Function and organization of the human cytosolic sulfotransferase (SULT) family
Abstract
The sulfuryl transfer reaction is of fundamental biological importance. One of the most important manifestations of this process are the reactions catalyzed by members of the cytosolic sulfotransferase (SULT) superfamily. These enzymes transfer the sulfuryl moiety from the universal donor PAPS (3'-phosphoadenosine 5'-phosphosulfate) to a wide variety of substrates with hydroxyl- or amino-groups. Normally a detoxification reaction this facilitates the elimination of a multitude of xenobiotics, although for some molecules sulfation is a bioactivation step. In addition, sulfation plays a key role in endocrine and other signalling pathways since many steroids, sterols, thyroid hormones and catecholamines exist primarily as sulfate conjugates in humans. This article summarizes much of our current knowledge of the organization and function of the human cytosolic sulfotransferases and highlights some of the important interspecies differences that have implications for, among other things, drug development and chemical safety analysis.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Five cytoplasmic SULTs are involved in the sulfation of steroids in humans: SULT1A1, SULT2E1, SULT2A1 and two isoforms of SULT2B1.
“Five cytoplasmic SULTs are involved in the sulfation of steroids in humans: SULT1A1, SULT2E1, SULT2A1 and two isoforms of SULT2B1 (SULT2B1a and SULT2B1b) [40,165].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [165]
Cites
The Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101 · see citing works
Human Sulfotransferases and Their Role in Chemical Metabolism
Gamage, N., Barnett, A., Hempel, N., Duggleby, R. G., Windmill, K. F., Martin, J. L., & McManus, M. E. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfj061 · Cited by 703 · see citing works
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682 · see citing works
(1997) · PubMed · Cited by 643 · see citing works
Sulfonation and molecular action
Strott, C. A. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0040 · Cited by 487 · see citing works
The Regulation of Steroid Action by Sulfation and Desulfation
Mueller, J. W., Gilligan, L. C., Idkowiak, J., Arlt, W., & Foster, P. A. (2015) · Endocrine Reviews · doi:10.1210/er.2015-1036 · Cited by 419 · see citing works
Kester, M. H. A., Bulduk, S., Tibboel, D., Meinl, W., Glatt, H. R., Falany, C. N., Coughtrie, M. W. H., Bergman, Å., Safe, S. H., Kuiper, G. G. J. M., et al. (2000) · Endocrinology · doi:10.1210/endo.141.5.7530 · Cited by 384 · see citing works
Self-citationRiches, Z., Stanley, E. L., Bloomer, J. C., & Coughtrie, M. W. H. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.028399 · Cited by 365 · see citing works
Self-citationThe importance of 3‘‐phosphoadenosine 5‘‐phosphosulfate (PAPS) in the regulation of sulfation
Klaassen, C. D., & Boles, J. W. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.6.9194521 · Cited by 357 · see citing works
Park-Chung, M., Malayev, A., Purdy, R. H., Gibbs, T. T., & Farb, D. H. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01381-5 · Cited by 354 · see citing works
A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily
Blanchard, R. L., Freimuth, R. R., Buck, J., Weinshilboum, R. M., & Coughtrie, M. W. H. (2004) · Pharmacogenetics · doi:10.1097/00008571-200403000-00009 · Cited by 320 · see citing works
Self-citationSulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase
Zhang, H., Varmalova, O., Vargas, F. M., Falany, C. N., & Leyh, T. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10888 · Cited by 223 · see citing works
Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse
Haque, M. F. U., King, L. M., Krakow, D., Cantor, R. M., Rusiniak, M. E., Swank, R. T., Superti‐Furga, A., Haque, S., Abbas, H., Ahmad, W., et al. (1998) · Nature Genetics · doi:10.1038/2458 · Cited by 217 · see citing works
Structural and Chemical Profiling of the Human Cytosolic Sulfotransferases
Allali‐Hassani, A., Pan, P. W., Dombrovski, L., Najmanovich, R., Tempel, W., Dong, A., Loppnau, P., Martin, F. A., Thonton, J., Edwards, A. M., et al. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050097 · Cited by 217 · see citing works
Role of sulfation in thyroid hormone metabolism
Visser, T. J. (1994) · Chemico-Biological Interactions · doi:10.1016/0009-2797(94)90071-x · Cited by 209 · see citing works
The role of drug metabolizing enzymes in clearance
Di, L. (2014) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2014.876006 · Cited by 208 · see citing works
Sulfation through the looking glass—recent advances in sulfotransferase research for the curious
Coughtrie, M. W. H. (2002) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500117 · Cited by 202 · see citing works
Self-citationTissue Distribution and Ontogeny of Sulfotransferase Enzymes in Mice
Alnouti, Y., & Klaassen, C. D. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl050 · Cited by 201 · see citing works
STROTT, C. A. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-6-670 · Cited by 200 · see citing works
Human phenol sulfotransferases SULT1A2 and SULT1A1
Raftogianis, R. B., Wood, T. C., & Weinshilboum, R. M. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00145-8 · Cited by 198 · see citing works
Kester, M. H. A., Bulduk, S., van Toor, H., Tibboel, D., Meinl, W., Glatt, H., Falany, C. N., Coughtrie, M. W. H., Schuur, A. G., Brouwer, A., et al. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.3.1142 · Cited by 182 · see citing works
Self-citationIdentification and localization of soluble sulfotransferases in the human gastrointestinal tract
Teubner, W., Meinl, W., Florian, S., Kretzschmar, M., & Glatt, H. R. (2007) · Biochemical Journal · doi:10.1042/bj20061431 · Cited by 170 · see citing works
Inactivating <i>PAPSS2</i> Mutations in a Patient with Premature Pubarche
Noordam, C., Dhir, V., McNelis, J. C., Schlereth, F., Hanley, N. A., Krone, N., Smeitink, J. A., Smeets, R., Sweep, F. C. G. J., Grinten, H. L. C.-V. D., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810489 · Cited by 169 · see citing works
Molecular enzymology of human liver cytosolic sulfotransferases
Falany, C. N. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90566-b · Cited by 158 · see citing works
X-ray Crystal Structure of Human Dopamine Sulfotransferase, SULT1A3
Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. M., Modi, S. P., Hersey, A., Taskinen, J., Cooke, R. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37862 · Cited by 158 · see citing works
Self-citationKester, M. H. A., Bulduk, S., van Toor, H., et al. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.87.3.8311 · Cited by 132 · see citing works
Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain
Falany, C. N., Xie, X., Wang, J., FERRER, J., & Falany, J. L. (2000) · Biochemical Journal · doi:10.1042/bj3460857 · Cited by 127 · see citing works
Javitt, N. B., Lee, Y. C., Shimizu, C., Fuda, H., & Strott, C. A. (2001) · Endocrinology · doi:10.1210/endo.142.7.8244 · Cited by 126 · see citing works
Qian, Y., Sun, X., Tong, M. H., Li, X. P., Richa, J., & Song, W. (2001) · Endocrinology · doi:10.1210/endo.142.12.8540 · Cited by 124 · see citing works
Defect in 3'-phosphoadenosine 5'-phosphosulfate formation in brachymorphic mice.
Sugahara, K., & Schwartz, N. B. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.12.6615 · Cited by 124 · see citing works
Demyan, W. F., Song, C. S., Kim, D. S., Her, S., Gallwitz, W., Rao, T. R., Słomczyńska, M., Chatterjee, B., & Roy, A. K. (1992) · Molecular Endocrinology · doi:10.1210/mend.6.4.1374839 · Cited by 117 · see citing works
Nagata, K., Ozawa, S., Miyata, M., Shimada, M., Gong, D., Yamazoe, Y., & Kato, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74524-4 · Cited by 116 · see citing works
Barker, E. V., Hume, R., Hallas, A., & Coughtrie, M. W. H. (1994) · Endocrinology · doi:10.1210/endo.134.2.8299591 · Cited by 115 · see citing works
Self-citationThe dimerization motif of cytosolic sulfotransferases
Petrotchenko, E. V., Pedersen, L. C., Borchers, C. H., Tomer, K. B., & Negishi, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02129-9 · Cited by 115 · see citing works
Sulfated steroids as endogenous neuromodulators
Gibbs, T. T., Russek, S. J., & Farb, D. H. (2006) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2006.07.031 · Cited by 114 · see citing works
DeBaun, J. R., Rowley, J., Miller, E. C., & MILLER, J. A. (1968) · Experimental Biology and Medicine · doi:10.3181/00379727-129-33301 · Cited by 114 · see citing works
Stanley, E. L., Hume, R., & Coughtrie, M. W. H. (2005) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.06.003 · Cited by 111 · see citing works
Self-citationSpontaneous fetal loss caused by placental thrombosis in estrogen sulfotransferase-deficient mice
Tong, M. H., Jiang, H., Liu, P., Lawson, J. A., Brass, L. F., & Song, W.-C. (2005) · Nature Medicine · doi:10.1038/nm1184 · Cited by 110 · see citing works
Meloche, C. A., & Falany, C. N. (2001) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(01)00064-4 · Cited by 102 · see citing works
Dajani, R., Hood, A. M., & Coughtrie, M. W. H. (1998) · Molecular Pharmacology · doi:10.1124/mol.54.6.942 · Cited by 98 · see citing works
Self-citationDopamine sulphate: an enigma resolved.
Eisenhofer, G., Coughtrie, M. W. H., & Goldstein, D. S. (1999) · PubMed · Cited by 93 · see citing works
Self-citationSteroid sulfatase deficiency and x-linked ichthyosis
Shapiro, L. J. (1979) · Clinical Biochemistry · doi:10.1016/s0009-9120(79)80096-x · Cited by 93 · see citing works
Regulation of MCF-7 Breast Cancer Cell Growth by β-estradiol Sulfation
Falany, J. L., Macrina, N., & Falany, C. N. (2002) · Breast Cancer Research and Treatment · doi:10.1023/a:1016147004188 · Cited by 92 · see citing works
Jetten, A. M., George, M. A., Nervi, C., Boone, L. R., & Rearick, J. I. (1989) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12276731 · Cited by 91 · see citing works
Freimuth, R. R., Wiepert, M., Chute, C. G., Wieben, E. D., & Weinshilboum, R. M. (2003) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500223 · Cited by 91 · see citing works
Rubin, G. L. (1999) · Molecular Human Reproduction · doi:10.1093/molehr/5.11.995 · Cited by 88 · see citing works
Stanley, E. L., Hume, R., Visser, T. J., & Coughtrie, M. W. H. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.12.8081 · Cited by 85 · see citing works
Self-citationTissue-specific expression of rat sulfotransferase messenger RNAs.
Dunn, R. T., & Klaassen, C. D. (1998) · PubMed · Cited by 82 · see citing works
Sulfotransferase-mediated activation of mutagens studied using heterologous expression systems
Glatt, H. R., Bartsch, I., Christoph, S., Coughtrie, M. W. H., Falany, C. N., Hagen, M., Landsiedel, R., Pabel, U., Phillips, D. H., Seidel, A., et al. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00133-6 · Cited by 82 · see citing works
Self-citationOostdijk, W., Idkowiak, J., Mueller, J. W., House, P. J., Taylor, A. E., O'Reilly, M. W., Hughes, B. A., de Vries, M. C., Kant, S. G., Santen, G. W. E., et al. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-3556 · Cited by 81 · see citing works
Sulfation of Thyroid Hormone by Estrogen Sulfotransferase
Kester, M. H. A., van Dijk, C. H., Tibboel, D., Hood, A. M., Rose, N. J. M., Meinl, W., Pabel, U., Glatt, H. R., Falany, C. N., Coughtrie, M. W. H., et al. (1999) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.84.7.5975 · Cited by 78 · see citing works
Self-citationRegulation of sulfotransferase mRNA expression in male and female rats of various ages
Klaassen, C. D., Liu, L., & Dunn, R. T. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00141-5 · Cited by 77 · see citing works
Arlt, V. M., Glatt, H. R., Muckel, E., Pabel, U., Sorg, B. L., Seidel, A., Frank, H., Schmeiser, H. H., & Phillips, D. H. (2003) · International Journal of Cancer · doi:10.1002/ijc.11143 · Cited by 75 · see citing works
Taskinen, J., Ethell, B. T., Pihlavisto, P., Hood, A. M., Burchell, B., & Coughtrie, M. W. H. (2003) · Drug Metabolism and Disposition · doi:10.1124/dmd.31.9.1187 · Cited by 63 · see citing works
Self-citationRen, S., & Ning, Y. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00552.2013 · Cited by 59 · see citing works
Pregnenolone sulfate as a modulator of synaptic plasticity
Smith, C. C., Gibbs, T. T., & Farb, D. H. (2014) · Psychopharmacology · doi:10.1007/s00213-014-3643-x · Cited by 58 · see citing works
Sulfation of tibolone and tibolone metabolites by expressed human cytosolic sulfotransferases
Falany, J. L., Macrina, N., & Falany, C. N. (2004) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.01.005 · Cited by 56 · see citing works
SULT2B1: unique properties and characteristics of a hydroxysteroid sulfotransferase family
Falany, C. N., & Rohn‐Glowacki, K. J. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2013.835609 · Cited by 55 · see citing works
Meloche, C. A., Sharma, V., Swedmark, S., Andersson, P., & Falany, C. N. (2002) · Drug Metabolism and Disposition · doi:10.1124/dmd.30.5.582 · Cited by 53 · see citing works
van den Boom, J., Heider, D., Martin, S. R., Pastore, A., & Mueller, J. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325498 · Cited by 50 · see citing works
Senggunprai, L., Yoshinari, K., & Yamazoe, Y. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.027441 · Cited by 48 · see citing works
Molecular Cloning, Expression, and Functional Characterization of Novel Mouse Sulfotransferases
Sakakibara, Y., Yanagisawa, K., Takami, Y., Nakayama, T., Suiko, M., & Liu, M. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8872 · Cited by 47 · see citing works
A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates
Cook, I. T., Wang, T., Falany, C. N., & Leyh, T. S. (2012) · Biochemistry · doi:10.1021/bi300631g · Cited by 45 · see citing works
Paradigms of Sulfotransferase Catalysis
Wang, T., Cook, I. T., Falany, C. N., & Leyh, T. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573501 · Cited by 43 · see citing works
Kiehlbauch, C. C., Lam, Y. F., & Ringer, D. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18941 · Cited by 42 · see citing works
Surh, Y., & MILLER, J. A. (1994) · Chemico-Biological Interactions · doi:10.1016/0009-2797(94)90076-0 · Cited by 37 · see citing works
The fetoplacental unit of primates*
Kuss, E. (2009) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-0029-1211276 · Cited by 36 · see citing works
Molecular Cloning, Expression and Characterization of A Novel Mouse SULT6 Cytosolic Sulfotransferase
Takahashi, S., Sakakibara, Y., Mishiro, E., Kouriki, H., Nobe, R., Kurogi, K., Yasuda, S., Liu, M.-C., & Suiko, M. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp087 · Cited by 33 · see citing works
Borthwick, E. B., Burchell, A. N., & Coughtrie, M. W. H. (1993) · Biochemical Journal · doi:10.1042/bj2890719 · Cited by 32 · see citing works
Self-citationRecent studies on the metabolic activation of chemical carcinogens.
MILLER, J. A. (1994) · PubMed · Cited by 31 · see citing works
Kocarek, T. A., Duanmu, Z., Fang, H., & Runge‐Morris, M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.07.032 · Cited by 29 · see citing works
Surh, Y.-J., Liem, A., Miller, E. C., & Miller, J. A. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90479-o · Cited by 28 · see citing works
He, D., & Falany, C. N. (2006) · Drug Metabolism and Disposition · doi:10.1124/dmd.106.011114 · Cited by 28 · see citing works
Riches, Z., Bloomer, J. C., & Coughtrie, M. W. H. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.04.006 · Cited by 28 · see citing works
Self-citationFord-Hutchinson, A. F., Ali, Z., Seerattan, R. A., Cooper, D. M. L., Hallgrímsson, B., SALO, P. T., & Jirik, F. R. (2005) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2004.12.011 · Cited by 27 · see citing works
Nowell, S. A., Green, B., Tang, Y. M., Wiese, R., & Kadlubar, F. F. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.006171 · Cited by 24 · see citing works
SULT1C3, an orphan sequence of the human genome, encodes an enzyme activating various promutagens
Meinl, W., Donath, C., Schneider, H., Sommer, Y., & Glatt, H. R. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.08.040 · Cited by 22 · see citing works
Meerman, J. H. N., Ringer, D. P., Coughtrie, M. W. H., Bamforth, K. J., & Gilissen, R. (1994) · Chemico-Biological Interactions · doi:10.1016/0009-2797(94)90073-6 · Cited by 21 · see citing works
Self-citationRamsey, T. L., Meltzer, H. Y., Brock, G. N., Mehrotra, B., Jayathilake, K., Bobo, W. V., & Brennan, M. D. (2011) · Pharmacogenomics · doi:10.2217/pgs.10.205 · Cited by 21 · see citing works
Rondini, E. A., Fang, H., Runge‐Morris, M., & Kocarek, T. A. (2013) · Drug Metabolism and Disposition · doi:10.1124/dmd.113.055673 · Cited by 21 · see citing works
Cytosolic Aryl Sulfotransferase 4A1 Interacts with the Peptidyl Prolyl Cis-Trans Isomerase Pin1
Mitchell, D. J., & Minchin, R. F. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.055442 · Cited by 18 · see citing works
Sidharthan, N. P., Butcher, N. J., Mitchell, D. J., & Minchin, R. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101520 · Cited by 17 · see citing works
Phosphorylation/dephosphorylation of human SULT4A1: Role of Erk1 and PP2A
Mitchell, D. J., Butcher, N. J., & Minchin, R. F. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.011 · Cited by 13 · see citing works
Ramsey, T. L., Liu, Q., & Brennan, M. D. (2014) · Pharmacogenomics · doi:10.2217/pgs.14.54 · Cited by 12 · see citing works
Crittenden, F., Thomas, H. R., Ethen, C. M., Wu, Z. L., Chen, D., Kraft, T. W., Parant, J. M., & Falany, C. N. (2014) · Drug Metabolism and Disposition · doi:10.1124/dmd.114.057042 · Cited by 11 · see citing works
Kurogi, K., Sakakibara, Y., 亀元, 洋., Takahashi, S., Yasuda, S., Liu, M., & Suiko, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07781.x · Cited by 8 · see citing works
Induction of hepatic estrogen sulfotransferase expression by hypophysectomy in female rats
Borthwick, E. B., Coughtrie, M. W. H., & Burchell, A. N. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00173-w · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Schiffer, L., Barnard, L., Baranowski, E. S., Gilligan, L. C., Taylor, A. E., Arlt, W., Shackleton, C. H. L., & Storbeck, K.-H. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.105439 · Cited by 450 · see citing works
“Five cytoplasmic SULTs are involved in the sulfation of steroids in humans: SULT1A1, SULT2E1, SULT2A1 and two isoforms of SULT2B1 (SULT2B1a and SULT2B1b) [40,165].”
Xenobiotic metabolism and disposition
Chen, G. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813602-7.00003-x · Cited by 154 · see citing works
Sulfation pathways from red to green
Günal, S., Hardman-Kavanaugh, R. E., Kopřiva, S., & Mueller, J. W. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007422 · Cited by 117 · see citing works
Regulation of coenzyme A levels by degradation: the ‘Ins and Outs’
Naquet, P., Kerr, E. W., Vickers, S. D., & Leonardi, R. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101028 · Cited by 115 · see citing works
The Role of Uptake and Efflux Transporters in the Disposition of Glucuronide and Sulfate Conjugates
Järvinen, E., Deng, F. Y., Kiander, W., Sinokki, A., Kidron, H., & Sjöstedt, N. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.802539 · Cited by 111 · see citing works
Sulfur Metabolism Under Stress
Miller, C. G., & Schmidt, E. E. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8151 · Cited by 74 · see citing works
Age-associated changes of cytochrome P450 and related phase-2 gene/proteins in livers of rats
Xu, S., Hu, A., Xie, L., Liu, J.-J., Wu, Q., & Liu, J. (2019) · PeerJ · doi:10.7717/peerj.7429 · Cited by 66 · see citing works
Understanding the Chemical Exposome During Fetal Development and Early Childhood: A Review
Krausová, M., Braun, D., Buerki-Thurnherr, T., Gundacker, C., Schernhammer, E., Wisgrill, L., & Warth, B. (2023) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-051922-113350 · Cited by 61 · see citing works
SULFATION PATHWAYS: Insights into steroid sulfation and desulfation pathways
Foster, P., & Mueller, J. W. (2018) · Journal of Molecular Endocrinology · doi:10.1530/jme-18-0086 · Cited by 57 · see citing works
Isvoran, A., Peng, Y., Ceauranu, S., Schmidt, L., Nicot, A. B., & Miteva, M. A. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.103349 · Cited by 47 · see citing works
Systems pharmacology of hepatic metabolism in zebrafish larvae
van Wijk, R. C., Krekels, E. H. J., Hankemeier, T., Spaink, H. P., & van der Graaf, P. H. (2016) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2017.04.003 · Cited by 46 · see citing works
Sulfonation, an underexploited area: from skeletal development to infectious diseases and cancer
Leung, A. W. Y., Backstrom, I., & Bally, M. B. (2016) · Oncotarget · doi:10.18632/oncotarget.10046 · Cited by 45 · see citing works
Histone tyrosine sulfation by SULT1B1 regulates H4R3me2a and gene transcription
Yu, W., Zhou, R., Li, N., Lei, Z.-C., Guo, D., Peng, F., Li, Y., Bai, X., Feng, S., Wang, Y., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01267-9 · Cited by 40 · see citing works
Mueller, J. W., Idkowiak, J., Gesteira, T. F., Vallet, C., Hardman-Kavanaugh, R. E., van den Boom, J., Dhir, V., Knauer, S. K., Rosta, E., & Arlt, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002248 · Cited by 39 · see citing works
Datta, P., Fu, L., He, W., Koffas, M. A. G., Dordick, J. S., & Linhardt, R. J. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10709-6 · Cited by 37 · see citing works
Skeletal Dysplasias Caused by Sulfation Defects
Paganini, C., Tota, C. G., Superti‐Furga, A., & Rossi, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082710 · Cited by 39 · see citing works
The effects of fasting on drug metabolism
Lammers, L. A., Achterbergh, R., Mathôt, R. A. A., & Romijn, J. A. (2020) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2020.1706728 · Cited by 32 · see citing works
Takahashi, K., Yoshino, T., Maki, Y., Ishiuchi, K., Namiki, T., Ogawa‐Ochiai, K., Minamizawa, K., Makino, T., Nakamura, T., Mimura, M., et al. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02588-2 · Cited by 32 · see citing works
Adaptive modifications in plant sulfur metabolism over evolutionary time
Kopřiva, S., Karvansara, P. R., & Takahashi, H. (2024) · Journal of Experimental Botany · doi:10.1093/jxb/erae252 · Cited by 31 · see citing works
Parker, V. S., Squirewell, E. J., Lehmler, H., Robertson, L. W., & Duffel, M. W. (2018) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2018.01.010 · Cited by 31 · see citing works
Cytochrome P450 and Other Drug-Metabolizing Enzymes As Therapeutic Targets
Foti, R. (2023) · Drug Metabolism and Disposition · doi:10.1124/dmd.122.001011 · Cited by 30 · see citing works
Zhou, Y., Zhao, Y., Xu, R., & Pan, L. (2020) · Environmental Research · doi:10.1016/j.envres.2020.109980 · Cited by 29 · see citing works
Carcinogenic Polycyclic Aromatic Hydrocarbons
Murray, J. R., & Penning, T. M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95691-5 · Cited by 28 · see citing works
Nishikawa, M., Masuyama, Y., Nunome, M., Yasuda, K., Sakaki, T., & Ikushiro, S. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8621-x · Cited by 27 · see citing works
The role of xenobiotic-metabolizing enzymes in the placenta: a growing research field
Blanco‐Castañeda, R., Galavíz-Hernández, C., Souto, P. C. D. S., Lima, V. V., Giachini, F. R. C., Escudero, C., Damiano, A. E., Barragán‐Zuñiga, L. J., Martínez‐Aguilar, G., & Sosa‐Macías, M. (2020) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2020.1733412 · Cited by 28 · see citing works
Pedersen, L. C., Yi, M., Pedersen, L. G., & Kaminski, A. M. (2022) · Drug Metabolism and Disposition · doi:10.1124/dmd.121.000478 · Cited by 25 · see citing works
The Importance of Tracking “Missing” Metabolites: How and Why?
Wang, S., Ballard, T. E., Christopher, L. J., Foti, R., Gu, C., Khojasteh, S. C., Liu, J., Ma, S., Ma, B., Obach, R. S., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01293 · Cited by 25 · see citing works
Marto, N., Morelló, J., Monteiro, E. C., & Pereira, S. A. (2017) · Drug Metabolism Reviews · doi:10.1080/03602532.2017.1335749 · Cited by 25 · see citing works
Burton, N. O., Dwivedi, V. K., Burkhart, K. B., Kaplan, R. E. W., Baugh, L. R., & Horvitz, H. R. (2018) · Nature Communications · doi:10.1038/s41467-018-07640-w · Cited by 24 · see citing works
Xie, L., Xiao, D., Wang, X., Wang, C., Bai, J., Yue, Q., Yue, H., Li, Y., Molnár, I., Xu, Y., et al. (2020) · mSphere · doi:10.1128/msphere.00949-20 · Cited by 24 · see citing works
Ghosh, D. (2023) · Steroids · doi:10.1016/j.steroids.2023.109249 · Cited by 23 · see citing works
Identification of Human Sulfotransferases Active towards Silymarin Flavonolignans and Taxifolin
Vrba, J., Papoušková, B., Kosina, P., Lněničková, K., Valentová, K., & Jitka Ulrichová, A. (2020) · Metabolites · doi:10.3390/metabo10080329 · Cited by 22 · see citing works
Brinkman, M. C., Teferra, A. A., Kassem, N. O., & Kassem, N. O. F. (2019) · Tobacco Control · doi:10.1136/tobaccocontrol-2019-054961 · Cited by 22 · see citing works
Alternative pathways for vitamin D metabolism
Slominski, A. T., Tuckey, R. C., Jenkinson, C., Li, W., & Jetten, A. M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91386-7.00001-5 · Cited by 21 · see citing works
Li, D., Knox, B., Chen, S., Wu, L., Tolleson, W. H., Liu, Z., Yu, D., Guo, L., Tong, W., & Ning, B. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.08.019 · Cited by 21 · see citing works
Mechanisms by Which Inducers of Drug Metabolizing Enzymes Alter Thyroid Hormones in Rats
Vansell, N. R. (2022) · Drug Metabolism and Disposition · doi:10.1124/dmd.121.000498 · Cited by 20 · see citing works
Evolution and multiple functions of sulfonation and cytosolic sulfotransferases across species
Kurogi, K., Suiko, M., & Sakakibara, Y. (2024) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbae008 · Cited by 20 · see citing works
Sulfation modification of dopamine in brain regulates aggregative behavior of animals
Chen, B., Tong, X., Zhang, X., Gui, W., Ai, G., Huang, L., Ding, D., Zhang, J., & Kang, L. (2021) · National Science Review · doi:10.1093/nsr/nwab163 · Cited by 18 · see citing works
den Braver-Sewradj, S. P., den Braver, M. D., van Dijk, M. V., Zhang, Y.-J., Dekker, S. J., Wijaya, L., Vermeulen, N. P. E., Richert, L., Commandeur, J., & Vos, J. C. (2018) · Current drug metabolism · doi:10.2174/1389200219666180108160046 · Cited by 14 · see citing works
Sun, Y., Machalz, D., Wolber, G., Parr, M. K., & Bureik, M. (2020) · Biomolecules · doi:10.3390/biom10111517 · Cited by 17 · see citing works
Huang, Y., & Xu, B. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.141790 · Cited by 16 · see citing works
Metabolic Activation and Cytotoxicity of Labetalol Hydrochloride Mediated by Sulfotransferases
Yang, L., Xin, L., Shi, J., Li, W., Tian, M., Hu, Z., Peng, Y., & Zheng, J. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.1c00060 · Cited by 15 · see citing works
Yin, M., Lu, J., Guo, Z., Zhang, Y., Liu, J., Wu, T., Guo, K., Luo, T., & Guo, Z. (2021) · Aging · doi:10.18632/aging.202273 · Cited by 15 · see citing works
Complex roles for sulfation in the toxicities of polychlorinated biphenyls
Duffel, M. W., & Lehmler, H. (2024) · Critical Reviews in Toxicology · doi:10.1080/10408444.2024.2311270 · Cited by 13 · see citing works
Shimels, M. Z., Rendine, S., Ruyter-Spira, C. P., Rich, P. J., Ejeta, G., & Bouwmeester, H. J. (2024) · Plants People Planet · doi:10.1002/ppp3.10549 · Cited by 14 · see citing works
Steroid sulfates in domestic mammals and laboratory rodents
Schuler, G. C. (2021) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2021.106622 · Cited by 13 · see citing works
Cytosolic sulfotransferases in endocrine disruption
Duffel, M. W. (2024) · Essays in Biochemistry · doi:10.1042/ebc20230101 · Cited by 12 · see citing works
The Role of Sulfation in Nematode Development and Phenotypic Plasticity
Igreja, C., & Sommer, R. J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.838148 · Cited by 11 · see citing works
Potential Involvement of Sulfotransferase in the Mechanism of Lamotrigine-induced Skin Rash
Cao, Y., Bairam, A. F., Liu, M., & Uetrecht, J. (2023) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.3c00187 · Cited by 12 · see citing works
Pharmacogenetics/Pharmacogenomics of Drug-Metabolizing Enzymes and Transporters
Arbitrio, M., Scionti, F., Martino, M. T. D., Pensabene, L., Tassone, P., & Tagliaferri, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00013-x · Cited by 12 · see citing works
Enzyme Kinetics of PAPS-Sulfotransferase
James, M. O. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1554-6_11 · Cited by 12 · see citing works
Chen, F., Li, D.-Y., Zhang, B., Sun, J., Sun, F., Ji, X., Qiu, J., Parker, R. B., Laizure, S. C., & Xu, J. (2018) · Drug Metabolism Reviews · doi:10.1080/03602532.2018.1497645 · Cited by 12 · see citing works
Mei, X., Gohal, S. A., Alatwi, E. S., Hui, Y., Yang, C., Song, Y., Zhou, C., & Liu, M. (2021) · Planta Medica · doi:10.1055/a-1351-0618 · Cited by 11 · see citing works
Recent developments in predicting CYP-independent metabolism
Dhuria, N. V., Haro, B., Kapadia, A. K. B., Lobo, K. A., Matusow, B., Schleiff, M. A., Tantoy, C., & Sodhi, J. K. (2021) · Drug Metabolism Reviews · doi:10.1080/03602532.2021.1923728 · Cited by 11 · see citing works
Inhibition of hydroxylated polychlorinated biphenyls (OH-PCBs) on sulfotransferases (SULTs)
Jia, R.-Y., Zhang, Z., Qin, G.-Q., Zhang, W., Yang, K., Liu, Y., Jiang, C., & Fang, Z. (2021) · Environmental Pollution · doi:10.1016/j.envpol.2021.118214 · Cited by 11 · see citing works
A simple method to measure sulfonation in man using paracetamol as probe drug
Marto, N., Morelló, J., Antunes, A. M. M., Lopes, S. A., Monteiro, E. C., & Pereira, S. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-88393-3 · Cited by 10 · see citing works
Intracellular spatiotemporal metabolism in connection to target engagement
Zhang, J., Qiu, Z., Zhang, Y. J., Wang, G., & Hao, H. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115024 · Cited by 10 · see citing works
Xu, X., Meng, X., Zhang, N., Jiang, H., Ge, H., Qian, K., & Wang, J. (2021) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2021.104905 · Cited by 10 · see citing works
Drug Metabolism: Phase II Enzymes
James, M. O. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00123-7 · Cited by 10 · see citing works
Inhibition of Human Sulfotransferases by Phthalate Monoesters
Huang, H., Lan, D., Zhang, Y., Fan, X.-J., Hu, M.-C., Qin, G.-Q., Wang, F.-G., Wu, Y., Zheng, T., & Liu, J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.868105 · Cited by 10 · see citing works
Singularities of nevirapine metabolism: from sex-dependent differences to idiosyncratic toxicity
Marinho, A. T., Miranda, J. P., Caixas, U., Charneira, C., Dias, C. G., Marques, M. M., Monteiro, E. C., Antunes, A. M. M., & Pereira, S. A. (2019) · Drug Metabolism Reviews · doi:10.1080/03602532.2019.1577891 · Cited by 10 · see citing works
Insight Into the Salivary Secretome of Varroa destructor and Salivary Toxicity to Apis cerana
Zhang, Y., & Han, R. (2018) · Journal of Economic Entomology · doi:10.1093/jee/toy224 · Cited by 10 · see citing works
Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment
Brylski, O., Ebbinghaus, S., & Mueller, J. W. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00031 · Cited by 10 · see citing works
Xie, C., Hu, W., Gan, L., Fu, B., Zhao, X., Tang, D., Liao, R., & Ye, L. (2022) · Metabolites · doi:10.3390/metabo12090870 · Cited by 9 · see citing works
Kondo, M., Ikenaka, Y., Nakayama, S. M. M., Kawai, Y. K., Mizukawa, H., Mitani, Y., Nomiyama, K., Tanabe, S., & Ishizuka, M. (2022) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2022.109476 · Cited by 9 · see citing works
Aromatase and steroid sulfatase from human placenta
Ghosh, D. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.04.025 · Cited by 9 · see citing works
Weththasinghe, S. A., Waller, C. C., Fam, H. L., Stevenson, B. J., Cawley, A., & McLeod, M. D. (2017) · Drug Testing and Analysis · doi:10.1002/dta.2224 · Cited by 9 · see citing works
Fitch, W. L., Smith, S. M., Saporito, M. S., Busse, G., Zhang, M., Ren, J., Fitzsimmons, M. E., Yi, P. C., English, S., Carter, A. N., et al. (2023) · Drug Metabolism and Disposition · doi:10.1124/dmd.122.001218 · Cited by 9 · see citing works
Role of drug-metabolizing enzymes in biotransformation of drugs
Yaqoob, A., Rehman, Q., Rehman, K., Akash, M. S. H., Hussain, I., & Ahmad, R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-95120-3.00013-0 · Cited by 8 · see citing works
Liao, L., Liu, Z., Liu, L., Huang, C., Li, Y., Mao, C., Xu, R., Liu, H., Liu, C., Peng, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57330-7 · Cited by 8 · see citing works
Identification and evolution of the plant sulfotransferase family
Han, S.-M., Chen, Z., Liu, Q., Yueying, D., Wang, J., Liu, H., Zou, J., Hong, Z., Zhang, H., Yang, W., et al. (2025) · BMC Genomics · doi:10.1186/s12864-025-12117-4 · Cited by 8 · see citing works
Wang, K., Chan, Y.-C., So, P., Liu, X., Lu, F., Cheung, W., Lee, S. S. T., & Au, S. W. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100074 · Cited by 8 · see citing works
Zhang, L., Song, W., Li, T., Mu, Y., Zhang, P., Hu, J., Lin, H., Zhang, J., Gao, H. F., & Zhang, L. (2023) · Structure · doi:10.1016/j.str.2023.04.012 · Cited by 8 · see citing works
Sterol Sulfates and Sulfotransferases in Marine Diatoms
Gallo, C., Nuzzo, G., d’Ippolito, G., Manzo, E., Sardo, A., & Fontana, A. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.03.003 · Cited by 8 · see citing works
Metabolic Biomarkers of Red Beetroot Juice Intake at Rest and after Physical Exercise
Giampaoli, O., Ieno, C., Sciubba, F., Spagnoli, M., Miccheli, A., Tomassini, A., Aureli, W., & Fattorini, L. (2023) · Nutrients · doi:10.3390/nu15092026 · Cited by 8 · see citing works
Nomoto, H., Maehashi, H., Shirai, M., Nakamura, M., Masaki, T., Mezaki, Y., Park, J., Aizawa, M., Ohkawa, K., Yoshida, K., et al. (2018) · Human Cell · doi:10.1007/s13577-018-0218-x · Cited by 8 · see citing works
Hansson, P., Blacker, C., Uvdal, H., Wadelius, M., Gréen, H., & Ljungman, G. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.104720 · Cited by 7 · see citing works
The impact of inactivation of the GH/IGF axis during aging on healthspan
Poudel, S. B., Ruff, R. R., He, Z., Dixit, M., Yildirim, G., Jayarathne, H. S. M., Manchanayake, D. H., Basta‐Pljakic, J., Duran‐Ortiz, S., Schaffler, M. B., et al. (2024) · GeroScience · doi:10.1007/s11357-024-01426-3 · Cited by 7 · see citing works
Changes in the Serum Metabolome of Patients Treated With Broad-Spectrum Antibiotics
Jaskiw, G. E., Obrenovich, M. E., Kundrapu, S., & Donskey, C. J. (2020) · Pathogens and Immunity · doi:10.20411/pai.v5i1.394 · Cited by 7 · see citing works
Peng, H., Feng, K., Jia, W., Li, Y., Lv, Q., & Zhang, Y. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01938-5 · Cited by 6 · see citing works
Yamauchi, K., Katsumata, S., & Ozaki, M. (2019) · Genes & Genetic Systems · doi:10.1266/ggs.19-00026 · Cited by 6 · see citing works
Liu, T., Zhang, X., Zhang, Y., Hou, J., Fang, D., Sun, H., Li, Q., & Xie, S. (2018) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2018.08.041 · Cited by 6 · see citing works
Close, R., Kremer, S., Mitchem, M., Bellinghiere, A., Nirmalkar, K., Borges, C. R., Krajmalnik‐Brown, R., & Shah, D. D. (2025) · PNAS Nexus · doi:10.1093/pnasnexus/pgaf403 · Cited by 5 · see citing works
Soprano, L. L., Ferrero, M. R., Jacobs, T., Couto, A. S., & Duschak, V. G. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1028496 · Cited by 5 · see citing works
Hwang, D.-K., Kim, J., Shin, Y., Choi, W.-G., Kim, S., Cho, Y., Lee, J. Y., Kang, H. C., & Lee, H. S. (2019) · Pharmaceutics · doi:10.3390/pharmaceutics11070355 · Cited by 5 · see citing works
Vicedomini, R., Righetti, N., Polit, L., Condémi, S., Longo, L., & Carbone, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.30.466563 · Cited by 5 · see citing works
Niu, X., Fan, Y., Chen, L., Deng, Y., Hao, Y., Zhu, G., Wang, L., Zhou, Q., Zhou, Q., & Ge, G. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.111204 · Cited by 4 · see citing works
Kurogi, K., Sakakibara, Y., Hashiguchi, T., Kakuta, Y., Kanekiyo, M., Teramoto, T., Fukushima, T., Bamba, T., Matsumoto, J., Fukusaki, E., et al. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae097 · Cited by 4 · see citing works
Vrba, J., Papoušková, B., Lněničková, K., Kosina, P., Vladimír Křen, A., & Jitka Ulrichová, A. (2021) · Antioxidants · doi:10.3390/antiox10060954 · Cited by 4 · see citing works
Maiti, S., MaitiDutta, S., & Chen, G. (2021) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000001155 · Cited by 4 · see citing works
Computational Analysis of Chemical Space of Natural Compounds Interacting with Sulfotransferases
Lessigiarska, I., Peng, Y., Tsakovska, I., Alov, P., Lagarde, N., Jereva, D., Villoutreix, B. O., Nicot, A. B., Pajeva, I. K., Pencheva, T., et al. (2021) · Molecules · doi:10.3390/molecules26216360 · Cited by 4 · see citing works
Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats
Bebová, M., Boštíková, Z., Moserová, M., Pávek, P., Anzenbacherová, E., Stiborová, M., & Hodek, P. (2017) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-017-2007-8 · Cited by 4 · see citing works
Chen, W., Li, Z., Liu, T., Lyu, Q., & Liu, W. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c02656 · Cited by 3 · see citing works
Mashirin, R., & Chitra, K. C. (2025) · Journal of Applied Toxicology · doi:10.1002/jat.4772 · Cited by 3 · see citing works
Mei, X., Gohal, S. A., Zhou, C., & Liu, M. (2022) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2022.2047030 · Cited by 3 · see citing works
Duffel, M. W. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00005-x · Cited by 3 · see citing works
Carbohydrate sulfotransferases in glycosaminoglycan biosynthesis
Barone, D., Joshi, L., & Kilcoyne, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-819655-7.00013-8 · Cited by 3 · see citing works
Sulfotransferase 4A1 Coding Sequence and Protein Structure Are Highly Conserved in Vertebrates
van Waardenburg, R. C. A. M., & Falany, C. N. (2024) · Genes · doi:10.3390/genes15070914 · Cited by 3 · see citing works
Juvonen, R. O., Pentikäinen, O. T., Huuskonen, J., Timonen, J. M., Kärkkäinen, O. K., Heikkinen, A. T., Fashe, M. M., & Raunio, H. (2020) · Xenobiotica · doi:10.1080/00498254.2020.1711544 · Cited by 3 · see citing works
Shen, F., Wen, H., Shan, C., An, K., Dong, B., Chai, C., Zhang, J., Zhang, Q., & Li, W. (2018) · Journal of Chromatography B · doi:10.1016/j.jchromb.2018.04.048 · Cited by 3 · see citing works
- Authors
- Coughtrie, M. W. H.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Coughtrie, Michael W.H.
- Venue
- Chemico-Biological Interactions
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 259
- Issue
- Pt A
- Pages
- 2-7
- ISSN
- 0009-2797 (ISSN-L)
- OpenAlex
- W2346100651
- Cited by
- 142
- References
- 86
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 14 · 2023: 19 · 2022: 14 · 2021: 19 · 2020: 13 · 2019: 18 · 2018: 12 · 2017: 8 · 2016: 3
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemico-Biological Interactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- cytosolic sulfotransferases, sulfation, PAPS, xenobiotic detoxification, metabolic activation, species differences, drug development, chemical safety
- MeSH terms
- Humans, Inactivation, Metabolic, Phosphoadenosine Phosphosulfate, Substrate Specificity, Sulfates, Sulfotransferases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review