vol.2 , pp. 81-87
    • Cook, I.T.1    Leyh, T.S.2    Kadlubar, S.A.3    Falany, C.N.4
  • 49
    • 0025193236 scopus 로고
    • Sulfation of minoxidil by human liver phenol sulfotransferase
    • C.N. Falany, and E.A. Kerl Sulfation of minoxidil by human liver phenol sulfotransferase Biochem Pharmacol 5 1990 1027 1032
    • (1990) Biochem Pharmacol , vol.5 , pp. 1027-1032
    • Falany, C.N.1    Kerl, E.A.2
  • 50
    • 0027377101 scopus 로고
    • Minoxidil sulphation in human liver and platelets. A study of interindividual variability
    • G.M. Pacifici, R. Bigotti, G. Marchi, and L. Giuliani Minoxidil sulphation in human liver and platelets. A study of interindividual variability Eur J Clin Pharmacol 4 1993 337 341
    • (1993) Eur J Clin Pharmacol , vol.4 , pp. 337-341
    • Pacifici, G.M.1    Bigotti, R.2    Marchi, G.3    Giuliani, L.4
  • 51
    • 0025366673 scopus 로고
    • The effect of multiple dosage on the kinetics of glucuronidation and sulphation of diflunisal in man
    • R.K. Verbeeck, G.R. Loewen, J.I. MacDonald, and R.J. Herman The effect of multiple dosage on the kinetics of glucuronidation and sulphation of diflunisal in man Br J Clin Pharmacol 4 1990 381 389
    • (1990) Br J Clin Pharmacol , vol.4 , pp. 381-389
    • Verbeeck, R.K.1    Loewen, G.R.2    Macdonald, J.I.3    Herman, R.J.4
  • 52
    • 0023155938 scopus 로고
    • The effect of acetaminophen on the disposition of fenoldopam: Competition for sulfation
    • J.A. Ziemniak, N. Allison, V.K. Boppana, J. Dubb, and R. Stote The effect of acetaminophen on the disposition of fenoldopam: competition for sulfation Clin Pharmacol Ther 3 1987 275 281
    • (1987) Clin Pharmacol Ther , vol.3 , pp. 275-281
    • Ziemniak, J.A.1    Allison, N.2    Boppana, V.K.3    Dubb, J.4    Stote, R.5
  • 54
    • 0020310135 scopus 로고
    • Platelet phenol sulfotransferase activity: Correlation with sulfate conjugation of acetaminophen
    • C. Reiter, and R. Weinshilboum Platelet phenol sulfotransferase activity: correlation with sulfate conjugation of acetaminophen Clin Pharmacol Ther 5 1982 612 621
    • (1982) Clin Pharmacol Ther , vol.5 , pp. 612-621
    • Reiter, C.1    Weinshilboum, R.2
  • 55
    • 0028014488 scopus 로고
    • Human liver budesonide sulphotransferase is inhibited by testosterone and correlates with by testosterone sulphotransferase
    • G.M. Pacifici, M.A. Ferroni, A. Temellini, A. Gucci, M.C. Morelli, and L. Giuliani Human liver budesonide sulphotransferase is inhibited by testosterone and correlates with by testosterone sulphotransferase Eur J Clin Pharmacol 1 1994 49 54
    • (1994) Eur J Clin Pharmacol , vol.1 , pp. 49-54
    • Pacifici, G.M.1    Ferroni, M.A.2    Temellini, A.3    Gucci, A.4    Morelli, M.C.5    Giuliani, L.6
  • 56
    • 0024241120 scopus 로고
    • Maternal and neonatal urinary excretion of sulfate and glucuronide ritodrine conjugates
    • W.T. Brashear, B.R. Kuhnert, and R. Wei Maternal and neonatal urinary excretion of sulfate and glucuronide ritodrine conjugates Clin Pharmacol Ther 6 1988 634 641
    • (1988) Clin Pharmacol Ther , vol.6 , pp. 634-641
    • Brashear, W.T.1    Kuhnert, B.R.2    Wei, R.3
  • 57
    • 0025831505 scopus 로고
    • Interindividual variability in the glucuronidation and sulphation of ethinyloestradiol in human liver
    • A. Temellini, L. Giuliani, and G.M. Pacifici Interindividual variability in the glucuronidation and sulphation of ethinyloestradiol in human liver Br J Clin Pharmacol 6 1991 661 664
    • (1991) Br J Clin Pharmacol , vol.6 , pp. 661-664
    • Temellini, A.1    Giuliani, L.2    Pacifici, G.M.3
  • 60
    • 0035217142 scopus 로고    scopus 로고
    • Human sulfotransferase SULT1C1 pharmacogenetics: Gene resequencing and functional genomic studies
    • R.R. Freimuth, B. Eckloff, E.D. Wieben, and R.M. Weinshilboum Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies Pharmacogenetics 9 2001 747 756
    • (2001) Pharmacogenetics , vol.9 , pp. 747-756
    • Freimuth, R.R.1    Eckloff, B.2    Wieben, E.D.3    Weinshilboum, R.M.4
  • 63
    • 34047102223 scopus 로고    scopus 로고
    • Sulfotransferase (sult) 1A1 pharmacogenetics: Functional 5[prime]-flanking region (5[prime]-FR) polymorphisms
    • P77-P77
    • J. Prondzinski, B. Thomae, L. Wang, B. Eckloff, E. Wieben, and R. Weinshilboum Sulfotransferase (sult) 1A1 pharmacogenetics: functional 5[prime]-flanking region (5[prime]-FR) polymorphisms Clin Pharmacol Ther 2 2003 P77-P77
    • (2003) Clin Pharmacol Ther , vol.2
    • Prondzinski, J.1    Thomae, B.2    Wang, L.3    Eckloff, B.4    Wieben, E.5    Weinshilboum, R.6
  • 64
    • 0020430630 scopus 로고
    • A genetic study of platelet phenolsulphotransferase activity in normal and schizophrenic twins
    • A.M. Reveley, S.M. Bonham Carter, M.A. Reveley, and M. Sandler A genetic study of platelet phenolsulphotransferase activity in normal and schizophrenic twins J Psychiatric Res 3 1982 303 307
    • (1982) J Psychiatric Res , vol.3 , pp. 303-307
    • Reveley, A.M.1    Bonham Carter, S.M.2    Reveley, M.A.3    Sandler, M.4
  • 65
    • 0030338743 scopus 로고    scopus 로고
    • Dietary modulation of human platelet phenolsulphotransferase activity
    • R.M. Harris, and R.H. Waring Dietary modulation of human platelet phenolsulphotransferase activity Xenobiot Fate For Compd Biol Syst 12 1996 1241 1247
    • (1996) Xenobiot Fate for Compd Biol Syst , vol.12 , pp. 1241-1247
    • Harris, R.M.1    Waring, R.H.2
  • 66
    • 0035689972 scopus 로고    scopus 로고
    • Differential inhibition of human liver and duodenum sulphotransferase activities by quercetin, a flavonoid present in vegetables, fruit and wine
    • F. Marchetti, C. De Santi, M. Vietri, A. Pietrabissa, R. Spisni, and F. Mosca Differential inhibition of human liver and duodenum sulphotransferase activities by quercetin, a flavonoid present in vegetables, fruit and wine Xenobiot Fate For Compd Biol Syst 12 2001 841 847
    • (2001) Xenobiot Fate for Compd Biol Syst , vol.12 , pp. 841-847
    • Marchetti, F.1    De Santi, C.2    Vietri, M.3    Pietrabissa, A.4    Spisni, R.5    Mosca, F.6
  • 67
    • 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
    • M. Vietri, F. Vaglini, A. Pietrabissa, R. Spisni, F. Mosca, and G.M. Pacifici Sulfation of R(-)-apomorphine in the human liver and duodenum, and its inhibition by mefenamic acid, salicylic acid and quercetin Xenobiot Fate For Compd Biol Syst 7 2002 587 594
    • (2002) Xenobiot Fate for Compd Biol Syst , vol.7 , pp. 587-594
    • Vietri, M.1    Vaglini, F.2    Pietrabissa, A.3    Spisni, R.4    Mosca, F.5    Pacifici, G.M.6
  • 68
    • 84863889483 scopus 로고    scopus 로고
    • Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: Role of 3′-phosphoadenosine 5′-phosphosulfate binding and structural rearrangements in regulating inhibition and activity
    • K.J. Rohn, I.T. Cook, T.S. Leyh, S.A. Kadlubar, and C.N. Falany Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: role of 3′-phosphoadenosine 5′-phosphosulfate binding and structural rearrangements in regulating inhibition and activity Drug Metab Dispos Biol Fate Chem 8 2012 1588 1595
    • (2012) Drug Metab Dispos Biol Fate Chem , vol.8 , pp. 1588-1595
    • Rohn, K.J.1    Cook, I.T.2    Leyh, T.S.3    Kadlubar, S.A.4    Falany, C.N.5
  • 69
    • 0032538626 scopus 로고    scopus 로고
    • The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis
    • Y. Kakuta The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis J Biol Chem 42 1998 27325 27330
    • (1998) J Biol Chem , vol.42 , pp. 27325-27330
    • Kakuta, Y.1
  • 70
    • 0033520425 scopus 로고    scopus 로고
    • Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis
    • E. Ong Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis J Biol Chem 36 1999 25608 25612
    • (1999) J Biol Chem , vol.36 , pp. 25608-25612
    • Ong, E.1
  • 71
    • 67349237767 scopus 로고    scopus 로고
    • Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate
    • T. Teramoto, Y. Sakakibara, M.C. Liu, M. Suiko, M. Kimura, and Y. Kakuta Snapshot of a Michaelis complex in a sulfuryl transfer reaction: crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate Biochem Biophys Res Commun 1 2009 83 87
    • (2009) Biochem Biophys Res Commun , vol.1 , pp. 83-87
    • Teramoto, T.1    Sakakibara, Y.2    Liu, M.C.3    Suiko, M.4    Kimura, M.5    Kakuta, Y.6
  • 72
    • 0037124087 scopus 로고    scopus 로고
    • Crystal structure of the human estrogen sulfotransferase-PAPS complex: Evidence for catalytic role of Ser137 in the sulfuryl transfer reaction
    • L.C. Pedersen, E. Petrotchenko, S. Shevtsov, and M. Negishi Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction J Biol Chem 20 2002 17928 17932
    • (2002) J Biol Chem , vol.20 , pp. 17928-17932
    • Pedersen, L.C.1    Petrotchenko, E.2    Shevtsov, S.3    Negishi, M.4
  • 73
    • 33750082361 scopus 로고    scopus 로고
    • Transition state of the sulfuryl transfer reaction of estrogen sulfotransferase
    • R.H. Hoff, P.G. Czyryca, M. Sun, T.S. Leyh, and A.C. Hengge Transition state of the sulfuryl transfer reaction of estrogen sulfotransferase J Biol Chem 41 2006 30645 30649
    • (2006) J Biol Chem , vol.41 , pp. 30645-30649
    • Hoff, R.H.1    Czyryca, P.G.2    Sun, M.3    Leyh, T.S.4    Hengge, A.C.5
  • 74
    • 0029007293 scopus 로고
    • A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase
    • J.M. Dolence, and C.D. Poulter A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase Proc Natl Acad Sci U S A 11 1995 5008 5011
    • (1995) Proc Natl Acad Sci U S A , vol.11 , pp. 5008-5011
    • Dolence, J.M.1    Poulter, C.D.2
  • 75
    • 34248550960 scopus 로고    scopus 로고
    • Transition state analysis of model and enzymatic prenylation reactions
    • S. Lenevich, J. Xu, A. Hosokawa, C.J. Cramer, and M.D. Distefano Transition state analysis of model and enzymatic prenylation reactions J Am Chem Soc 18 2007 5796 5797
    • (2007) J Am Chem Soc , vol.18 , pp. 5796-5797
    • Lenevich, S.1    Xu, J.2    Hosokawa, A.3    Cramer, C.J.4    Distefano, M.D.5
  • 76
    • 77955923297 scopus 로고    scopus 로고
    • Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: A mass spectrometry approach
    • L.M. Danan, Z. Yu, P.J. Ludden, W. Jia, K.L. Moore, and J.A. Leary Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach J Am Soc Mass Spectrom 9 2010 1633 1642
    • (2010) J Am Soc Mass Spectrom , vol.9 , pp. 1633-1642
    • Danan, L.M.1    Yu, Z.2    Ludden, P.J.3    Jia, W.4    Moore, K.L.5    Leary, J.A.6
  • 77
    • 0027757048 scopus 로고
    • The physical biochemistry and molecular genetics of sulfate activation
    • T.S. Leyh the physical biochemistry and molecular genetics of sulfate activation Crit Rev Biochem Mol Biol 6 1993 515 542
    • (1993) Crit Rev Biochem Mol Biol , vol.6 , pp. 515-542
    • Leyh, T.S.1
  • 78
    • 0014429240 scopus 로고
    • Kinetic studies of the phenol sulphotranferase reaction
    • R.K. Banerjee, and A.B. Roy Kinetic studies of the phenol sulphotranferase reaction Biochim Biophys Acta 3 1968 573 586
    • (1968) Biochim Biophys Acta , vol.3 , pp. 573-586
    • Banerjee, R.K.1    Roy, A.B.2
  • 79
    • 0022540097 scopus 로고
    • Purification and kinetic characterization of a phenol-sulfating form of phenol sulfotransferase from human brain
    • R.M. Whittemore, L.B. Pearce, and J.A. Roth Purification and kinetic characterization of a phenol-sulfating form of phenol sulfotransferase from human brain Arch Biochem Biophys 2 1986 464 471
    • (1986) Arch Biochem Biophys , vol.2 , pp. 464-471
    • Whittemore, R.M.1    Pearce, L.B.2    Roth, J.A.3
  • 80
    • 55849116013 scopus 로고    scopus 로고
    • Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase
    • E. Tyapochkin, P.F. Cook, and G. Chen Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase Biochemistry 45 2008 11894 11899
    • (2008) Biochemistry , vol.45 , pp. 11894-11899
    • Tyapochkin, E.1    Cook, P.F.2    Chen, G.3
  • 81
    • 0019891912 scopus 로고
    • Mechanistic deductions from isotope effects in multireactant enzyme mechanisms
    • P.F. Cook, and W.W. Cleland Mechanistic deductions from isotope effects in multireactant enzyme mechanisms Biochemistry 7 1981 1790 1796
    • (1981) Biochemistry , vol.7 , pp. 1790-1796
    • Cook, P.F.1    Cleland, W.W.2
  • 82
    • 0032080151 scopus 로고    scopus 로고
    • Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase
    • H. Zhang, O. Varlamova, F.M. Vargas, C.N. Falany, and T.S. Leyh Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase J Biol Chem 18 1998 10888 10892
    • (1998) J Biol Chem , vol.18 , pp. 10888-10892
    • Zhang, H.1    Varlamova, O.2    Vargas, F.M.3    Falany, C.N.4    Leyh, T.S.5
  • 83
    • 23944500803 scopus 로고    scopus 로고
    • Sulfonation of environmental chemicals and their metabolites in the polar bear (Ursus maritimus)
    • J.C. Sacco, and M.O. James Sulfonation of environmental chemicals and their metabolites in the polar bear (Ursus maritimus) Drug Metab Dispos Biol Fate Chem 9 2005 1341 1348
    • (2005) Drug Metab Dispos Biol Fate Chem , vol.9 , pp. 1341-1348
    • Sacco, J.C.1    James, M.O.2
  • 84
    • 0022646351 scopus 로고
    • The effect of inhibitors of mitochondrial energy production on hepatic glutathione, UDP-glucuronic acid, and adenosine 3′-phosphate-5′-phosphosulfate concentrations
    • R.L. Dills, and C.D. Klaassen The effect of inhibitors of mitochondrial energy production on hepatic glutathione, UDP-glucuronic acid, and adenosine 3′-phosphate-5′-phosphosulfate concentrations Drug Metab Dispos Biol Fate Chem 2 1986 190 196
    • (1986) Drug Metab Dispos Biol Fate Chem , vol.2 , pp. 190-196
    • Dills, R.L.1    Klaassen, C.D.2
  • 85
    • 0025012491 scopus 로고
    • Effect of sulfhydryl-deficient diets on hepatic metallothionein, glutathione, and adenosine 3′-phosphate 5′-phosphosulfate (PAPS) levels in rats
    • L.E. Sendelbach, C.A. White, S. Howell, Z. Gregus, and C.D. Klaassen Effect of sulfhydryl-deficient diets on hepatic metallothionein, glutathione, and adenosine 3′-phosphate 5′-phosphosulfate (PAPS) levels in rats Toxicol Appl Pharmacol 2 1990 259 267
    • (1990) Toxicol Appl Pharmacol , vol.2 , pp. 259-267
    • Sendelbach, L.E.1    White, C.A.2    Howell, S.3    Gregus, Z.4    Klaassen, C.D.5
  • 86
    • 84907200601 scopus 로고    scopus 로고
    • Paradigms of sulfotransferase catalysis - The mechanism of SULT2A1
    • T. Wang, I. Cook, C.N. Falany, and T.S. Leyh Paradigms of sulfotransferase catalysis - the mechanism of SULT2A1 J Biol Chem 289 2014 26474 26480
    • (2014) J Biol Chem , vol.289 , pp. 26474-26480
    • Wang, T.1    Cook, I.2    Falany, C.N.3    Leyh, T.S.4
  • 87
    • 0019877641 scopus 로고
    • On the mechanism of aryl sulfotransferase
    • M.W. Duffel, and W.B. Jakoby On the mechanism of aryl sulfotransferase J Biol Chem 21 1981 11123 11127
    • (1981) J Biol Chem , vol.21 , pp. 11123-11127
    • Duffel, M.W.1    Jakoby, W.B.2
  • 88
    • 40849137940 scopus 로고    scopus 로고
    • Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1)
    • L.Y. Lu, Y.C. Hsieh, M.Y. Liu, Y.H. Lin, C.J. Chen, and Y.S. Yang Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1) Mol Pharmacol 3 2008 660 668
    • (2008) Mol Pharmacol , vol.3 , pp. 660-668
    • Lu, L.Y.1    Hsieh, Y.C.2    Liu, M.Y.3    Lin, Y.H.4    Chen, C.J.5    Yang, Y.S.6
  • 89
    • 79951943420 scopus 로고    scopus 로고
    • Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes
    • H.O. Gulcan, and M.W. Duffel Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexes Arch Biochem Biophys 2 2011 232 240
    • (2011) Arch Biochem Biophys , vol.2 , pp. 232-240
    • Gulcan, H.O.1    Duffel, M.W.2
  • 90
    • 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
    • N.U. Gamage, S. Tsvetanov, R.G. Duggleby, M.E. McManus, and J.L. Martin The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates J Biol Chem 50 2005 41482 41486
    • (2005) J Biol Chem , vol.50 , pp. 41482-41486
    • Gamage, N.U.1    Tsvetanov, S.2    Duggleby, R.G.3    McManus, M.E.4    Martin, J.L.5
  • 91
    • 0032548889 scopus 로고    scopus 로고
    • Effects of 3′-phosphoadenosine 5′-phosphate on the activity and folding of phenol sulfotransferase
    • Y.S. Yang, S.W. Tsai, and E.S. Lin Effects of 3′-phosphoadenosine 5′-phosphate on the activity and folding of phenol sulfotransferase Chem Biol Interact 1-3 1998 129 135
    • (1998) Chem Biol Interact , vol.1-3 , pp. 129-135
    • Yang, Y.S.1    Tsai, S.W.2    Lin, E.S.3
  • 94
    • 33748457919 scopus 로고    scopus 로고
    • Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3′- 5′-diphosphate (PAP)
    • L. Dombrovski, A. Dong, A. Bochkarev, and A.N. Plotnikov Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3′- 5′-diphosphate (PAP) Proteins 4 2006 1091 1094
    • (2006) Proteins , vol.4 , pp. 1091-1094
    • Dombrovski, L.1    Dong, A.2    Bochkarev, A.3    Plotnikov, A.N.4
  • 96
    • 0037093546 scopus 로고    scopus 로고
    • Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate
    • P.H. Rehse, M. Zhou, and S.X. Lin Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate Biochem J Pt 1 2002 165 171
    • (2002) Biochem J Pt , vol.1 , pp. 165-171
    • Rehse, P.H.1    Zhou, M.2    Lin, S.X.3
  • 98
    • 84886588118 scopus 로고    scopus 로고
    • Structural rearrangement of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation
    • I.T. Cook, T.S. Leyh, S.A. Kadlubar, and C.N. Falany Structural rearrangement of SULT2A1: effects on dehydroepiandrosterone and raloxifene sulfation Hormone Mol Biol Clin Investig 2 2009 81 87
    • (2009) Hormone Mol Biol Clin Investig , vol.2 , pp. 81-87
    • Cook, I.T.1    Leyh, T.S.2    Kadlubar, S.A.3    Falany, C.N.4
  • 99
    • 84898798773 scopus 로고    scopus 로고
    • Inhibition of SULT4A1 expression induces up-regulation of phototransduction gene expression in 72-hour postfertilization zebrafish larvae
    • F. Crittenden, H. Thomas, C.M. Ethen, Z.L. Wu, D. Chen, and T.W. Kraft Inhibition of SULT4A1 expression induces up-regulation of phototransduction gene expression in 72-hour postfertilization zebrafish larvae Drug Metab Dispos Biol Fate Chem 5 2014 947 953
    • (2014) Drug Metab Dispos Biol Fate Chem , vol.5 , pp. 947-953
    • Crittenden, F.1    Thomas, H.2    Ethen, C.M.3    Wu, Z.L.4    Chen, D.5    Kraft, T.W.6
  • 100
    • 0032437886 scopus 로고    scopus 로고
    • A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3
    • R. Dajani, A.M. Hood, and M.W. Coughtrie A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3 Mol Pharmacol 6 1998 942 948
    • (1998) Mol Pharmacol , vol.6 , pp. 942-948
    • Dajani, R.1    Hood, A.M.2    Coughtrie, M.W.3
  • 102
    • 0037184096 scopus 로고    scopus 로고
    • Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase
    • H. Fuda, Y.C. Lee, C. Shimizu, N.B. Javitt, and C.A. Strott Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase J Biol Chem 39 2002 36161 36166
    • (2002) J Biol Chem , vol.39 , pp. 36161-36166
    • Fuda, H.1    Lee, Y.C.2    Shimizu, C.3    Javitt, N.B.4    Strott, C.A.5
  • 103
    • 0242582327 scopus 로고    scopus 로고
    • Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms
    • K.A. Lee, H. Fuda, Y.C. Lee, M. Negishi, C.A. Strott, and L.C. Pedersen Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms J Biol Chem 45 2003 44593 44599
    • (2003) J Biol Chem , vol.45 , pp. 44593-44599
    • Lee, K.A.1    Fuda, H.2    Lee, Y.C.3    Negishi, M.4    Strott, C.A.5    Pedersen, L.C.6
  • 104
    • 0037470234 scopus 로고    scopus 로고
    • Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition
    • N.U. Gamage, R.G. Duggleby, A.C. Barnett, M. Tresillian, C.F. Latham, and N.E. Liyou Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition J Biol Chem 9 2003 7655 7662
    • (2003) J Biol Chem , vol.9 , pp. 7655-7662
    • Gamage, N.U.1    Duggleby, R.G.2    Barnett, A.C.3    Tresillian, M.4    Latham, C.F.5    Liyou, N.E.6
  • 106
    • 0034625464 scopus 로고    scopus 로고
    • Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
    • L.C. Pedersen, E.V. Petrotchenko, and M. Negishi Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase FEBS Lett 1 2000 61 64
    • (2000) FEBS Lett , vol.1 , pp. 61-64
    • Pedersen, L.C.1    Petrotchenko, E.V.2    Negishi, M.3
  • 107
    • 1642453680 scopus 로고    scopus 로고
    • Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: Structure of the enzyme-ADT complex
    • H.J. Chang, R. Shi, P. Rehse, and S.X. Lin Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex J Biol Chem 4 2004 2689 2696
    • (2004) J Biol Chem , vol.4 , pp. 2689-2696
    • Chang, H.J.1    Shi, R.2    Rehse, P.3    Lin, S.X.4
  • 110
    • 0032909806 scopus 로고    scopus 로고
    • Effects of molybdate and pentachlorophenol on the sulfation of alpha-naphthol
    • J.W. Boles, and C.D. Klaassen Effects of molybdate and pentachlorophenol on the sulfation of alpha-naphthol Toxicol Lett 1 1999 1 8
    • (1999) Toxicol Lett , vol.1 , pp. 1-8
    • Boles, J.W.1    Klaassen, C.D.2
  • 111
    • 0029618138 scopus 로고
    • Depletion of hepatic 3′-phosphoadenosine 5′-phosphosulfate (PAPS) and sulfate in rats by xenobiotics that are sulfated
    • H.J. Kim, J.H. Cho, and C.D. Klaassen Depletion of hepatic 3′-phosphoadenosine 5′-phosphosulfate (PAPS) and sulfate in rats by xenobiotics that are sulfated J Pharmacol Exp Ther 2 1995 654 658
    • (1995) J Pharmacol Exp Ther , vol.2 , pp. 654-658
    • Kim, H.J.1    Cho, J.H.2    Klaassen, C.D.3
  • 112
    • 0032563290 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of human bifunctional 3′-phosphoadenosine 5′-phosphosulfate synthase and its functional domains
    • K.V. Venkatachalam, H. Akita, and C.A. Strott Molecular cloning, expression, and characterization of human bifunctional 3′-phosphoadenosine 5′-phosphosulfate synthase and its functional domains J Biol Chem 30 1998 19311 19320
    • (1998) J Biol Chem , vol.30 , pp. 19311-19320
    • Venkatachalam, K.V.1    Akita, H.2    Strott, C.A.3
  • 113
    • 17344364658 scopus 로고    scopus 로고
    • Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse
    • M. Faiyaz ul Haque, L.M. King, D. Krakow, R.M. Cantor, M.E. Rusiniak, and R.T. Swank Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse Nat Genet 2 1998 157 162
    • (1998) Nat Genet , vol.2 , pp. 157-162
    • Faiyaz Ul Haque, M.1    King, L.M.2    Krakow, D.3    Cantor, R.M.4    Rusiniak, M.E.5    Swank, R.T.6
  • 114
    • 0032548887 scopus 로고    scopus 로고
    • Sulfate activation and transport in mammals: System components and mechanisms
    • N.B. Schwartz, S. Lyle, J.D. Ozeran, H. Li, A. Deyrup, and K. Ng Sulfate activation and transport in mammals: system components and mechanisms Chem Biol Interact 1-3 1998 143 151
    • (1998) Chem Biol Interact , vol.1-3 , pp. 143-151
    • Schwartz, N.B.1    Lyle, S.2    Ozeran, J.D.3    Li, H.4    Deyrup, A.5    Ng, K.6
  • 115
    • 1842583797 scopus 로고    scopus 로고
    • Human 3′-phosphoadenosine 5′-phosphosulfate synthetase (isoform 1, brain): Kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5′-phosphosulfate kinase domains
    • E.B. Lansdon, A.J. Fisher, and I.H. Segel Human 3′-phosphoadenosine 5′-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5′-phosphosulfate kinase domains Biochemistry 14 2004 4356 4365
    • (2004) Biochemistry , vol.14 , pp. 4356-4365
    • Lansdon, E.B.1    Fisher, A.J.2    Segel, I.H.3
  • 116
    • 0037101780 scopus 로고    scopus 로고
    • Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms
    • H. Fuda, C. Shimizu, Y.C. Lee, H. Akita, and C.A. Strott Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms Biochem J Pt 2 2002 497 504
    • (2002) Biochem J Pt , vol.2 , pp. 497-504
    • Fuda, H.1    Shimizu, C.2    Lee, Y.C.3    Akita, H.4    Strott, C.A.5
  • 117
    • 0033960622 scopus 로고    scopus 로고
    • Nuclear localization of PAPS synthetase 1: A sulfate activation pathway in the nucleus of eukaryotic cells. FASEB journal
    • S. Besset, J.B. Vincourt, F. Amalric, and J.P. Girard Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells. FASEB journal Off Publ Fed Am Soc Exp Biol 2 2000 345 354
    • (2000) Off Publ Fed Am Soc Exp Biol , vol.2 , pp. 345-354
    • Besset, S.1    Vincourt, J.B.2    Amalric, F.3    Girard, J.P.4
  • 118
    • 84855385018 scopus 로고    scopus 로고
    • Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm
    • E. Schroder, L. Gebel, A.A. Eremeev, J. Morgner, D. Grum, and S.K. Knauer Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm PloS One 1 2012 e29559
    • (2012) PloS One , vol.1 , pp. e29559
    • Schroder, E.1    Gebel, L.2    Eremeev, A.A.3    Morgner, J.4    Grum, D.5    Knauer, S.K.6
  • 120
    • 34248524402 scopus 로고    scopus 로고
    • Expression profile of Papss2 (3′-phosphoadenosine 5′-phosphosulfate synthase 2) during cartilage formation and skeletal development in the mouse embryo. Developmental dynamics
    • C. Stelzer, A. Brimmer, P. Hermanns, B. Zabel, and U.H. Dietz Expression profile of Papss2 (3′-phosphoadenosine 5′-phosphosulfate synthase 2) during cartilage formation and skeletal development in the mouse embryo. Developmental dynamics Off Publ Am Assoc Anat 5 2007 1313 1318
    • (2007) Off Publ Am Assoc Anat , vol.5 , pp. 1313-1318
    • Stelzer, C.1    Brimmer, A.2    Hermanns, P.3    Zabel, B.4    Dietz, U.H.5
  • 121
    • 33746357573 scopus 로고    scopus 로고
    • Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment
    • S. Goettsch, R.A. Badea, J.W. Mueller, C. Wotzlaw, B. Schoelermann, and L. Schulz Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment J Mol Biol 3 2006 436 449
    • (2006) J Mol Biol , vol.3 , pp. 436-449
    • Goettsch, S.1    Badea, R.A.2    Mueller, J.W.3    Wotzlaw, C.4    Schoelermann, B.5    Schulz, L.6
  • 122
    • 33744951681 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel 3′-phosphoadenosine 5′-phosphosulfate transporter, PAPST2
    • S. Kamiyama, N. Sasaki, E. Goda, K. Ui-Tei, K. Saigo, and H. Narimatsu Molecular cloning and characterization of a novel 3′-phosphoadenosine 5′-phosphosulfate transporter, PAPST2 J Biol Chem 16 2006 10945 10953
    • (2006) J Biol Chem , vol.16 , pp. 10945-10953
    • Kamiyama, S.1    Sasaki, N.2    Goda, E.3    Ui-Tei, K.4    Saigo, K.5    Narimatsu, H.6
  • 123
    • 0029876794 scopus 로고    scopus 로고
    • Identification and partial purification of PAPS translocase
    • J.D. Ozeran, J. Westley, and N.B. Schwartz Identification and partial purification of PAPS translocase Biochemistry 12 1996 3695 3703
    • (1996) Biochemistry , vol.12 , pp. 3695-3703
    • Ozeran, J.D.1    Westley, J.2    Schwartz, N.B.3
  • 124
    • 0000377421 scopus 로고
    • Metabolism of sulfur compounds (sulfate metabolism)
    • J.D. Gregory, and P.W. Robbins Metabolism of sulfur compounds (sulfate metabolism) Annu Rev Biochem 347-364 1960
    • (1960) Annu Rev Biochem , vol.347
    • Gregory, J.D.1    Robbins, P.W.2
  • 125
    • 0026649746 scopus 로고
    • Homeostasis of sulfate and 3′-phosphoadenosine 5′-phosphosulfate in rats after acetaminophen administration
    • H.J. Kim, P. Rozman, C. Madhu, and C.D. Klaassen Homeostasis of sulfate and 3′-phosphoadenosine 5′-phosphosulfate in rats after acetaminophen administration J Pharmacol Exp Ther 3 1992 1015 1021
    • (1992) J Pharmacol Exp Ther , vol.3 , pp. 1015-1021
    • Kim, H.J.1    Rozman, P.2    Madhu, C.3    Klaassen, C.D.4
  • 126
    • 0023110646 scopus 로고
    • Comparison of adenosine 3′-phosphate 5′-phosphosulfate concentrations in tissues from different laboratory animals
    • E.A. Brzeznicka, G.A. Hazelton, and C.D. Klaassen Comparison of adenosine 3′-phosphate 5′-phosphosulfate concentrations in tissues from different laboratory animals Drug Metab Dispos Biol Fate Chem 1 1987 133 135
    • (1987) Drug Metab Dispos Biol Fate Chem , vol.1 , pp. 133-135
    • Brzeznicka, E.A.1    Hazelton, G.A.2    Klaassen, C.D.3
  • 127
    • 0025162286 scopus 로고
    • Sulphotransferase and its substrate: Adenosine-3′-phosphate-5′-phosphosulphate in human fetal liver and placenta
    • M. Cappiello, M. Franchi, A. Rane, and G.M. Pacifici Sulphotransferase and its substrate: adenosine-3′-phosphate-5′-phosphosulphate in human fetal liver and placenta Dev Pharmacol Ther 1 1990 62 65
    • (1990) Dev Pharmacol Ther , vol.1 , pp. 62-65
    • Cappiello, M.1    Franchi, M.2    Rane, A.3    Pacifici, G.M.4
  • 128
    • 66149131846 scopus 로고    scopus 로고
    • An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases
    • B. Weitzner, T. Meehan, Q. Xu, and R.L. Dunbrack Jr. An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases Proteins 2 2009 289 295
    • (2009) Proteins , vol.2 , pp. 289-295
    • Weitzner, B.1    Meehan, T.2    Xu, Q.3    Dunbrack, Jr.R.L.4
  • 129
    • 0028848909 scopus 로고
    • Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene
    • C.C. Kiehlbauch, Y.F. Lam, and D.P. Ringer Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene J Biol Chem 32 1995 18941 18947
    • (1995) J Biol Chem , vol.32 , pp. 18941-18947
    • Kiehlbauch, C.C.1    Lam, Y.F.2    Ringer, D.P.3
  • 130
    • 0023812901 scopus 로고
    • Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets
    • J.A. Heroux, and J.A. Roth Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets Mol Pharmacol 2 1988 194 199
    • (1988) Mol Pharmacol , vol.2 , pp. 194-199
    • Heroux, J.A.1    Roth, J.A.2
  • 132
    • 0014030843 scopus 로고
    • Symmetry of protein oligomers formed by isologous association
    • K.R. Hanson Symmetry of protein oligomers formed by isologous association J Mol Biol 2 1966 405 409
    • (1966) J Mol Biol , vol.2 , pp. 405-409
    • Hanson, K.R.1
  • 136
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod, J. Wyman, and J.P. Changeux On the nature of allosteric transitions: a plausible model J Mol Biol 12 1965 88 118
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 137
    • 66449124488 scopus 로고    scopus 로고
    • Dimerization is responsible for the structural stability of human sulfotransferase 1A1
    • L.Y. Lu, H.P. Chiang, W.T. Chen, and Y.S. Yang Dimerization is responsible for the structural stability of human sulfotransferase 1A1 Drug Metab Dispos Biol Fate Chem 5 2009 1083 1088
    • (2009) Drug Metab Dispos Biol Fate Chem , vol.5 , pp. 1083-1088
    • Lu, L.Y.1    Chiang, H.P.2    Chen, W.T.3    Yang, Y.S.4
  • 139
    • 0015247054 scopus 로고
    • Half-Of-The-Sites reactivity and the conformational states of cytidine triphosphate synthetase
    • A. Levitzki, W.B. Stallcup, and D.E. Koshland Jr. Half-of-the-sites reactivity and the conformational states of cytidine triphosphate synthetase Biochemistry 18 1971 3371 3378
    • (1971) Biochemistry , vol.18 , pp. 3371-3378
    • Levitzki, A.1    Stallcup, W.B.2    Koshland, Jr.D.E.3
  • 141
    • 0345426287 scopus 로고    scopus 로고
    • The structural mechanism for half-The-Sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits
    • A.C. Anderson, R.H. O'Neil, W.L. DeLano, and R.M. Stroud The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits Biochemistry 42 1999 13829 13836
    • (1999) Biochemistry , vol.42 , pp. 13829-13836
    • Anderson, A.C.1    O'Neil, R.H.2    Delano, W.L.3    Stroud, R.M.4
  • 142
    • 84880701665 scopus 로고    scopus 로고
    • New insights into the half-Of-The-Sites reactivity of human aldehyde dehydrogenase 1A1
    • B. Yoval-Sanchez, J.P. Pardo, and J.S. Rodriguez-Zavala New insights into the half-of-the-sites reactivity of human aldehyde dehydrogenase 1A1 Proteins 8 2013 1330 1339
    • (2013) Proteins , vol.8 , pp. 1330-1339
    • Yoval-Sanchez, B.1    Pardo, J.P.2    Rodriguez-Zavala, J.S.3
  • 143
    • 0001497377 scopus 로고
    • Chemda: Enzymes with asymmetrically arranged subunits
    • Y.D. Degani Chemda: enzymes with asymmetrically arranged subunits Trends Biochem Sci 12 1980 337 341
    • (1980) Trends Biochem Sci , vol.12 , pp. 337-341
    • Degani, Y.D.1
  • 144
    • 0038035198 scopus 로고    scopus 로고
    • The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
    • P.S. Pruett, A. Azzi, S.A. Clark, M.S. Yousef, J.L. Gattis, and T. Somasundaram The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase J Biol Chem 29 2003 26952 26957
    • (2003) J Biol Chem , vol.29 , pp. 26952-26957
    • Pruett, P.S.1    Azzi, A.2    Clark, S.A.3    Yousef, M.S.4    Gattis, J.L.5    Somasundaram, T.6
  • 145
    • 78650909033 scopus 로고    scopus 로고
    • Arginine kinase: Joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility
    • X. Niu, L. Bruschweiler-Li, O. Davulcu, J.J. Skalicky, R. Bruschweiler, and M.S. Chapman Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility J Mol Biol 2 2011 479 496
    • (2011) J Mol Biol , vol.2 , pp. 479-496
    • Niu, X.1    Bruschweiler-Li, L.2    Davulcu, O.3    Skalicky, J.J.4    Bruschweiler, R.5    Chapman, M.S.6
  • 147
    • 77953261062 scopus 로고    scopus 로고
    • The human estrogen sulfotransferase: A half-site reactive enzyme
    • M. Sun, and T.S. Leyh The human estrogen sulfotransferase: a half-site reactive enzyme Biochemistry 23 2010 4779 4785
    • (2010) Biochemistry , vol.23 , pp. 4779-4785
    • Sun, M.1    Leyh, T.S.2
  • 149
    • 0030296282 scopus 로고    scopus 로고
    • Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16
    • T.P. Dooley, and Z. Huang Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16 Biochem Biophys Res Commun 1 1996 134 140
    • (1996) Biochem Biophys Res Commun , vol.1 , pp. 134-140
    • Dooley, T.P.1    Huang, Z.2
  • 151
    • 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 1 1993 70 77
    • (1993) Mol Pharmacol , vol.1 , pp. 70-77
    • Wilborn, T.W.1    Comer, K.A.2    Dooley, T.P.3    Reardon, I.M.4    Heinrikson, R.L.5    Falany, C.N.6
  • 152
    • 0029951532 scopus 로고    scopus 로고
    • Human phenol sulfotransferase STP2 gene: Molecular cloning, structural characterization, and chromosomal localization
    • C. Her, R. Raftogianis, and R.M. Weinshilboum Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization Genomics 3 1996 409 420
    • (1996) Genomics , vol.3 , pp. 409-420
    • Her, C.1    Raftogianis, R.2    Weinshilboum, R.M.3
  • 153
    • 0028101442 scopus 로고
    • Thermolabile phenol sulfotransferase gene (STM): Localization to human chromosome 16p11.2
    • I.A. Aksoy, D.F. Callen, S. Apostolou, C. Her, and R.M. Weinshilboum Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2 Genomics 1 1994 275 277
    • (1994) Genomics , vol.1 , pp. 275-277
    • Aksoy, I.A.1    Callen, D.F.2    Apostolou, S.3    Her, C.4    Weinshilboum, R.M.5
  • 155
    • 0028334382 scopus 로고
    • Human liver thermolabile phenol sulfotransferase: CDNA cloning, expression and characterization
    • T.C. Wood, I.A. Aksoy, S. Aksoy, and R.M. Weinshilboum Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization Biochem Biophys Res Commun 3 1994 1119 1127
    • (1994) Biochem Biophys Res Commun , vol.3 , pp. 1119-1127
    • Wood, T.C.1    Aksoy, I.A.2    Aksoy, S.3    Weinshilboum, R.M.4
  • 156
    • 0030808766 scopus 로고    scopus 로고
    • Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases
    • K. Fujita, K. Nagata, S. Ozawa, H. Sasano, and Y. Yamazoe Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases J Biochem 5 1997 1052 1061
    • (1997) J Biochem , vol.5 , pp. 1052-1061
    • Fujita, K.1    Nagata, K.2    Ozawa, S.3    Sasano, H.4    Yamazoe, Y.5
  • 157
    • 0034656291 scopus 로고    scopus 로고
    • Human sulfotransferases SULT1C1 and SULT1C2: CDNA characterization, gene cloning, and chromosomal localization
    • R.R. Freimuth, R.B. Raftogianis, T.C. Wood, E. Moon, U.J. Kim, and J. Xu Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization Genomics 2 2000 157 165
    • (2000) Genomics , vol.2 , pp. 157-165
    • Freimuth, R.R.1    Raftogianis, R.B.2    Wood, T.C.3    Moon, E.4    Kim, U.J.5    Xu, J.6
  • 158
    • 1342289636 scopus 로고    scopus 로고
    • Human cytosolic sulfotransferase database mining: Identification of seven novel genes and pseudogenes
    • R.R. Freimuth, M. Wiepert, C.G. Chute, E.D. Wieben, and R.M. Weinshilboum Human cytosolic sulfotransferase database mining: identification of seven novel genes and pseudogenes pharmacogenomics J 1 2004 54 65
    • (2004) Pharmacogenomics J , vol.1 , pp. 54-65
    • Freimuth, R.R.1    Wiepert, M.2    Chute, C.G.3    Wieben, E.D.4    Weinshilboum, R.M.5
  • 159
    • 79958841703 scopus 로고    scopus 로고
    • SwissParam: A fast force field generation tool for small organic molecules
    • V. Zoete, M.A. Cuendet, A. Grosdidier, and O. Michielin SwissParam: a fast force field generation tool for small organic molecules J Comput Chem 11 2011 2359 2368
    • (2011) J Comput Chem , vol.11 , pp. 2359-2368
    • Zoete, V.1    Cuendet, M.A.2    Grosdidier, A.3    Michielin, O.4
  • 160
    • 0028359554 scopus 로고
    • Human liver estrogen sulfotransferase: Identification by cDNA cloning and expression
    • I.A. Aksoy, T.C. Wood, and R. Weinshilboum Human liver estrogen sulfotransferase: identification by cDNA cloning and expression Biochem Biophys Res Commun 3 1994 1621 1629
    • (1994) Biochem Biophys Res Commun , vol.3 , pp. 1621-1629
    • Aksoy, I.A.1    Wood, T.C.2    Weinshilboum, R.3
  • 161
    • 0028969206 scopus 로고
    • Dehydroepiandrosterone sulfotransferase gene (STD): Localization to human chromosome band 19q13.3
    • D.M. Otterness, H.W. Mohrenweiser, B.F. Brandriff, and R.M. Weinshilboum Dehydroepiandrosterone sulfotransferase gene (STD): localization to human chromosome band 19q13.3 Cytogenet cell Genet 1-2 1995 45 47
    • (1995) Cytogenet Cell Genet , vol.1-2 , pp. 45-47
    • Otterness, D.M.1    Mohrenweiser, H.W.2    Brandriff, B.F.3    Weinshilboum, R.M.4
  • 163
    • 0026739431 scopus 로고
    • Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver
    • A.N. Kong, L. Yang, M. Ma, D. Tao, and T.D. Bjornsson Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver Biochem Biophys Res Commun 1 1992 448 454
    • (1992) Biochem Biophys Res Commun , vol.1 , pp. 448-454
    • Kong, A.N.1    Yang, L.2    Ma, M.3    Tao, D.4    Bjornsson, T.D.5
  • 164
    • 0027475375 scopus 로고
    • Cloning and expression of human liver dehydroepiandrosterone sulphotransferase
    • K.A. Comer, J.L. Falany, and C.N. Falany Cloning and expression of human liver dehydroepiandrosterone sulphotransferase Biochem J 289 1993 233 240
    • (1993) Biochem J , vol.289 , pp. 233-240
    • Comer, K.A.1    Falany, J.L.2    Falany, C.N.3
  • 165
    • 0032213662 scopus 로고    scopus 로고
    • Human hydroxysteroid sulfotransferase SULT2B1: Two enzymes encoded by a single chromosome 19 gene
    • C. Her, T.C. Wood, E.E. Eichler, H.W. Mohrenweiser, L.S. Ramagli, and M.J. Siciliano Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene Genomics 3 1998 284 295
    • (1998) Genomics , vol.3 , pp. 284-295
    • Her, C.1    Wood, T.C.2    Eichler, E.E.3    Mohrenweiser, H.W.4    Ramagli, L.S.5    Siciliano, M.J.6
  • 166
    • 0000128616 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a human sulfotransferase, SULT4A1, that represents a novel SULT family
    • S.E.D. Walther, L. R, and R.B. Raftogianis Cloning, expression and characterization of a human sulfotransferase, SULT4A1, that represents a novel SULT family ISSX Proc Abstr 338 1999
    • (1999) ISSX Proc Abstr , vol.338
    • Walther, S.E.D.1    Raftogianis, R.B.2
  • 167
    • 8744230973 scopus 로고    scopus 로고
    • Human thyroid phenol sulfotransferase enzymes 1A1 and 1A3: Activities in normal and diseased thyroid glands, and inhibition by thyroid hormones and phytoestrogens
    • C.C. Ebmeier, and R.J. Anderson Human thyroid phenol sulfotransferase enzymes 1A1 and 1A3: activities in normal and diseased thyroid glands, and inhibition by thyroid hormones and phytoestrogens J Clin Endocrinol Metab 11 2004 5597 5605
    • (2004) J Clin Endocrinol Metab , vol.11 , pp. 5597-5605
    • Ebmeier, C.C.1    Anderson, R.J.2
  • 168
    • 34249799590 scopus 로고    scopus 로고
    • Identification and localization of soluble sulfotransferases in the human gastrointestinal tract
    • W. Teubner, W. Meinl, S. Florian, M. Kretzschmar, and H. Glatt Identification and localization of soluble sulfotransferases in the human gastrointestinal tract Biochem J 2 2007 207 215
    • (2007) Biochem J , vol.2 , pp. 207-215
    • Teubner, W.1    Meinl, W.2    Florian, S.3    Kretzschmar, M.4    Glatt, H.5
  • 169
    • 0034649125 scopus 로고    scopus 로고
    • Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells
    • T.P. Dooley, R. Haldeman-Cahill, J. Joiner, and T.W. Wilborn Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells Biochem Biophys Res Commun 1 2000 236 245
    • (2000) Biochem Biophys Res Commun , vol.1 , pp. 236-245
    • Dooley, T.P.1    Haldeman-Cahill, R.2    Joiner, J.3    Wilborn, T.W.4
  • 170
    • 20444397024 scopus 로고    scopus 로고
    • Identification and immunohistochemical localization of Sulfotransferase 2B1b (SULT2B1b) in human lung
    • D. He, A.R. Frost, and C.N. Falany Identification and immunohistochemical localization of Sulfotransferase 2B1b (SULT2B1b) in human lung Biochim Biophys Acta 1-2 2005 119 126
    • (2005) Biochim Biophys Acta , vol.1-2 , pp. 119-126
    • He, D.1    Frost, A.R.2    Falany, C.N.3
  • 171
    • 84872575044 scopus 로고    scopus 로고
    • Sulfation of buprenorphine, pentazocine, and naloxone by human cytosolic sulfotransferases
    • K. Kurogi, M. Chen, Y. Lee, B. Shi, T. Yan, and M.Y. Liu Sulfation of buprenorphine, pentazocine, and naloxone by human cytosolic sulfotransferases Drug Metab Lett 2 2012 109 115
    • (2012) Drug Metab Lett , vol.2 , pp. 109-115
    • Kurogi, K.1    Chen, M.2    Lee, Y.3    Shi, B.4    Yan, T.5    Liu, M.Y.6
  • 172
    • 0024309210 scopus 로고
    • Human intestinal phenol sulfotransferase: Assay conditions, activity levels and partial purification of the thermolabile form
    • R.S. Sundaram, C. Szumlanski, D. Otterness, J.A. van Loon, and R.M. Weinshilboum Human intestinal phenol sulfotransferase: assay conditions, activity levels and partial purification of the thermolabile form Drug Metab Dispos Biol Fate Chem 3 1989 255 264
    • (1989) Drug Metab Dispos Biol Fate Chem , vol.3 , pp. 255-264
    • Sundaram, R.S.1    Szumlanski, C.2    Otterness, D.3    Van Loon, J.A.4    Weinshilboum, R.M.5
  • 173
    • 63849300219 scopus 로고    scopus 로고
    • Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3
    • S. Yasuda, M.Y. Liu, M. Suiko, Y. Sakakibara, and M.C. Liu Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3 J Neurochem 6 2007 2679 2689
    • (2007) J Neurochem , vol.6 , pp. 2679-2689
    • Yasuda, S.1    Liu, M.Y.2    Suiko, M.3    Sakakibara, Y.4    Liu, M.C.5
  • 174
    • 0033621476 scopus 로고    scopus 로고
    • X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity
    • R. Dajani, A. Cleasby, M. Neu, A.J. Wonacott, H. Jhoti, and A.M. Hood X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity J Biol Chem 53 1999 37862 37868
    • (1999) J Biol Chem , vol.53 , pp. 37862-37868
    • Dajani, R.1    Cleasby, A.2    Neu, M.3    Wonacott, A.J.4    Jhoti, H.5    Hood, A.M.6
  • 175
    • 0033053169 scopus 로고    scopus 로고
    • Enzymatic characterization of human cytosolic sulfotransferases; Identification of ST1B2 as a thyroid hormone sulfotransferase
    • K. Fujita, K. Nagata, T. Yamazaki, E. Watanabe, M. Shimada, and Y. Yamazoe Enzymatic characterization of human cytosolic sulfotransferases; identification of ST1B2 as a thyroid hormone sulfotransferase Biol Pharm Bull 5 1999 446 452
    • (1999) Biol Pharm Bull , vol.5 , pp. 446-452
    • Fujita, K.1    Nagata, K.2    Yamazaki, T.3    Watanabe, E.4    Shimada, M.5    Yamazoe, Y.6
  • 176
    • 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
    • L.Q. Wang, C.N. Falany, and M.O. James Triclosan as a substrate and inhibitor of 3′-phosphoadenosine 5′-phosphosulfate-sulfotransferase and UDP-glucuronosyl transferase in human liver fractions Drug Metab Dispos Biol Fate Chem 10 2004 1162 1169
    • (2004) Drug Metab Dispos Biol Fate Chem , vol.10 , pp. 1162-1169
    • Wang, L.Q.1    Falany, C.N.2    James, M.O.3
  • 177
    • 84872742282 scopus 로고    scopus 로고
    • Nomenclature and molecular biology of the human sulfotransferase family
    • G.M.C. Pacifici, W.H. Michael, CRC Press Boca Raton, FL
    • R.L. Blanchard Nomenclature and molecular biology of the human sulfotransferase family G.M.C. Pacifici, W.H. Michael, Human cytosolic sulfotransferases 2005 CRC Press Boca Raton, FL 1 26
    • (2005) Human Cytosolic Sulfotransferases , pp. 1-26
    • Blanchard, R.L.1
  • 178
    • 41849104724 scopus 로고    scopus 로고
    • On the sulfation and methylation of catecholestrogens in human mammary epithelial cells and breast cancer cells
    • Y. Hui, S. Yasuda, M.Y. Liu, Y.Y. Wu, and M.C. Liu On the sulfation and methylation of catecholestrogens in human mammary epithelial cells and breast cancer cells Biol Pharm Bull 4 2008 769 773
    • (2008) Biol Pharm Bull , vol.4 , pp. 769-773
    • Hui, Y.1    Yasuda, S.2    Liu, M.Y.3    Wu, Y.Y.4    Liu, M.C.5
  • 181
    • 84903762281 scopus 로고    scopus 로고
    • Expression of the orphan cytosolic sulfotransferase SULT4A1 and its major splice variant in human tissues and cells: Dimerization, degradation and polyubiquitination
    • N.P. Sidharthan, N.J. Butcher, D.J. Mitchell, and R.F. Minchin Expression of the orphan cytosolic sulfotransferase SULT4A1 and its major splice variant in human tissues and cells: dimerization, degradation and polyubiquitination PloS One 7 2014 e101520
    • (2014) PloS One , vol.7 , pp. e101520
    • Sidharthan, N.P.1    Butcher, N.J.2    Mitchell, D.J.3    Minchin, R.F.4
  • 182
    • 77952745911 scopus 로고    scopus 로고
    • Crystal structures of SULT1A2 and SULT1A1∗3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2
    • J. Lu, H. Li, J. Zhang, M. Li, M.Y. Liu, and X. An Crystal structures of SULT1A2 and SULT1A1∗3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2 Biochem Biophys Res Commun 2 2010 429 434
    • (2010) Biochem Biophys Res Commun , vol.2 , pp. 429-434
    • Lu, J.1    Li, H.2    Zhang, J.3    Li, M.4    Liu, M.Y.5    An, X.6
  • 183
    • 80051669875 scopus 로고    scopus 로고
    • Directed evolution of sulfotransferases and paraoxonases by ancestral libraries
    • U. Alcolombri, M. Elias, and D.S. Tawfik Directed evolution of sulfotransferases and paraoxonases by ancestral libraries J Mol Biol 4 2011 837 853
    • (2011) J Mol Biol , vol.4 , pp. 837-853
    • Alcolombri, U.1    Elias, M.2    Tawfik, D.S.3
  • 184
    • 80055109953 scopus 로고    scopus 로고
    • The molecular basis for the broad substrate specificity of human sulfotransferase 1A1
    • I. Berger, C. Guttman, D. Amar, R. Zarivach, and A. Aharoni The molecular basis for the broad substrate specificity of human sulfotransferase 1A1 PloS One 11 2011 e26794
    • (2011) PloS One , vol.11 , pp. e26794
    • Berger, I.1    Guttman, C.2    Amar, D.3    Zarivach, R.4    Aharoni, A.5
  • 185
    • 23744515308 scopus 로고    scopus 로고
    • Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3′-phosphoadenosine 5′-phosphate
    • J.H. Lu, H.T. Li, M.C. Liu, J.P. Zhang, M. Li, and X.M. An Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3′-phosphoadenosine 5′-phosphate Biochem Biophys Res Commun 2 2005 417 423
    • (2005) Biochem Biophys Res Commun , vol.2 , pp. 417-423
    • Lu, J.H.1    Li, H.T.2    Liu, M.C.3    Zhang, J.P.4    Li, M.5    An, X.M.6
  • 188
    • 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
    • S. Shevtsov, E.V. Petrotchenko, L.C. Pedersen, and M. Negishi Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase Environ Health Perspect 7 2003 884 888
    • (2003) Environ Health Perspect , vol.7 , pp. 884-888
    • Shevtsov, S.1    Petrotchenko, E.V.2    Pedersen, L.C.3    Negishi, M.4
  • 189
    • 84884899283 scopus 로고    scopus 로고
    • Mimicking of estradiol binding by flame retardants and their metabolites: A crystallographic analysis
    • R.A. Gosavi, G.A. Knudsen, L.S. Birnbaum, and L.C. Pedersen Mimicking of estradiol binding by flame retardants and their metabolites: a crystallographic analysis Environ Health Perspect 10 2013 1194 1199
    • (2013) Environ Health Perspect , vol.10 , pp. 1194-1199
    • Gosavi, R.A.1    Knudsen, G.A.2    Birnbaum, L.S.3    Pedersen, L.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.