메뉴 건너뛰기




Volumn 45, Issue 4, 2013, Pages 423-430

Structure, dynamics and selectivity in the sulfotransferase family

Author keywords

Isomerization; Metabolism; Molecular dynamics; Structure; Substrate inhibition; Sulfotransferase; SULT; Synergy

Indexed keywords

NUCLEOTIDE; PRASTERONE; RALOXIFENE; SULFOTRANSFERASE; SULFOTRANSFERASE 1A1; SULFOTRANSFERASE 2A1; UNCLASSIFIED DRUG;

EID: 84887359121     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.3109/03602532.2013.835625     Document Type: Review
Times cited : (32)

References (58)
  • 1
    • 34249073088 scopus 로고    scopus 로고
    • Structural and chemical profiling of the human cytosolic sulfotransferases
    • Allali-Hassani A, Pan PW, Dombrovski L, et al. (2007). Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol 5:e97.
    • (2007) PLoS Biol , vol.5
    • Allali-Hassani, A.1    Pan, P.W.2    Dombrovski, L.3
  • 2
    • 33748750527 scopus 로고    scopus 로고
    • Tissue distribution and ontogeny of sulfotransferase enzymes in mice
    • DOI 10.1093/toxsci/kfl050
    • Alnouti Y, Klaassen CD. (2006). Tissue distribution and ontogeny of sulfotransferase enzymes in mice. Toxicol Sci 93:242-255. (Pubitemid 44400443)
    • (2006) Toxicological Sciences , vol.93 , Issue.2 , pp. 242-255
    • Alnouti, Y.1    Klaassen, C.D.2
  • 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
    • Bai Q, Xu L, Kakiyama G, et al. (2011). Sulfation of 25- hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells. Atherosclerosis 214:350-356.
    • (2011) Atherosclerosis , vol.214 , pp. 350-356
    • Bai, Q.1    Xu, L.2    Kakiyama, G.3
  • 4
    • 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
  • 5
    • 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
    • DOI 10.1074/jbc.M310446200
    • Chang HJ, Shi R, Rehse P, Lin SX. (2004). 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 279:2689-2696. (Pubitemid 38114257)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2689-2696
    • Chang, H.-J.1    Shi, R.2    Rehse, P.3    Lin, S.-X.4
  • 6
    • 84872506191 scopus 로고    scopus 로고
    • The gate that governs sulfotransferase selectivity
    • Cook I, Wang T, Almo SC, et al. (2013a). The gate that governs sulfotransferase selectivity. Biochemistry 52:415-424.
    • (2013) Biochemistry , vol.52 , pp. 415-424
    • Cook, I.1    Wang, T.2    Almo, S.C.3
  • 7
    • 84875439090 scopus 로고    scopus 로고
    • Testing the sulfotransferase molecular pore hypothesis
    • Cook I, Wang T, Almo SC, et al. (2013b). Testing the sulfotransferase molecular pore hypothesis. J Biol Chem 288:8619-8626.
    • (2013) J Biol Chem , vol.288 , pp. 8619-8626
    • Cook, I.1    Wang, T.2    Almo, S.C.3
  • 8
    • 84863931141 scopus 로고    scopus 로고
    • A nucleotide-gated molecular pore selects sulfotransferase substrates
    • Cook I, Wang T, Falany CN, Leyh TS. (2012). A nucleotide-gated molecular pore selects sulfotransferase substrates. Biochemistry 51: 5674-5683.
    • (2012) Biochemistry , vol.51 , pp. 5674-5683
    • Cook, I.1    Wang, T.2    Falany, C.N.3    Leyh, T.S.4
  • 9
    • 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-receptor activation
    • Cook IT, Duniec-Dmuchowski Z, Kocarek TA, et al. (2009). 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: Formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver-receptor activation. Drug Metab Dispos 37:2069-2078.
    • (2009) Drug Metab Dispos , vol.37 , pp. 2069-2078
    • Cook, I.T.1    Duniec-Dmuchowski, Z.2    Kocarek, T.A.3
  • 10
    • 84886588118 scopus 로고    scopus 로고
    • Structural rearrangment of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation
    • Cook IT, Leyh TS, Kadlubar SA, Falany CN. (2010). Structural rearrangment of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation. Horm Mol Biol Clin Invest 1:81-87.
    • (2010) Horm Mol Biol Clin Invest , vol.1 , pp. 81-87
    • Cook, I.T.1    Leyh, T.S.2    Kadlubar, S.A.3    Falany, C.N.4
  • 11
    • 84862073598 scopus 로고    scopus 로고
    • Crystal structures of human sulfotransferases: Insights into the mechanisms of action and substrate selectivity
    • Dong D, Ako R, Wu B. (2012). Crystal structures of human sulfotransferases: Insights into the mechanisms of action and substrate selectivity. Expert Opin Drug Metab Toxicol 8:635-646.
    • (2012) Expert Opin Drug Metab Toxicol , vol.8 , pp. 635-646
    • Dong, D.1    Ako, R.2    Wu, B.3
  • 12
    • 0019877641 scopus 로고
    • On the mechanism of aryl sulfotransferase
    • Duffel MW, Jakoby WB. (1981). On the mechanism of aryl sulfotransferase. J Biol Chem 256:11123-11127.
    • (1981) J Biol Chem , vol.256 , pp. 11123-11127
    • Duffel, M.W.1    Jakoby, W.B.2
  • 13
    • 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
  • 14
    • 0025230526 scopus 로고
    • Purification and characterization of human liver phenol-sulfating phenol sulfotransferase
    • DOI 10.1016/0003-9861(90)90265-Z
    • Falany CN, Vazquez ME, Heroux JA, Roth JA. (1990). Purification and characterization of human liver phenol-sulfating phenol sulfotransferase.Arch Biochem Biophys 278:312-318. (Pubitemid 20126057)
    • (1990) Archives of Biochemistry and Biophysics , vol.278 , Issue.2 , pp. 312-318
    • Falany, C.N.1    Vazquez, M.E.2    Heroux, J.A.3    Roth, J.A.4
  • 15
    • 0024401919 scopus 로고
    • Purification and characterization of human liver dehydroepiandrosterone sulphotransferase
    • Falany CN, Vazquez ME, Kalb JM. (1989). Purification and characterization of human liver dehydroepiandrosterone sulphotransferase.Biochem J 260:641-646. (Pubitemid 19155657)
    • (1989) Biochemical Journal , vol.260 , Issue.3 , pp. 641-646
    • Falany, C.N.1    Vazquez, M.E.2    Kalb, J.M.3
  • 16
    • 0032548886 scopus 로고    scopus 로고
    • Identification and characterization of cytosolic sulfotransferases in normal human endometrium
    • DOI 10.1016/S0009-2797(97)00143-9, PII S0009279797001439
    • Falany JL, Azziz R, Falany CN. (1998). Identification and characterization of cytosolic sulfotransferases in normal human endometrium.Chem Biol Interact 109:329-339. (Pubitemid 28161124)
    • (1998) Chemico-Biological Interactions , vol.109 , Issue.1-3 , pp. 329-339
    • Falany, J.L.1    Azziz, R.2    Falany, C.N.3
  • 17
    • 0029976195 scopus 로고    scopus 로고
    • Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone
    • DOI 10.1210/en.137.4.1395
    • Falany JL, Falany CN. (1996). Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone.Endocrinology 137:1395-1401. (Pubitemid 26095258)
    • (1996) Endocrinology , vol.137 , Issue.4 , pp. 1395-1401
    • Falany, J.L.1    Falany, C.N.2
  • 18
    • 0035990745 scopus 로고    scopus 로고
    • Regulation of MCF-7 breast cancer cell growth by β-estradiol sulfation
    • DOI 10.1023/A:1016147004188
    • Falany JL, Macrina N, Falany CN. (2002). Regulation of MCF-7 breast cancer cell growth by beta-estradiol sulfation. Breast Cancer Res Treat 74:167-176. (Pubitemid 34816222)
    • (2002) Breast Cancer Research and Treatment , vol.74 , Issue.2 , pp. 167-176
    • Falany, J.L.1    Macrina, N.2    Falany, C.N.3
  • 19
    • 33344467530 scopus 로고    scopus 로고
    • Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases
    • DOI 10.1124/dmd.105.006551
    • Falany JL, Pilloff DE, Leyh TS, Falany CN. (2006). Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases.Drug Metab Dispos 34:361-368. (Pubitemid 43290893)
    • (2006) Drug Metabolism and Disposition , vol.34 , Issue.3 , pp. 361-368
    • Falany, J.L.1    Pilloff, D.E.2    Leyh, T.S.3    Falany, C.N.4
  • 21
    • 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
  • 23
    • 0001244133 scopus 로고
    • A linear method for determining liver sinusoidal and extravascular volumes
    • Goresky CA. (1963). A linear method for determining liver sinusoidal and extravascular volumes. Am J Physiol 204:626-640.
    • (1963) Am J Physiol , vol.204 , pp. 626-640
    • Goresky, C.A.1
  • 24
    • 79951943420 scopus 로고    scopus 로고
    • Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes
    • Gulcan HO, Duffel MW. (2011). Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes. Arch Biochem Biophys 507:232-240.
    • (2011) Arch Biochem Biophys , vol.507 , pp. 232-240
    • Gulcan, H.O.1    Duffel, M.W.2
  • 25
    • 0025848759 scopus 로고
    • Modification of liver cell volume by insulin and glucagon
    • Hallbrucker C, Vom Dahl S, Lang F, et al. (1991). Modification of liver cell volume by insulin and glucagon. Pflugers Arch 418:519-521.
    • (1991) Pflugers Arch , vol.418 , pp. 519-521
    • Hallbrucker, C.1    Vom Dahl, S.2    Lang, F.3
  • 26
    • 33947714587 scopus 로고    scopus 로고
    • SERMs: Meeting the promise of multifunctional medicines
    • DOI 10.1093/jnci/djk062
    • Jordan VC. (2007). SERMs: Meeting the promise of multifunctional medicines. J Natl Cancer Inst 99:350-356. (Pubitemid 47078725)
    • (2007) Journal of the National Cancer Institute , vol.99 , Issue.5 , pp. 350-356
    • Jordan, V.C.1
  • 29
    • 0031136606 scopus 로고    scopus 로고
    • The importance of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in the regulation of sulfation
    • Klaassen CD, Boles JW. (1997). Sulfation and sulfotransferases 5: The importance of 30-phosphoadenosine 50-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J 11:404-418. (Pubitemid 27259982)
    • (1997) FASEB Journal , vol.11 , Issue.6 , pp. 404-418
    • Klaassen, C.D.1    Boles, J.W.2
  • 30
    • 0033051051 scopus 로고    scopus 로고
    • Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells
    • DOI 10.1016/S0960-0760(99)00022-9, PII S0960076099000229
    • Kotov A, Falany JL, Wang J, Falany CN. (1999). Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells. J Steroid Biochem Mol Biol 68:137-144. (Pubitemid 29242843)
    • (1999) Journal of Steroid Biochemistry and Molecular Biology , vol.68 , Issue.3-4 , pp. 137-144
    • Kotov, A.1    Falany, J.L.2    Wang, J.3    Falany, C.N.4
  • 31
    • 0032076761 scopus 로고    scopus 로고
    • DHEA and the intracrine formation of androgens and estrogens in peripheral target tissues: Its role during aging
    • DOI 10.1016/S0039-128X(98)00007-5, PII S0039128X98000075
    • Labrie F, Bélanger A, Luu-The V, et al. (1998). DHEA and the intracrine formation of androgens and estrogens in peripheral target tissues: Its role during aging. Steroids 63:322-328. (Pubitemid 28265670)
    • (1998) Steroids , vol.63 , Issue.5-6 , pp. 322-328
    • Labrie, F.1    Belanger, A.2    Luu-The, V.3    Labrie, C.4    Simard, J.5    Cusan, L.6    Gomez, J.-L.7    Candas, B.8
  • 32
    • 80054869844 scopus 로고    scopus 로고
    • Health benefits and possible risks of broccoli-an overview
    • Latté KP, Appel KE, Lampen A. (2011). Health benefits and possible risks of broccoli-an overview. Food Chem Toxicol 49: 3287-3309.
    • (2011) Food Chem Toxicol , vol.49 , pp. 3287-3309
    • Latté, K.P.1    Appel, K.E.2    Lampen, A.3
  • 33
    • 77952745911 scopus 로고    scopus 로고
    • Crystal structures of SULT1A2 and SULT1A1 3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2
    • Lu J, Li H, Zhang J, et al. (2010). Crystal structures of SULT1A2 and SULT1A1 *3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun 396: 429-434.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 429-434
    • Lu, J.1    Li, H.2    Zhang, J.3
  • 34
    • 40849137940 scopus 로고    scopus 로고
    • Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1)
    • Lu LY, Hsieh YC, Liu MY, et al. (2008). Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Mol Pharmacol 73:660-668.
    • (2008) Mol Pharmacol , vol.73 , pp. 660-668
    • Lu, L.Y.1    Hsieh, Y.C.2    Liu, M.Y.3
  • 35
    • 0030926557 scopus 로고    scopus 로고
    • Developmental and functional biology of the primate fetal adrenal cortex
    • DOI 10.1210/er.18.3.378
    • Mesiano S, Jaffe RB. (1997). Developmental and functional biology of the primate fetal adrenal cortex. Endocr Rev 18:378-403. (Pubitemid 27246882)
    • (1997) Endocrine Reviews , vol.18 , Issue.3 , pp. 378-403
    • Mesiano, S.1    Jaffe, R.B.2
  • 36
    • 0015895154 scopus 로고
    • Serum gonadotropin and steroid patterns in early human gestation
    • Mishell DR, Thorneycroft IH, Nagata Y, et al. (1973). Serum gonadotropin and steroid patterns in early human gestation. Am J Obstet Gynecol 117:631-642.
    • (1973) Am J Obstet Gynecol , vol.117 , pp. 631-642
    • Mishell, D.R.1    Thorneycroft, I.H.2    Nagata, Y.3
  • 37
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine O-sulfation
    • DOI 10.1074/jbc.R300008200
    • Moore KL. (2003). The biology and enzymology of protein tyrosine O-sulfation. J Biol Chem 278:24243-24246. (Pubitemid 37548571)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24243-24246
    • Moore, K.L.1
  • 38
    • 0020632276 scopus 로고
    • Serum concentration and renal excretion by normal adults of inorganic sulfate after acetaminophen, ascorbic acid or sodium sulfate
    • Morris ME, Levy G. (1983). Serum concentration and renal excretion by normal adults of inorganic sulfate after acetaminophen, ascorbic acid, or sodium sulfate. Clin Pharmacol Ther 33:529-536. (Pubitemid 13093775)
    • (1983) Clinical Pharmacology and Therapeutics , vol.33 , Issue.4 , pp. 529-536
    • Morris, M.E.1    Levy, G.2
  • 39
    • 33645122881 scopus 로고    scopus 로고
    • Pharmacogenetics of human cytosolic sulfotransferases
    • Nowell S, Falany CN. (2006). Pharmacogenetics of human cytosolic sulfotransferases. Oncogene 25:1673-1678.
    • (2006) Oncogene , vol.25 , pp. 1673-1678
    • Nowell, S.1    Falany, C.N.2
  • 40
    • 0022379968 scopus 로고
    • Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study
    • Okanoue T, Ohta M, Ou O, et al. (1985). Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study. Lab Invest 53:534-540. (Pubitemid 16204929)
    • (1985) Laboratory Investigation , vol.53 , Issue.5 , pp. 534-540
    • Okanoue, T.1    Ohta, M.2    Ou, O.3
  • 41
    • 0037124087 scopus 로고    scopus 로고
    • 137 in the sulfuryl transfer reaction
    • DOI 10.1074/jbc.M111651200
    • Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. (2002). Crystal structure of the human estrogen sulfotransferase-PAPS complex: Evidence for catalytic role of Ser137 in the sulfuryl transfer reaction.J Biol Chem 277:17928-17932. (Pubitemid 34967603)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 17928-17932
    • Pedersen, L.C.1    Petrotchenko, E.2    Shevtsov, S.3    Negishi, M.4
  • 42
    • 0034625464 scopus 로고    scopus 로고
    • Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
    • DOI 10.1016/S0014-5793(00)01479-4, PII S0014579300014794
    • Pedersen LC, Petrotchenko EV, Negishi M. (2000). Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 475: 61-64. (Pubitemid 30331079)
    • (2000) FEBS Letters , vol.475 , Issue.1 , pp. 61-64
    • Pedersen, L.C.1    Petrotchenko, E.V.2    Negishi, M.3
  • 43
    • 0035830755 scopus 로고    scopus 로고
    • The dimerization motif of cytosolic sulfotransferases
    • DOI 10.1016/S0014-5793(01)02129-9, PII S0014579301021299
    • Petrotchenko EV, Pedersen LC, Borchers CH, et al. (2001). The dimerization motif of cytosolic sulfotransferases. FEBS Lett 490: 39-43. (Pubitemid 32126640)
    • (2001) FEBS Letters , vol.490 , Issue.1-2 , pp. 39-43
    • Petrotchenko, E.V.1    Pedersen, L.C.2    Borchers, C.H.3    Tomer, K.B.4    Negishi, M.5
  • 44
    • 14644390973 scopus 로고    scopus 로고
    • Missense mutations as a cause of metachromatic leukodystrophy: Degradation of arylsulfatase A in the endoplasmic reticulum
    • DOI 10.1111/j.1742-4658.2005.04553.x
    • Poeppel P, Habetha M, Marcão A, et al. (2005). Missense mutations as a cause of metachromatic leukodystrophy. Degradation of arylsulfatase A in the endoplasmic reticulum. FEBS J 272: 1179-1188. (Pubitemid 40314937)
    • (2005) FEBS Journal , vol.272 , Issue.5 , pp. 1179-1188
    • Poeppel, P.1    Habetha, M.2    Marcao, A.3    Bussow, H.4    Berna, L.5    Gieselmann, V.6
  • 45
    • 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
  • 46
    • 0036794380 scopus 로고    scopus 로고
    • Inhibition of zaleplon metabolism by cimetidine in the human liver: In vitro studies with subcellular fractions and precision-cut liver slices
    • DOI 10.1080/00498250210158221
    • Renwick AB, Ball SE, Tredger JM, et al. (2002). Inhibition of zaleplon metabolism by cimetidine in the human liver: In vitro studies with subcellular fractions and precision-cut liver slices. Xenobiotica 32: 849-862. (Pubitemid 35155520)
    • (2002) Xenobiotica , vol.32 , Issue.10 , pp. 849-862
    • Renwick, A.B.1    Ball, S.E.2    Tredger, J.M.3    Price, R.J.4    Walters, D.G.5    Kao, J.6    Scatina, J.A.7    Lake, B.G.8
  • 47
    • 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
  • 49
    • 77953261062 scopus 로고    scopus 로고
    • The human estrogen sulfotransferase: A halfsite reactive enzyme
    • Sun M, Leyh TS. (2010). The human estrogen sulfotransferase: A halfsite reactive enzyme. Biochemistry 49:4779-4785.
    • (2010) Biochemistry , vol.49 , pp. 4779-4785
    • Sun, M.1    Leyh, T.S.2
  • 50
    • 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
  • 51
    • 55849116013 scopus 로고    scopus 로고
    • Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase
    • Tyapochkin E, Cook PF, Chen G. (2008). Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry 47:11894-11899.
    • (2008) Biochemistry , vol.47 , pp. 11894-11899
    • Tyapochkin, E.1    Cook, P.F.2    Chen, G.3
  • 52
    • 70350418742 scopus 로고    scopus 로고
    • Para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E-PAP complex and reformation of E-PAPS
    • Tyapochkin E, Cook PF, Chen G. (2009). para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E-PAP complex and reformation of E-PAPS. J Biol Chem 284: 29357-29364.
    • (2009) J Biol Chem , vol.284 , pp. 29357-29364
    • Tyapochkin, E.1    Cook, P.F.2    Chen, G.3
  • 53
    • 0029177220 scopus 로고
    • Effect of time on feed on performance of feedlot steers, carcass characteristics, and tenderness and composition of longissimus muscles
    • Van Koevering MT, Gill DR, Owens FN, et al. (1995). Effect of time on feed on performance of feedlot steers, carcass characteristics, and tenderness and composition of longissimus muscles. J Anim Sci 73: 21-28.
    • (1995) J Anim Sci , vol.73 , pp. 21-28
    • Van Koevering, M.T.1    Gill, D.R.2    Owens, F.N.3
  • 54
    • 2942721004 scopus 로고    scopus 로고
    • Virtual screening using protein-ligand docking: Avoiding artificial enrichment
    • Verdonk ML, Berdini V, Hartshorn MJ, et al. (2004). Virtual screening using protein-ligand docking: Avoiding artificial enrichment. J Chem Inf Comput Sci 44:793-806.
    • (2004) J Chem Inf Comput Sci , vol.44 , pp. 793-806
    • Verdonk, M.L.1    Berdini, V.2    Hartshorn, M.J.3
  • 58
    • 33746861953 scopus 로고    scopus 로고
    • Molecular mechanisms of cholestasis
    • DOI 10.1007/s10354-006-0312-7
    • Zollner G, Trauner M. (2006). Molecular mechanisms of cholestasis.Wien Med Wochenschr 156:380-385. (Pubitemid 44182023)
    • (2006) Wiener Medizinische Wochenschrift , vol.156 , Issue.13-14 , pp. 380-385
    • Zollner, G.1    Trauner, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.