ReviewDrug metabolism and disposition: the biological fate of chemicals2016
Design and Interpretation of Human Sulfotransferase 1A1 Assays.
Review in Drug metabolism and disposition: the biological fate of chemicals, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Allosteric Mechanisms Triggering Substrate and Cofactor Binding in the SULT1A1 Dimer as Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Role of Conformational Dynamics of Sulfotransferases SULT1A1 and SULT1A3 in Substrate Specificity.International journal of molecular sciences · 2023Article
- Article
- Sulfotransferase 2B1b, Sterol Sulfonation, and Disease.Pharmacological reviews · 2023Review
- Insights into the substrate binding mechanism of SULT1A1 through molecular dynamics with excited normal modes simulations.Scientific reports · 2021Article
- An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells.RSC chemical biology · 2021Article
- Enzyme Kinetics of PAPS-Sulfotransferase.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Combinatorial Biosynthesis of Sulfated Benzenediol Lactones with a Phenolic Sulfotransferase from Fusarium graminearum PH-1.mSphere · 2020Article
- The Human UGT2B7 Nanodisc.Drug metabolism and disposition: the biological fate of chemicals · 2020Article
- Allosteres to regulate neurotransmitter sulfonation.The Journal of biological chemistry · 2019Article
- Isoform-specific therapeutic control of sulfonation in humans.Biochemical pharmacology · 2019Article
- The NSAID allosteric site of human cytosolic sulfotransferases.The Journal of biological chemistry · 2017Article
- Tetrahydrobiopterin regulates monoamine neurotransmitter sulfonation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The structure of the catechin-binding site of human sulfotransferase 1A1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1.Biochemistry · 2016Article
Corrections and comments
- Erratum issued
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The human sulfotransferases (SULTs) regulate the activities of hundreds, if not thousands, of small molecule metabolites via transfer of the sulfuryl-moiety (-SO3) from the nucleotide donor, 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the hydroxyls and amines of the recipients. Our understanding of the molecular basis of SULT catalysis has expanded considerably in recent years. The basic kinetic mechanism of these enzymes, previously thought to be ordered, has been redefined as random for SULT2A1, a representative member of the superfamily. An active-site cap whose structure and dynamics are highly responsive to nucleotides was discovered and shown to be critical in determining SULT selectivity, a topic of longstanding interest to the field. We now realize that a given SULT can operate in two specificity modes-broad and narrow-depending on the disposition of the cap. More recent work has revealed that the caps of the SULT1A1 are controlled by homotropic allosteric interactions between PAPS molecules bound at the dimer's active sites. These interactions cause the catalytic efficiency of SULT1A1 to vary in a substrate-dependent fashion by as much as two orders of magnitude over a range of PAPS concentrations that spans those found in human tissues. SULT catalysis is further complicated by the fact that these enzymes are frequently inhibited by their substrates. This review provides an overview of the mechanistic features of SULT1A1 that are important for the design and interpretation of SULT1A1 assays.
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What OpenQuestion holds
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.