ReviewDrug metabolism reviews2013
Regulation of the cytosolic sulfotransferases by nuclear receptors.
Review in Drug metabolism reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 89 citations in OpenAlex.
- A simple method to measure sulfonation in man using paracetamol as probe drug.Scientific reports · 2021Trial
- The steroid metabolome in women with premenstrual dysphoric disorder during GnRH agonist-induced ovarian suppression: effects of estradiol and progesterone addback.Translational psychiatry · 2017Trial
- Downregulation of hepatic sulfotransferase 1E1 expression associated with decreased expression of multidrug resistance-associated protein 2.Drug metabolism and disposition: the biological fate of chemicals · 2025Article
- Transcriptomic and lipidomic analysis of aging-associated inflammatory signature in mouse liver.Inflammation and regeneration · 2025Article
- Targeting the ceramidase ACER3 attenuates cholestasis in mice by mitigating bile acid overload via unsaturated ceramide-mediated LXRβ signaling transduction.Nature communications · 2025Article
- Cytosolic sulfotransferases in endocrine disruption.Essays in biochemistry · 2024Review
- Agonists of the Nuclear Receptor PPARγ Can Produce Biased Signaling.Molecular pharmacology · 2024Article
- Sulfotransferase 4A1 Coding Sequence and Protein Structure Are Highly Conserved in Vertebrates.Genes · 2024Review
- Complex roles for sulfation in the toxicities of polychlorinated biphenyls.Critical reviews in toxicology · 2024Review
- Estrogen sulfotransferase and sulfatase in steroid homeostasis, metabolic disease, and cancer.Steroids · 2024Review
- Bioactivation of cinnamic alcohol in a reconstructed human epidermis model and evaluation of sensitizing potency of the identified metabolites.Frontiers in toxicology · 2024Article
- Transient rapamycin treatment during developmental stage extends lifespan in Mus musculus and Drosophila melanogaster.EMBO reports · 2022Article
- Integrated Deadenylase Genetic Association Network and Transcriptome Analysis in Thoracic Carcinomas.Molecules (Basel, Switzerland) · 2022Article
- Estrogen Sulfotransferase is Highly Expressed in Vascular Endothelial Cells Overlying Atherosclerotic Plaques.The protein journal · 2022Article
- The effects of sulfated secondary bile acids on intestinal barrier function and immune response in an inflammatoryHeliyon · 2022Article
- Prostate Cancer-Focus on Cholesterol.Cancers · 2021Review
- Interaction of Native- and Oxidized-Low-Density Lipoprotein with Human Estrogen Sulfotransferase.The protein journal · 2021Article
- An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells.RSC chemical biology · 2021Article
- A microbial metabolite remodels the gut-liver axis following bariatric surgery.Cell host & microbe · 2021 · on this mapArticle
- Cholesterol Metabolites 25-Hydroxycholesterol and 25-Hydroxycholesterol 3-Sulfate Are Potent Paired Regulators: From Discovery to Clinical Usage.Metabolites · 2020Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The cytosolic sulfotransferases (SULTs) are a multigene family of enzymes that catalyze the transfer of a sulfonate group from the physiologic sulfate donor, 3'-phosphoadenosine-5'-phosphosulfate, to a nucleophilic substrate to generate a polar product that is more amenable to elimination from the body. As catalysts of both xenobiotic and endogenous metabolism, the SULTs are major points of contact between the external and physiological environments, and modulation of SULT-catalyzed metabolism can not only affect xenobiotic disposition, but it can also alter endogenous metabolic processes. Therefore, it is not surprising that SULT expression is regulated by numerous members of the nuclear receptor (NR) superfamily that function as sensors of xenobiotics as well as endogenous molecules, such as fatty acids, bile acids, and oxysterols. These NRs include the peroxisome proliferator-activated receptors, pregnane X receptor, constitutive androstane receptor, vitamin D receptor, liver X receptors, farnesoid X receptor, retinoid-related orphan receptors, and estrogen-related receptors. This review summarizes current information about NR regulation of SULT expression. Because species differences in SULT subfamily composition and tissue-, sex-, development-, and inducer-dependent regulation are prominent, these differences will be emphasized throughout the review. In addition, because of the central role of the SULTs in cellular physiology, the effect of NR-mediated SULT regulation on physiological and pathophysiological processes will be discussed. Gaps in current knowledge that require further investigation are also highlighted.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.