References
- Bauman E. Ueber sulfosauren im harn. Ber Dtsch Chem Ges. 1876;54-58(German).
- Nelson SD, Gordon WP. Mammalian drug metabolism. J Nat Prod. 1983;46(1):71–78.
- Chen X, Zhong D, Blume H. Stereoselective pharmacokinetics of propafenone and its major metabolites in healthy Chinese volunteers. Eur J Pharm Sci. 2000;10(1):11–16.
- Blanchard RL, Freimuth RR, Buck J, et al.. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics. 2004;14(3):199–211. DOI:https://doi.org/10.1097/00008571-200403000-00009.
- Reiter C, Mwaluko G, Dunnette J, et al.. Thermolabile and thermostable human platelet phenol sulfotransferase.Substrate specificity and physical separation. Naunyn Schmiedebergs Arch Pharmacol. 1983;324(2):140–147.
- Young JWF, Okazaki H, Laws JER, et al.. Human brain phenol sulfotransferase: biochemical properties and regional localization. J Neurochem. 1984;43(3):706–715.
- Falany CN. Enzymology of human cytosolic sulfotransferases. FASEB J. 1997;11(4):206–216.
- Raftogianis RB, Wood TC, Otterness DM, et al.. Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype. Biochem Biophys Res Commun. 1997;239(1):298–304.
- Raftogianis RB, Wood TC, Weinshilboum RM. Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations. Biochem Pharmacol. 1999;58(4):605–616.
- Thomae BA, Rifki OF, Theobald MA, et al.. Human catecholamine sulfotransferase (SULT1A3) pharmacogenetics: functional genetic polymorphism. J Neurochem. 2003;87(4):809–819.
- Freimuth RR, Eckloff B, Wieben ED, et al.. Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies. Pharmacogenetics. 2001;11(9):747–756.
- Adjei AA, Thomae BA, Prondzinski JL, et al.. Human estrogen sulfotransferase (SULT1E1) pharmacogenomics: gene resequencing and functional genomics. Br J Pharmacol. 2003;139(8):373–1382.
- Aksoy IA, Wood TC, Weinshilboum R. Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem Biophys Res Commun. 1994;16;200(3):1621–1629.
- Liu TA, Bhuiyan S, Liu MY, et al.. Zebrafish as a model for the study of the phase II cytosolic sulfotransferases. Curr Drug Metab. 2010;11(6):538–546. DOI:https://doi.org/10.2174/138920010791636158.
- Freimuth RR, Wiepert M, Chute CG, et al., Human cytosolic sulfotransferase database mining: identification of seven novel genes and pseudogenes. Pharmacogenomics J. (2004)(4): 54–65. 2004. DOI:https://doi.org/10.1038/sj.tpj.6500223.
- Hildebrandt MA, Salavaggione OE, Martin YN, et al.. Human SULT1A3 pharmacogenetics: gene duplication and functional genomic studies. Biochem Biophys Res Commun. 2004;321(4):870–878. DOI:https://doi.org/10.1016/j.bbrc.2004.07.038.
- Veronese ME, Burgess W, Zhu X, et al.. Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitorsensitivity studies. Biochem J. 1994;302(2):497–502. DOI:https://doi.org/10.1042/bj3020497.
- Sugahara T, Pai TG, Suiko M, et al.. Differential roles of human monoamine (M)-form and simple phenol (P)-form phenol sulfotransferases in drug metabolism. J Biochem. 2003;133(2):259–262. DOI:https://doi.org/10.1093/jb/mvg033.
- Buhl AE, Waldon DJ, Baker CA, et al.. Minoxidil sulfate is the active metabolite that stimulates hair follicles. J Invest Dermatol. 1990;95(5):553–557. DOI:https://doi.org/10.1111/1523-1747.ep12504905.
- Fujita KI, Nagata K, Yamazaki T, et al.. Enzymatic characterization of human cytosolic sulfotransferases: identification of ST1B2 as a thyroid hormone sulfotransferase. Biol Pharm Bull. 1999;22(5):446–452. DOI:https://doi.org/10.1248/bpb.22.446.
- Wang J, Falany JL, Falany CN. Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver. Mol Pharmacol. 1999;53(2):274–282.
- Sakakibara Y, Takami Y, Zwieb C, et al.. Purification, characterization, and molecular cloning of a novel rat liver Dopa/tyrosine sulfotransferase. J Biol Chem. 1995;270(51):30470–30478. DOI:https://doi.org/10.1074/jbc.270.51.30470.
- Wu SY, Green WL, Huang WS, et al.. Alternate pathways of thyroid hormone metabolism. Thyroid. 2005;15(8):943–958. DOI:https://doi.org/10.1089/thy.2005.15.943.
- Sakakibara Y, Yanagisawa K, Katafuchi J, et al.. Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J Biol Chem. 1998;273(51):33929–33935. DOI:https://doi.org/10.1074/jbc.273.51.33929.
- Meinl W, Donath C, Schneider H, et al.. SULT1C3, an orphan sequence of the human genome, encodes an enzyme activating various promutagens. Food Chem Toxicol. 2008;46(4):1249–1256. DOI:https://doi.org/10.1016/j.fct.2007.08.040.
- Meinl W, Ebert B, Glatt H, et al.. Sulfotransferase Forms Expressed in Human Intestinal Caco-2 and TC7 Cells at Varying Stages of Differentiation and Role in Benzo[a]pyrene Metabolism. Drug Metab Dispos. 2008;36(2):276–283.
- Allali-Hassani A, Pan PW, Dombrovski L, et al.. Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol. 2007;5(5):e97. DOI:https://doi.org/10.1371/journal.pbio.0050097.
- Li X, Clemens DL, Anderson RJ. Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1). Biochem Pharmacol. 2000;60(11):1713–1716.
- Hui Y, Luo L, Zhang L, et al.. Sulfation of afimoxifene, endoxifen, raloxifene, and fulvestrant by the human cytosolic sulfotransferases (SULTs): A systematic analysis. J Pharmacol Sci. 2015;128(3):144–149. DOI:https://doi.org/10.1016/j.jphs.2015.06.004.
- Luo L, Zhou C, Hui Y, et al.. Human cytosolic sulfotransferase SULT1C4 mediates the sulfation of doxorubicin and epirubicin. Drug Metab Pharmacokinet. 2016;31(2):163–166. DOI:https://doi.org/10.1016/j.dmpk.2016.01.003.
- Guidry AL, Tibbs ZE, Runge-Morris M, et al.. Expression, purification and characterization of human cytosolic sulfotransferase (SULT) 1C4. Hormone molecular biology and clinical investigation. Horm Mol Biol Clin Investg. 2021;21(1):27–36. DOI: https://doi.org/10.1515/hmbci-2016-0053.
- Falany CN, Krasnykh V, Falany JL. Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J Steroid Biochem Mol Biol. 1995;52(6):529–539.
- Barbosa ACS, Feng Y, Yu C, et al.. Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases. Expert Opin Drug Metab Toxicol. 2019;15(4):329–339. DOI:https://doi.org/10.1080/17425255.2019.1588884.
- Nakano H, Ogura K, Takahashi E, et al.. Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases. Drug Metab Pharmacokinet. 2004;19(3):216–226. DOI:https://doi.org/10.2133/dmpk.19.216.
- Mueller JW, Gilligan LC, Idkowiak J, et al.. The regulation of steroid action by sulfation and desulfation. Endocr Rev. 2015;36(5):526–563. DOI:https://doi.org/10.1210/er.2015-1036.
- Radominska A, Comer KA, Zimniak P, et al.. Human liver steroid sulphotransferase sulphates bile acids. Biochem J. 1990;272(3):597–604. DOI:https://doi.org/10.1042/bj2720597.
- Forbes KJ, Hagen M, Glatt H, et al.. Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995;112(1):53–60. 10.1016/0303-7207(95)03585-U.
- Meloche CA, Sharma V, Swedmark S, et al.. Sulfation of budesonide by human cytosolic sulfotransferase, dehydroepiandrosterone-sulfotransferase (DHEA-ST). Drug Metab Dispos. 2002;30(5):582–585. DOI:https://doi.org/10.1124/dmd.30.5.582.
- Falany JL, Macrina N, Falany CN. Sulfation of tibolone and tibolone metabolites by expressed human cytosolic sulfotransferases. J Steroid Biochem Mol Biol. 2004;88(4–5):383–391.
- Her C, Wood TC, Eichler EE, et al.. Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998;53(3):284–295. DOI:https://doi.org/10.1006/geno.1998.5518.
- Fuda H, Lee YC, Shimizu C, et al.. 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. 2002;277(39):36161–36166. DOI:https://doi.org/10.1074/jbc.M207165200.
- Smith CC, Gibbs TT, Farb DH. Pregnenolone sulfate as a modulator of synaptic plasticity. Psychopharmacology (Berl). 2014;231(17):3537–3556.
- Strott CA, Higashi Y. Cholesterol sulfate in human physiology what’s it all about?. J Lipid Res. 2003;44(7):1268–1278.
- Wang F, Beck-García K, Zorzin C, et al.. Inhibition of T cell receptor signaling by cholesterol sulfate, a naturally occurring derivative of membrane cholesterol. Nat Immunol. 2016;17(7):844–850. DOI:https://doi.org/10.1038/ni.3462.
- Sakurai T, Uruno T, Sugiura Y, et al.. Cholesterol sulfate is a DOCK2 inhibitor that mediates tissue-specific immune evasion in the eye. Sci Signal. 2018;11(541):4874. eaao. doi:https://doi.org/10.1126/scisignal.aao4874.
- Falany CN, Xie X, Wang J, et al.. Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain. Biochem J. 2000;346(3):857–864. DOI:https://doi.org/10.1042/bj3460857.
- Sakakibara Y, Suiko M, Pai TG, et al.. Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization. Gene. 2002;285(1–2):39–47. DOI:https://doi.org/10.1016/S0378-1119(02)00431-6.
- Brennan MD, Condra J. Transmission disequilibrium suggests a role for the sulfotransferase‐4A1 gene in schizophrenia. Am J Med Genet B Neuropsychiatr Genet. 2005;139(1):69–72.
- Meltzer HY, Brennan MD, Woodward ND, et al.. Association of Sult4A1 SNPs with psychopathology and cognition in patients with schizophrenia or schizoaffective disorder. Schizophr Res. 2008;106(2–3):258–264. DOI:https://doi.org/10.1016/j.schres.2008.08.029.
- Lewis AG, Minchin RF. Lack of exonic sulfotransferase 4A1 mutations in controls and schizophrenia cases. Psychiatric Genetics. 2009;19(1):53–55.
- Crittenden F, Thomas HR, Parant JM, et al.. Activity suppression behavior phenotype in SULT4A1 frameshift mutant zebrafish. Drug Metab Dispos. 2015;43(7):1037–1044.
- Garcia PL, Hossain MI, Andrabi SA, et al.. Generation and characterization of SULT4A1 mutant mouse models. Drug Metab Dispos. 2018;46(1):41–45.
- Sugahara T, Liu CC, Pai TG, et al.. Molecular cloning, expression, and functional characterization of a novel zebrafish cytosolic sulfotransferase. Biochem Biophys Res Commun. 2003;300(3):725–730.
- Cao H, Agarwal SK, Burnside J. Cloning and expression of a novel chicken sulfotransferase cDNA regulated by GH. J Endocrinol. 1999;160(3):491.
- Takahashi S, Sakakibara Y, Mishiro E, et al.. Molecular cloning, expression and characterization of a novel mouse SULT6 cytosolic sulfotransferase. J Biochem. 2009;146(3):399–405. DOI:https://doi.org/10.1093/jb/mvp087.
- Nowell S, Falany CN. Pharmacogenetics of human cytosolic sulfotransferases. Oncogene. 2006;13:25(11):1673–1678. DOI:https://doi.org/10.1038/sj.onc.1209376.
- Hui Y, Liu M-C. Sulfation of ritodrine by the human cytosolic sulfotransferases (SULTs): Effects of SULT1A3 genetic polymorphism. European journal of pharmacology. 2015;761:125–129.
- Daniels J, Kadlubar S. Sulfotransferase genetic variation: from cancer risk to treatment response. Drug Metab Rev. 2013;45(4):415–422. DOI:https://doi.org/10.3109/03602532.2013.835621.
- Gamage N, Barnett A, Hempel N, et al.. Human sulfotransferases and their role in chemical metabolism. Toxicol Sci. 2006;90(1):5–22. DOI:https://doi.org/10.1093/toxsci/kfj061.
- Hempel N, Gamage N, Martin JL, et al.. Human cytosolic sulfotransferase SULT1A1. Int J Biochem Cell Biol. 2007;39(4):685–689. DOI:https://doi.org/10.1016/j.biocel.2006.10.002.
- Glatt H, Meinl W. Pharmacogenetics of soluble sulfotransferases (SULTs). Naunyn Schmiedebergs Arch Pharmacol. 2004;369(1):55–68.
- Riches Z, Stanley EL, Bloomer JC, et al.. Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: the SULT “pie”. Drug Metab Dispos. 2009;37(11):2255–2261. DOI:https://doi.org/10.1124/dmd.109.028399.
- Salman ED, Kadlubar SA, Falany CN. Expression and localization of cytosolic sulfotransferase (SULT) 1A1 and SULT1A3 in normal human brain. Drug Metab Dispos. 2009;37(4):706–709.
- Richard K, Hume R, Kaptein E, et al.. Sulfation of thyroid hormone and dopamine during human development: ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain. J Clin Endocrinol Metab. 2001;86(6):2734–2742. DOI:https://doi.org/10.1210/jcem.86.6.7569.
- Vietri M, Pietrabissa A, Mosca F, et al.. Human adult and foetal liver sulphotransferases: inhibition by mefenamic acid and salicylic acid. Xenobiotica. 2001;31(3):153–161. DOI:https://doi.org/10.1080/00498250110043481.
- Stanley EL, Hume R, Coughtrie MWH. Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification. Mol Cell Endocrinol. 2005;240(1–2):32–42.
- Price RA, Spielman RS, Lucena AL, et al.. Genetic polymorphism for human platelet thermostable phenol sulfotransferase (TS PST) activity. Genetics. 1989;122(4):905–914. DOI:https://doi.org/10.1093/genetics/122.4.905.
- Hebbring SJ, Adjei AA, Baer JL, et al.. Human SULT1A1 gene: copy number differences and functional implications. Hum Mol Genet. 2007;16(5):463–470. DOI:https://doi.org/10.1093/hmg/ddl468.
- Bardakci F, Arslan S, Bardakci S, et al.. Sulfotransferase 1A1 (SULT1A1) polymorphism and susceptibility to primary brain tumors. J Cancer Res Clin Oncol. 2007;134(1):109–114. DOI:https://doi.org/10.1007/s00432-007-0256-3.
- Hildebrandt MA, Carrington DP, Thomae BA, et al.. Genetic diversity and function in the human cytosolic sulfotransferases. Pharmacogenomics J. 2007;7(2):133–143. DOI:https://doi.org/10.1038/sj.tpj.6500404.
- Li X, Clemens DL, Cole JR, et al.. Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3ʹ,5-triiodothyronine as the substrate. J Endocrinol. 2001;171(3):525–532. DOI:https://doi.org/10.1677/joe.0.1710525.
- Nagar S, Walther S, Blanchard RL. Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation. Mol Pharmacol. 2006;69(6):2084–2092.
- Gjerde J, Hauglid M, Breilid H, et al.. Effects of CYP2D6 and SULT1A1 genotypes including SULT1A1 gene copy number on tamoxifen metabolism. Ann Oncol. 2008;19(1):56–61. DOI:https://doi.org/10.1093/annonc/mdm434.
- Coughtrie MW. Sulfation through the looking glass--recent advances in sulfotransferase research for the curious. Pharmacogenomics J. 2002;2(5):297–308.
- Lindsay J, Wang LL, Li Y, et al.. Structure, function and polymorphism of human cytosolic sulfotransferases. Curr Drug Metab. 2008;9(2):99–105. DOI:https://doi.org/10.2174/138920008783571819.
- Carlini EJ, Raftogianis RB, Wood TC, et al.. Sulfation pharmacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian, Chinese and African-American subjects. Pharmacogenetics. 2001;11(1):57–68. DOI:https://doi.org/10.1097/00008571-200102000-00007.
- Ozawa S, Shimizu M, Katoh T, et al.. Sulfating-activity and stability of cDNA-expressed allozymes of human phenol sulfotransferase, ST1A3*1 ((213)Arg) and ST1A3*2 ((213)His), both of which exist in Japanese as well as Caucasians. J Biochem. 1999;126(2):271–277. DOI:https://doi.org/10.1093/oxfordjournals.jbchem.a022445.
- Rasool MI, Bairam AF, Gohal SA, et al.. Effects of the human SULT1A1 polymorphisms on the sulfation of acetaminophen, O-desmethylnaproxen, and tapentadol. Pharmacol Rep. 2019;71(2):257–265. DOI:https://doi.org/10.1016/j.pharep.2018.12.001.
- Marazziti D, Palego L, Mazzanti C, et al.. Human platelet sulfotransferase shows seasonal rhythms. Chronobiol Int. 1995;12(2):100–105. DOI:https://doi.org/10.3109/07420529509064505.
- Marazziti D, Palego L, Rossi A, et al.. Gender-related seasonality of human platelet phenolsulfotransferase activity. Neuropsychobiology. 1998;38(1):1–5. DOI:https://doi.org/10.1159/000026509.
- Coughtrie MW, Gilissen RA, Shek B, et al.. Phenol sulphotransferase SULT1A1 polymorphism: molecular diagnosis and allele frequencies in Caucasian and African populations. Biochem J. 1999;337(1):45–49. DOI:https://doi.org/10.1042/bj3370045.
- Dalhoff K, Buus Jensen K, Enghusen Poulsen H. Cancer and molecular biomarkers of phase 2. Methods Enzymol. 2005;400:618–627.
- Wu MT, Wang YT, Ho CK, et al.. SULT1A1 polymorphism and esophageal cancer in males. Int J Cancer. 2003;103(1):101–104. DOI:https://doi.org/10.1002/ijc.10805.
- Han DF, Zhou X, Hu MB, et al.. Sulfotransferase 1A1 (SULT1A1) polymorphism and breast cancer risk in Chinese women. Toxicol Lett. 2004;150(2):167–177. DOI:https://doi.org/10.1016/j.toxlet.2004.01.012.
- Boccia S, Persiani R, La Torre G, et al.. Sulfotransferase 1A1 polymorphism and gastric cancer risk: a pilot case-control study. Cancer Lett. 2005;229(2):235–243. DOI:https://doi.org/10.1016/j.canlet.2005.06.035.
- Wang Y, Spitz MR, Tsou AM, et al.. Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer. 2002;35(2):137–142. DOI:https://doi.org/10.1016/S0169-5002(01)00406-8.
- Arslan S, Silig Y, Pinarbasi H. An investigation of the relationship between SULT1A1 Arg(213)His polymorphism and lung cancer susceptibility in a Turkish population. Cell Biochem Funct. 2009;27(4):211–215.
- Tasnim T, MMA A-M, Nahid NA, et al.. Genetic variants of SULT1A1 and XRCC1 genes and risk of lung cancer in Bangladeshi population. Tumour Biol. 2017;39(11):1010428317729270. DOI:https://doi.org/10.1177/1010428317729270.
- Daniels J, Kadlubar S. Pharmacogenetics of SULT1A1. Pharmacogenomics. 2014;15(14):1823–1838.
- Wong CF, Liyou N, Leggett B, et al.. Association of the SULT1A1 R213H polymorphism with colorectal cancer. Clin Exp Pharmacol Physiol. 2002;29(9):754–758. DOI:https://doi.org/10.1046/j.1440-1681.2002.03738.x.
- Steiner M, Bastian M, Schulz WA, et al.. Phenol sulphotransferase SULT1A1 polymorphism in prostate cancer: lack of association. Arch Toxicol. 2000;74(4–5):222–225. DOI:https://doi.org/10.1007/s002040000118.
- Tamaki Y, Arai T, Sugimura H, et al.. Association between Cancer Risk and Drug-metabolizing Enzyme Gene (CYP2A6, CYP2A13, CYP4B1, SULT1A1, GSTM1 and GSTT1) Polymorphisms in Cases of Lung Cancer in Japan. Drug Metab Pharmacokinet. 2011;26(5):516–522. DOI:https://doi.org/10.2133/dmpk.DMPK-11-RG-046.
- Ozawa S, Katoh T, Inatomi H, et al.. Association of genotypes of carcinogen-activating enzymes, phenol sulfotransferase SULT1A1 (ST1A3) and arylamine N-acetyltransferase NAT2, with urothelial cancer in a Japanese population. Int J Cancer. 2002;102(4):418–421. DOI:https://doi.org/10.1002/ijc.10728.
- Zheng L, Wang Y, Schabath MB, et al.. Sulfotransferase 1A1 (SULT1A1) polymorphism and bladder cancer risk: a case-control study. Cancer Lett. 2003;202(1):61–69. DOI:https://doi.org/10.1016/j.canlet.2003.08.007.
- Lu J, Li H, Zhang J, et al.. Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun. 2010;396(2):429–434. DOI:https://doi.org/10.1016/j.bbrc.2010.04.109.
- Zheng W, Xie D, Cerhan JR, et al. Sulfotransferase 1A1 polymorphism, endogenous estrogen exposure, well-done meat intake, and breast cancer risk. Cancer Epidemiol Biomarkers Prev. 2001;10(2):89–94.
- Tang D, Rundle A, Mooney L, et al.. Sulfotransferase 1A1 (SULT1A1) polymorphism, PAH-DNA adduct levels in breast tissue and breast cancer risk in a case-control study. Breast Cancer Res Treat. 2003;78(2):217–222. DOI:https://doi.org/10.1023/A:1022968303118.
- Nowell S, Sweeney C, Winters M, et al.. Association between sulfotransferase 1A1 genotype and survival of breast cancer patients receiving tamoxifen therapy. J Natl Cancer Inst. 2002;94(21):1635–1640. DOI:https://doi.org/10.1093/jnci/94.21.1635.
- Nowell SA, Ahn J, Rae JM, et al.. Association of genetic variation in tamoxifen-metabolizing enzymes with overall survival and recurrence of disease in breast cancer patients. Breast Cancer Res Treat. 2005;91(3):249–258. DOI:https://doi.org/10.1007/s10549-004-7751-x.
- Lee H, Wang Q, Yang F, et al.. SULT1A1 Arg213His polymorphism, smoked meat, and breast cancer risk: a case-control study and meta-analysis. DNA Cell Biol. 2012;31(5):688–699. DOI:https://doi.org/10.1089/dna.2011.1403.
- Tengström M, Mannermaa A, Kosma VM, et al.. SULT1A1 rs9282861 polymorphism-a potential modifier of efficacy of the systemic adjuvant therapy in breast cancer?. BMC Cancer. 2012;12(1):257. DOI:https://doi.org/10.1186/1471-2407-12-257.
- Grabinski JL, Smith LS, Chisholm GB, et al.. Genotypic and allelic frequencies of SULT1A1 polymorphisms in women receiving adjuvant tamoxifen therapy. Breast Cancer Res Treat. 2006;95(1):13–16. DOI:https://doi.org/10.1007/s10549-005-9019-5.
- Choi JY, Lee KM, Park SK, et al.. Genetic polymorphisms of SULT1A1 and SULT1E1 and the risk and survival of breast cancer. Cancer Epidemiol Biomarkers Prev. 2005;14(5):1090–1095. DOI:https://doi.org/10.1158/1055-9965.EPI-04-0688.
- Serrano D, Lazzeroni M, Zambon CF, et al.. Efficacy of tamoxifen based on cytochrome P450 2D6, CYP2C19 and SULT1A1 genotype in the Italian Tamoxifen Prevention Trial. Pharmacogenomics J. 2011;11(2):100–107. DOI:https://doi.org/10.1038/tpj.2010.17.
- Knechtel G, Hofmann G, Gerger A, et al.. Analysis of common germline polymorphisms as prognostic factors in patients with lymph node-positive breast cancer. J Cancer Res Clin Oncol. 2010;136(12):1813–1819. DOI:https://doi.org/10.1007/s00432-010-0839-2.
- Tao P, Li H, Wang Q, et al. [A case-control study on association of SULT1A1 polymorphism, smoked meat intake with breast cancer risk.] Zhonghua Yu Fang Yi Xue Za Zhi. 2012;46(9):831-835.
- Li W, Gu M. SULT1A1 Arg213His polymorphism is associated with bladder cancer risk: a meta-analysis. Med Sci Monit. 2014;20:1590–1595.
- Sun XF, Ahmadi A, Arbman G, et al.. Polymorphisms in sulfotransferase 1A1 and glutathione S-transferase P1 genes in relation to colorectal cancer risk and patients’ survival. World J Gastroenterol. 2005;11(43):6875–6879. DOI:https://doi.org/10.3748/wjg.v11.i43.6875.
- Lilla C, Risch A, Verla-Tebit E, et al.. SULT1A1 genotype and susceptibility to colorectal cancer. Int J Cancer. 2007;120(1):201–206. DOI:https://doi.org/10.1002/ijc.22156.
- Cotterchio M, Boucher BA, Manno M, et al.. Red meat intake, doneness, polymorphisms in genes that encode carcinogen-metabolizing enzymes, and colorectal cancer risk. Cancer Epidemiol Biomarkers Prev. 2008;17(11):3098–3107. DOI:https://doi.org/10.1158/1055-9965.EPI-08-0341.
- Lopes BA, Emerenciano M, Gonçalves BA, et al.. Polymorphisms in CYP1B1, CYP3A5, GSTT1, and SULT1A1 are associated with early age acute leukemia. PLoS One. 2015;10(5):e0127308. DOI:https://doi.org/10.1371/journal.pone.0127308.
- Nowell S, Ratnasinghe DL, Ambrosone CB, et al.. Association of SULT1A1 phenotype and genotype with prostate cancer risk in African-Americans and Caucasians. Cancer Epidemiol Biomarkers Prev. 2004;13(2):270–276. DOI:https://doi.org/10.1158/1055-9965.EPI-03-0047.
- Dajani R, Cleasby A, Neu M, et al.. X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. J Biol Chem. 1999;274(53):37862–37868.
- Rubin GL, Sharp S, Jones AL, et al.. Design, production and characterization of antibodies discriminating between the phenol- and monoamine-sulphating forms of human phenol sulphotransferase. Xenobiotica. 1996;26(11):1113– 1119. DOI:https://doi.org/10.3109/00498259609050256.
- Dooley TP, Obermoeller RD, Leiter EH, et al.. Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2. Genomics. 1993;18(2):440–443. DOI:https://doi.org/10.1006/geno.1993.1494.
- Kumar RM, KaraMohamed S, Sudi J, et al.. Recurrent 16p11.2 microdeletions in autism. Hum Mol Genet. 2008;17(4):628–638. DOI:https://doi.org/10.1093/hmg/ddm376.
- Weiss LA, Shen Y, Korn JM, et al.. Association between microdeletion and microduplication at 16p11.2 and autism. N Engl J Med. 2008;358(7):667–675. DOI:https://doi.org/10.1056/NEJMoa075974.
- Steinman KJ, Spence SJ, Ramocki MB, et al.. 16p11.2 deletion and duplication: Characterizing neurologic phenotypes in a large clinically ascertained cohort. Am J Med Genet A. 2016;170(11):2943–2955. DOI:https://doi.org/10.1002/ajmg.a.37820.
- Angelakos CC, Watson AJ, O’Brien WT, et al.. Hyperactivity and male-specific sleep deficits in the 16p11.2 deletion mouse model of autism. Autism Res. 2017;10(4):572–584. DOI:https://doi.org/10.1002/aur.1707.
- Butcher NJ, Horne MK, Mellick GD, et al.. Sulfotransferase 1A3/4 copy number variation is associated with neurodegenerative disease. Pharmacogenomics J. 2018;18(2):209–214. DOI:https://doi.org/10.1038/tpj.2017.4.
- Rosenfeld JA, Coppinger J, Bejjani BA, et al.. Speech delays and behavioral problems are the predominant features in individuals with developmental delays and 16p11.2 microdeletions and microduplications. J Neurodev Disord. 2010;2(1):26–38. DOI:https://doi.org/10.1007/s11689-009-9037-4.
- Fernandez BA, Roberts W, Chung B, et al.. Phenotypic spectrum associated with de novo and inherited deletions and duplications at 16p11.2 in individuals ascertained for diagnosis of autism spectrum disorder. J Med Genet. 2010;47(3):195–203. DOI:https://doi.org/10.1136/jmg.2009.069369.
- Jacquemont S, Reymond A, Zufferey F, et al.. Mirror extreme BMI phenotypes associated with gene dosage at the chromosome 16p11.2 locus. Nature. 2011;478(7367):97–102. DOI:https://doi.org/10.1038/nature10406.
- McCarthy SE, Makarov V, Kirov G, et al.. Microduplications of 16p11.2 are associated with schizophrenia. Nat Genet. 2009;41(11):1223–1227. DOI:https://doi.org/10.1038/ng.474.
- Shinawi M, Liu P, Kang SH, et al. Recurrent reciprocal 16p11.2 rearrangements associated with global developmental delay, behavioural problems, dysmorphism, epilepsy, and abnormal head size. J Med Genet. 2010;47(5):332–341.
- Wang L, Yee VC, Weinshilboum RM. Aggresome formation and pharmacogenetics: sulfotransferase 1A3 as a model system. Biochem Biophys Res Commun. 2004;325(2):426–433.
- Bairam AF, Rasool MI, Alherz FA, et al. Sulfation of catecholamines and serotonin by SULT1A3 allozymes. Biochem Pharmacol. 2018;151:104–113.
- Bairam AF, Rasool MI, Alherz FA, et al. Effects of human SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of acetaminophen and opioid drugs by the cytosolic sulfotransferase SULT1A3. Arch Biochem Biophys. 2018;648:44–52.
- Bairam AF, Rasool MI, Alherz FA, et al.. Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. Pharmacogenet Genomics. 2019;29(5):99–105. DOI:https://doi.org/10.1097/FPC.0000000000000371.
- Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem Biol Interact. 2000;129(1–2):141–170.
- Meinl W, Tsoi C, Swedmark S, et al.. Highly selective bioactivation of 1-and 2-hydroxy-3-methylcholanthrene to mutagens by individual human and other mammalian sulphotransferases expressed in Salmonella typhimurium. Mutagenesis. 2013;28(5):609–619. DOI:https://doi.org/10.1093/mutage/get039.
- Fujita K, Nagata K, Ozawa S, et al.. Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases. J Biochem. 1997;122(5):1052–1061. DOI:https://doi.org/10.1093/oxfordjournals.jbchem.a021846.
- Iida A, Sekine A, Saito S, et al.. Catalog of 320 single nucleotide polymorphisms (SNPs) in 20 quinone oxidoreductase and sulfotransferase genes. J Hum Genet. 2001;46(4):225–240. DOI:https://doi.org/10.1007/s100380170093.
- Tibbs ZE, Guidry AL, Falany JL, et al.. A high frequency missense SULT1B1 allelic variant (L145V) selectively expressed in African descendants exhibits altered kinetic properties. Xenobiotica. 2018;48(1):79–88. DOI:https://doi.org/10.1080/00498254.2017.1282646.
- Monzo M, Brunet S, Urbano-Ispizua A, et al.. Genomic polymorphisms provide prognostic information in intermediate-risk acute myeloblastic leukemia. Blood. 2006;107(12):4871–4879. DOI:https://doi.org/10.1182/blood-2005-08-3272.
- Yip CKY, Bansal S, Wong SY, et al.. Identification of Galeterone and Abiraterone as Inhibitors of Dehydroepiandrosterone Sulfonation Catalyzed by Human Hepatic Cytosol, SULT2A1, SULT2B1b, and SULT1E1. Drug Metab Dispos. 2018;46(4):470–482. DOI:https://doi.org/10.1124/dmd.117.078980.
- Zhang H, Varlamova O, Vargas FM, et al. Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. J Biol Chem. 1998;273(18):10888–10892.
- Petrotchenko EV, Doerflein ME, Kakuta Y, et al.. Substrate gating confers steroid specificity to estrogen sulfotransferase. J Biol Chem. 1999;274(42):30019–30022. DOI:https://doi.org/10.1074/jbc.274.42.30019.
- Schrag ML, Cui D, Rushmore TH, et al.. Sulfotransferase 1E1 is a low km isoform mediating the 3-O-sulfation of ethinyl estradiol. Drug Metab Dispos. 2004;32(11):1299–1303. DOI:https://doi.org/10.1124/dmd.32.11.1299.
- Falany JL, Pilloff DE, Leyh TS, et al.. Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases. Drug Metab Dispos. 2006;34(3):361–368. DOI:https://doi.org/10.1124/dmd.105.006551.
- Nishiyama T, Ogura K, Nakano H, et al.. Reverse geometrical selectivity in glucuronidation and sulfation of cis- and trans-4-hydroxytamoxifens by human liver UDP-glucuronosyltransferases and sulfotransferases. Biochem Pharmacol. 2002;63(10):1817–1830. DOI:https://doi.org/10.1016/S0006-2952(02)00994-2.
- Suiko M, Sakakibara Y, Liu MC. Sulfation of environmental estrogen-like chemicals by human cytosolic sulfotransferases. Biochem Biophys Res Commun. 2000;267(1):80–84.
- Edavana VK, Yu X, Dhakal IB, et al. Sulfation of fulvestrant by human liver cytosols and recombinant SULT1A1 and SULT1E1. Pharmgenomics Pers Med. 2011;4:137–145.
- Falany JL, Falany CN. Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines. Cancer Res. 2013;28(5):1551–1555.
- Falany JL, Falany CN. Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone. Endocrinology. 1996;137(4):1395–1401.
- Qian Y, Deng C, Song WC. Expression of estrogen sulfotransferase in MCF-7 cells by cDNA transfection suppresses the estrogen response: potential role of the enzyme in regulating estrogen-dependent growth of breast epithelial cells. J Pharmacol Exp Ther. 1998;286(1):555–560.
- Song WC, Qian Y, Sun X, et al.. Cellular localization and regulation of expression of testicular estrogen sulfotransferase. Endocrinology. 1997;138(11):5006–5012. DOI:https://doi.org/10.1210/endo.138.11.5512.
- Hirata H, Hinoda Y, Okayama N, et al.. CYP1A1, SULT1A1, and SULT1E1 polymorphisms are risk factors for endometrial cancer susceptibility. Cancer. 2008;112(9):1964–1973. DOI:https://doi.org/10.1002/cncr.23392.
- Rebbeck TR, Troxel AB, Wang Y, et al.. Estrogen sulfation genes, hormone replacement therapy, and endometrial cancer risk. J Natl Cancer Inst. 2006;98(18):1311–1320. DOI:https://doi.org/10.1093/jnci/djj360.
- Hsieh YC, Jeng JS, Lin HJ, et al.. Epistasis analysis for estrogen metabolic and signaling pathway genes on young ischemic stroke patients. PLoS One. 2012;7(10):e47773. DOI:https://doi.org/10.1371/journal.pone.0047773.
- Lee SA, Choi JY, Shin CS, et al.. SULT1E1 genetic polymorphisms modified the association between phytoestrogen consumption and bone mineral density in healthy Korean women. Calcif Tissue Int. 2006;79(3):152–159. DOI:https://doi.org/10.1007/s00223-006-0008-4.
- Cohen S, Laitman Y, Kaufman B, et al.. SULT1E1 and ID2 genes as candidates for inherited predisposition to breast and ovarian cancer in Jewish women. Fam Cancer. 2009;8(2):135–144. DOI:https://doi.org/10.1007/s10689-008-9218-4.
- Li S, Xie L, Du M, et al.. Association study of genetic variants in estrogen metabolic pathway genes and colorectal cancer risk and survival. Arch Toxicol. 2018;92(6):1991–1999. DOI:https://doi.org/10.1007/s00204-018-2195-y.
- Woo HI, Lee SK, Kim J, et al.. Variations in plasma concentrations of tamoxifen metabolites and the effects of genetic polymorphisms on tamoxifen metabolism in Korean patients with breast cancer. Oncotarget. 2017;8(59):100296–100311. DOI:https://doi.org/10.18632/oncotarget.22220.
- Agarwal N, Alex AB, Farnham JM, et al.. Inherited Variants in SULT1E1 and Response to Abiraterone Acetate by Men with Metastatic Castration Refractory Prostate Cancer. J Urol. 2016;196(4):1112–1116. DOI:https://doi.org/10.1016/j.juro.2016.04.079.
- El Daibani AA, Alherz FA, Abunnaja MS, et al.. Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17β-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes. Eur J Drug Metab Pharmacokinet. 2021;46(1):105–118. DOI:https://doi.org/10.1007/s13318-020-00653-1.
- El Daibani AA Studies on the Functional Relevance of Genetic Polymorphisms of the Human Cytosolic Sulfotransferase 1E1 (SULT1E1) [dissertation]. University of Toledo; 2018. [cited 2021 Jun 15]. Available from: https://etd.ohiolink.edu/
- Comer KA, Falany CN. Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal. Mol Pharmacol. 1992;41(4):645–651.
- Falany CN, Comer KA, Dooley TP, et al.. Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization. Ann N Y Acad Sci. 1995;774(1 Dehydroepiand):59–72. DOI:https://doi.org/10.1111/j.1749-6632.1995.tb17372.x.
- Forbes KJ, Hagen M, Glatt H, et al.. Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995;112(1):53–60. DOI:https://doi.org/10.1016/0303-7207(95)03585-U.
- Ekström L, Rane A. Genetic variation, expression and ontogeny of sulfotransferase SULT2A1 in humans. Pharmacogenomics J. 2015;15(4):293–297.
- Chang H, Shi R, Rehse P, et al.. 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. 2004;279(4):2689–2696. DOI:https://doi.org/10.1074/jbc.M310446200.
- Aksoy IA, Sochorová V, Weinshilboum RM. Human liver dehydroepiandrosterone sulfotransferase: nature and extent of individual variation. Clin Pharmacol Ther. 1993;54(5):498–506.
- Thomae BA, Eckloff BW, Freimuth RR, et al.. Human sulfotransferase SULT2A1 pharmacogenetics: genotype-to-phenotype studies. Pharmacogenomics J. 2002;2(1):48–56. DOI:https://doi.org/10.1038/sj.tpj.6500089.
- Wilborn TW, Lang NP, Smith M, et al.. Association of SULT2A1 allelic variants with plasma adrenal androgens and prostate cancer in African American men. J Steroid Biochem Mol Biol. 2006;98(18):1311–1320. DOI:https://doi.org/10.1016/j.jsbmb.2006.01.006.
- Zhai G, Teumer A, Stolk L, et al.. Eight common genetic variants associated with serum DHEAS levels suggest a key role in ageing mechanisms. PLoS Genet. 2011;7(4):e1002025. DOI:https://doi.org/10.1371/journal.pgen.1002025.
- García-Anguita A, Ortega L, Garcés C. Relationship of dehydroepiandrosterone sulfate with overweight and insulin sensitivity in 12-16-year-old Spanish children. Horm Metab Res. 2013;45(7):545–547.
- Kwon EM, Holt SK, Fu R, et al.. Androgen metabolism and JAK/STAT pathway genes and prostate cancer risk. Cancer Epidemiol. 2012;36(4):347–353. DOI:https://doi.org/10.1016/j.canep.2012.04.002.
- Louwers YV, de Jong FH, NAA VH, et al.. Variants in SULT2A1 affect the DHEA sulphate to DHEA ratio in patients with polycystic ovary syndrome but not the hyperandrogenic phenotype. J Clin Endocrinol Metab. 2013;98(9):3848–3855.
- Miller E, Zalzala MH, Abunnaja MS, et al.. Effects of Human Sulfotransferase 2A1 Genetic Polymorphisms 3 on the Sulfation of Tibolone. Eur J Drug Metab Pharmacokinet. 2018;43(4):415–421. DOI:https://doi.org/10.1007/s13318-017-0458-2.
- Abunnaja MS, Alherz FA, El Daibani AA, et al.. Effects of genetic polymorphisms on the sulfation of dehydroepiandrosterone and pregnenolone by human cytosolic sulfotransferase SULT2A1. Biochem Cell Biol. 2018;96(5):655–662. DOI:https://doi.org/10.1139/bcb-2017-0341.
- Abunnaja MS. Investigation of the Genetic Polymorphisms of the Human Cytosolic Sulfotransferase SULT2A1: Potential Impact on the Metabolism of Hydroxysteroids and Drugs [dissertation]. University of Toledo: OhioLINK Electronic Theses and Dissertations Center; 2019.
- He D, Falany CN. Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation. Drug Metab Dispos. 2006;34(10):1749–1755.
- Pai TG, Sugahara T, Suiko M, et al.. Differential xenoestrogen-sulfating activities of the human cytosolic sulfotransferases: molecular cloning, expression, and purification of human SULT2B1a and SULT2B1b sulfotransferases. Biochim Biophys Acta. 2002;1573(2):165–170. DOI:https://doi.org/10.1016/S0304-4165(02)00416-6.
- Fuda H, Javitt NB, Mitamura K, et al.. Oxysterols are substrates for cholesterol sulfotransferase. J Lipid Res. 2007;48(6):1343–1352. DOI:https://doi.org/10.1194/jlr.M700018-JLR200.
- Cook IT, Duniec-Dmuchowski Z, Kocarek TA, et al.. 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. 2009;37(10):2069–2078. DOI:https://doi.org/10.1124/dmd.108.025759.
- Ren S, Ning Y. Sulfation of 25-hydroxycholesterol regulates lipid metabolism, inflammatory responses, and cell proliferation. Am J Physiol Endocrinol Metab. 2014;306(2):E123–30.
- Geese WJ, Raftogianis RB. Biochemical characterization and tissue distribution of human SULT2B1. Biochem Biophys Res Commun. 2001;288(1):280–289.
- Higashi Y, Fuda H, Yanai H, et al.. Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes. J Invest Dermatol. 2004;122(5):1207–1213. DOI:https://doi.org/10.1111/j.0022-202X.2004.22416.x.
- Koizumi M, Momoeda M, Hiroi H, et al.. Expression and regulation of cholesterol sulfotransferase (SULT2B1b) in human endometrium. Fertil Steril. 2010;93(5):1538–1544. DOI:https://doi.org/10.1016/j.fertnstert.2009.01.075.
- He D, Frost AR, Falany CN. Identification and immunohistochemical localization of Sulfotransferase 2B1b (SULT2B1b) in human lung. Biochim Biophys Acta. 2005;1724(1–2):119–126.
- Yanai H, Javitt NB, Higashi Y, et al.. Expression of cholesterol sulfotransferase (SULT2B1b) in human platelets. Circulation. 2004;109(1):92–96. DOI:https://doi.org/10.1161/01.CIR.0000108925.95658.8D.
- Salman ED, Faye-Petersen O, Falany CN. Hydroxysteroid sulfotransferase 2B1b expression and localization in normal human brain. Horm Mol Biol Clin Investg. 2012;36(4):445–454. DOI:https://doi.org/10.1515/HMBCI.2011.117.
- He D, Falany CN. Inhibition of SULT2B1b expression alters effects of 3beta-hydroxysteroids on cell proliferation and steroid hormone receptor expression in human LNCaP prostate cancer cells. Prostate. 2007;67(12):1318–1329.
- Seo YK, Mirkheshti N, Song CS, et al.. SULT2B1b sulfotransferase: induction by vitamin D receptor and reduced expression in prostate cancer. Mol Endocrinol. 2013;27(6):925–939. DOI:https://doi.org/10.1210/me.2012-1369.
- Chen W, Zhou H, Ye L, et al.. Overexpression of SULT2B1b Promotes Angiogenesis in Human Gastric Cancer. Cell Physiol Biochem. 2016;38(3):1040–1054. DOI:https://doi.org/10.1159/000443055.
- Hu L, Yang GZ, Zhang Y, et al.. Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma. Lab Invest. 2015;95(9):1005–1018. DOI:https://doi.org/10.1038/labinvest.2015.84.
- Hong W, Guo F, Yang M, et al.. Hydroxysteroid sulfotransferase 2B1 affects gastric epithelial function and carcinogenesis induced by a carcinogenic agent. Lipids Health Dis. 2019;18(1):203. DOI:https://doi.org/10.1186/s12944-019-1149-6.
- Heinz L, Kim GJ, Marrakchi S, et al.. Mutations in SULT2B1 Cause Autosomal-Recessive Congenital Ichthyosis in Humans. Am J Hum Genet. 2017;100(6):926–939. DOI:https://doi.org/10.1016/j.ajhg.2017.05.007.
- Youssefian L, Vahidnezhad H, Saeidian AH, et al.. Autosomal recessive congenital ichthyosis: Genomic landscape and phenotypic spectrum in a cohort of 125 consanguineous families. Hum Mutat. 2019;40(3):288–298. DOI:https://doi.org/10.1002/humu.23695.
- Hyland PL, Freedman ND, Hu N, et al.. Genetic variants in sex hormone metabolic pathway genes and risk of esophageal squamous cell carcinoma. Carcinogenesis. 2013;34(5):1062–1068. DOI:https://doi.org/10.1093/carcin/bgt030.
- Hevir N, Sinkovec J, Rizner TL. Disturbed expression of phase I and phase II estrogen-metabolizing enzymes in endometrial cancer: lower levels of CYP1B1 and increased expression of S-COMT. Mol Cell Endocrinol. 2011;331(1):158–167.
- Ji Y, Moon I, Zlatkovic J, et al.. Human hydroxysteroid sulfotransferase SULT2B1 pharmacogenomics: gene sequence variation and functional genomics. J Pharmacol Exp Ther. 2007;322(2):529–540. DOI:https://doi.org/10.1124/jpet.107.122895.
- Alherz FA, Abunnaja MS, El Daibani AA, et al.. On the role of genetic polymorphisms in the sulfation of cholesterol by human cytosolic sulphotransferase SULT2B1b. J Biochem. 2018;164(3):215–221. DOI:https://doi.org/10.1093/jb/mvy042.
- Alherz FA, El Daibani AA, Abunnaja MS, et al. Effect of SULT2B1 genetic polymorphisms on the sulfation of dehydroepiandrosterone and pregnenolone by SULT2B1b allozymes. Mol Cell Endocrinol. 2019;496:110535.
- Zanger UM, Cytochrome SM. P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol Ther. 2013;138(1):103–141.
- Hizbullah, Ahmed S, Mumtaz MN, et al. Genetic variations in drug-metabolizing enzyme CYP2C9 among major ethnic groups of Pakistani population. Gene. 2020;746:144659.
- Meaden CW, Mozeika A, Asri R, et al.. A review of the existing literature on buprenorphine pharmacogenomics. Pharmacogenomics J. 2021;21(2):128–139.
- Zhao Q, Liu B, Zhang J, et al.. Association between a COMT polymorphism and clinical response to risperidone treatment: a pharmacogenetic study. Psychiatr Genet. 2012;22(6):298–299. DOI:https://doi.org/10.1097/YPG.0b013e328358629a.
- Matsuoka H, Tsurutani J, Chiba Y, et al.. Selection of opioids for cancer-related pain using a biomarker: a randomized, multi-institutional, open-label trial (RELIEF study). BMC Cancer. 2017;17(1):674. DOI:https://doi.org/10.1186/s12885-017-3664-z.
- Semiz S, Dujic T, Ostanek B, et al.. Association of NAT2 polymorphisms with type 2 diabetes in a population from Bosnia and Herzegovina. Arch Med Res. 2011;42(4):311–317. DOI:https://doi.org/10.1016/j.arcmed.2011.06.007.
- Selinski S, Blaszkewicz M, Ickstadt K, et al.. Improvements in algorithms for phenotype inference: the NAT2 example. Curr Drug Metab. 2014;15(2):233–249. DOI:https://doi.org/10.2174/1389200215666140202215717.
- Lu Y, Fang Y, Wu X, et al.. Effects of UGT1A9 genetic polymorphisms on monohydroxylated derivative of oxcarbazepine concentrations and oxcarbazepine monotherapeutic efficacy in Chinese patients with epilepsy. Eur J Clin Pharmacol. 2017;73(3):307–315. DOI:https://doi.org/10.1007/s00228-016-2157-3.
- Li J, Peng P, Mei Q, et al.. The impact of UGT2B7 C802T and CYP3A4*1G polymorphisms on pain relief in cancer patients receiving oxycontin. Support Care Cancer. 2018;26(8):2763–2767. DOI:https://doi.org/10.1007/s00520-018-4130-4.
- Takanashi S, Bachur NR. Adriamycin metabolism in man. Evidence from urinary metabolites. Drug Metab Dispos. 1976;4. p. 79–87.
- Nygren LR. P. Cancer. 1994;74:2857–2862.
- Gianni L, Norton L, Wolmark N, et al.. Role of anthracyclines in the treatment of early breast cancer. J Clin Oncol. 2009;27(28):4798–4808. DOI:https://doi.org/10.1200/JCO.2008.21.4791.
- Krischer JP, Epstein S, Cuthbertson DD, et al.. Clinical cardiotoxicity following anthracycline treatment for childhood cancer: the Pediatric Oncology Group experience. J Clin Oncol. 1997;15(4):1544–1552. DOI:https://doi.org/10.1200/JCO.1997.15.4.1544.
- Deng S, Wojnowski L. Genotyping the risk of anthracycline-induced cardiotoxicity. Cardiovascular toxicology. 2007;7(2):129–134.
- Montaner JS, Reiss P, Cooper D, et al.. A randomized, double-blind trial comparing combinations of nevirapine, didanosine, and zidovudine for HIV-infected patients. J Am Med Assoc. 1998;279(12):930–937. DOI:https://doi.org/10.1001/jama.279.12.930.
- Sweat MD, O’Reilly KR, Schmid GP, et al.. Cost-effectiveness of nevirapine to prevent mother-to-child HIV transmission in eight African countries. AIDS. 2004;18(12):1661–1671. DOI:https://doi.org/10.1097/01.aids.0000131353.06784.8f.
- Sharma AM, Klarskov K, Uetrecht J. Nevirapine bioactivation and covalent binding in the skin. Chem Res Toxicol. 2013;26:410–421.
- Sharma AM, Novalen M, Tanino T, et al.. 12-OH-nevirapine sulfate, formed in the skin, is responsible for nevirapine-induced skin rash. Chem Res Toxicol. 2013;26(5):817–827. DOI:https://doi.org/10.1021/tx400098z.
- Kranendonk M, Alves M, Antunes P, et al. Human sulfotransferase 1A1-dependent mutagenicity of 12-hydroxy-nevirapine: the missing link?. Chem Res Toxicol. 2014;27:1967–1971.
- Dooley TP, Haldeman-Cahill R, Joiner J, et al.. Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells. Biochem Biophys Res Commun. 2000;277(1):236–245. DOI:https://doi.org/10.1006/bbrc.2000.3643.
- Luu-The V, Duche D, Ferraris C, et al.. Expression profiles of phases 1 and 2 metabolizing enzymes in human skin and the reconstructed skin models Episkin™ and full thickness model from Episkin™. J Steroid Biochem Mol Biol. 2009;116(3–5):178–186. DOI:https://doi.org/10.1016/j.jsbmb.2009.05.011.
- Yasuda S, Idell S, Liu MC. Generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible. Biochem J. 2007;401(2):497–503.
- Liu MC, Yasuda S, Idell S. Sulfation of nitrotyrosine: biochemistry and functional implications. IUBMB Life. 2007;59(10):622–627.
- Yasuda S, Yasuda T, Liu MY, et al.. Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: role of the human SULT1A3. Toxicol Appl Pharmacol. 2011;251(2):104–109. DOI:https://doi.org/10.1016/j.taap.2010.12.006.
- Murata M, Oxidative KS. DNA damage induced by nitrotyrosine, a biomarker of inflammation. Biochem Biophys Res Commun. 2004;316(1):123–128.
- Peluffo H, Shacka JJ, Ricart K, et al.. Induction of motor neuron apoptosis by free 3-nitro-L-tyrosine. J Neurochem. 2004;89(3):602–612. DOI:https://doi.org/10.1046/j.1471-4159.2004.02363.x.
- Mohiuddin I, Chai H, Lin PH, et al.. Nitrotyrosine and chlorotyrosine: clinical significance and biological functions in the vascular system. J Surg Res. 2006;133(2):143–149. DOI:https://doi.org/10.1016/j.jss.2005.10.008.
- Chai H, Mohiuddin I, Lin P, et al.. Chlorotyrosine induces endothelial dysfunction in human coronary artery endothelial cells and porcine coronary arteries. J Surg Res. 2007;137(2):174. DOI:https://doi.org/10.1016/j.jss.2006.12.066.