PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
24610083-10	2014	Treatment of cells with all compounds, except RSVTM, caused increased estradiol levels, which could be explained by the demonstrated inhibition of estrogen sulfate conjugation, catalyzed by SULT1E1.	rsvtm	46-51	sulfotransferase family 1E member 1	Homo sapiens	190-197
24610083-10	2014	Treatment of cells with all compounds, except RSVTM, caused increased estradiol levels, which could be explained by the demonstrated inhibition of estrogen sulfate conjugation, catalyzed by SULT1E1.	Estradiol	70-79	sulfotransferase family 1E member 1	Homo sapiens	190-197
24610083-10	2014	Treatment of cells with all compounds, except RSVTM, caused increased estradiol levels, which could be explained by the demonstrated inhibition of estrogen sulfate conjugation, catalyzed by SULT1E1.	estrogen sulfate	147-163	sulfotransferase family 1E member 1	Homo sapiens	190-197
24598415-6	2014	Regulation of phase II rather than phase I metabolic enzymes was implicated mechanistically: raloxifene and DMA were observed to upregulate sulfotransferase (SULT 1E1) and glucuronidase (UGT 1A1).	Raloxifene Hydrochloride	93-103	sulfotransferase family 1E member 1	Homo sapiens	158-166
24598415-6	2014	Regulation of phase II rather than phase I metabolic enzymes was implicated mechanistically: raloxifene and DMA were observed to upregulate sulfotransferase (SULT 1E1) and glucuronidase (UGT 1A1).	desmethylarzoxifene	108-111	sulfotransferase family 1E member 1	Homo sapiens	158-166
23866734-1	2013	In patients with obstructive coronary artery disease, electrocardiographic (ECG) ST-segment elevation (STE) is frequently seen during dobutamine stress echocardiography (DSE) in leads overlying previous transmural left ventricular (LV) myocardial infarction.	Dobutamine	134-144	sulfotransferase family 1E member 1	Homo sapiens	103-106
23866734-8	2013	In conclusion, dobutamine-induced ECG STE in LV segments with normal baseline wall motion is a highly reliable marker of viable collateral-dependent myocardium.	Dobutamine	15-25	sulfotransferase family 1E member 1	Homo sapiens	38-41
23959441-2	2013	Tetrabromobisphenol A (TBBPA), the most widely used BFR, and human metabolites of certain congeners of polybrominated diphenyl ether (e.g., 3-OH-BDE-47) have been suggested to inhibit estrogen sulfotransferase, potentially affecting estrogen metabolism.	tetrabromobisphenol A	0-21	sulfotransferase family 1E member 1	Homo sapiens	184-209
23959441-2	2013	Tetrabromobisphenol A (TBBPA), the most widely used BFR, and human metabolites of certain congeners of polybrominated diphenyl ether (e.g., 3-OH-BDE-47) have been suggested to inhibit estrogen sulfotransferase, potentially affecting estrogen metabolism.	Halogenated Diphenyl Ethers	103-132	sulfotransferase family 1E member 1	Homo sapiens	184-209
23959441-2	2013	Tetrabromobisphenol A (TBBPA), the most widely used BFR, and human metabolites of certain congeners of polybrominated diphenyl ether (e.g., 3-OH-BDE-47) have been suggested to inhibit estrogen sulfotransferase, potentially affecting estrogen metabolism.	3-oh-bde-47	140-151	sulfotransferase family 1E member 1	Homo sapiens	184-209
23959441-5	2013	METHODS: We used X-ray crystallography to obtain atomic detail of the binding modes of TBBPA and 3-OH-BDE-47 to estrogen sulfotransferase for comparison with binding of the endogenous substrate estradiol.	tetrabromobisphenol A	87-92	sulfotransferase family 1E member 1	Homo sapiens	112-137
23922954-3	2013	In this descriptive study, correlations were examined between concentrations of tamoxifen metabolites and genotypes for CYP2D6, CYP3A4, CYP3A5, SULT1A1, SULT1A2 and SULT1E1 in 135 patients with estrogen receptor-positive breast cancer.	Tamoxifen	80-89	sulfotransferase family 1E member 1	Homo sapiens	165-172
23685729-6	2013	SULT1E1 activity was indicated by counting the transformed 3H-estradiol sulfate from 3H-labeled 17beta-estradiol added into the cell culture medium.	3h-estradiol sulfate	59-79	sulfotransferase family 1E member 1	Homo sapiens	0-7
23685729-6	2013	SULT1E1 activity was indicated by counting the transformed 3H-estradiol sulfate from 3H-labeled 17beta-estradiol added into the cell culture medium.	Tritium	59-61	sulfotransferase family 1E member 1	Homo sapiens	0-7
23685729-6	2013	SULT1E1 activity was indicated by counting the transformed 3H-estradiol sulfate from 3H-labeled 17beta-estradiol added into the cell culture medium.	Estradiol	96-112	sulfotransferase family 1E member 1	Homo sapiens	0-7
23685729-7	2013	The activity of SULT1E1 reduced following treatment with WY14643, whereas SULT1E1 activity was enhanced in the presence of IGF-1.	pirinixic acid	57-64	sulfotransferase family 1E member 1	Homo sapiens	16-23
23685729-10	2013	The PPAR-alpha agonist WY14643 downregulated, while IGF-1 upregulated, the luciferase activity of the SULT1E1 promoter.	pirinixic acid	23-30	sulfotransferase family 1E member 1	Homo sapiens	102-109
23685729-11	2013	In conclusion, the PPAR-alpha agonist WY14643 and IGF-1 may regulate SULT1E1 expression at the transcriptional level and modulate the levels of active estrogens in endothelial cells and smooth muscle cells, thereby affecting the physiology and pathophysiology of vascular walls.	pirinixic acid	38-45	sulfotransferase family 1E member 1	Homo sapiens	69-76
23384540-3	2013	E2 can be further sulfated to estradiol sulfate (E2S) using SULT1E1.	estradiol sulfate	30-47	sulfotransferase family 1E member 1	Homo sapiens	60-67
23384540-3	2013	E2 can be further sulfated to estradiol sulfate (E2S) using SULT1E1.	Estradiol	49-52	sulfotransferase family 1E member 1	Homo sapiens	60-67
23370358-10	2013	Mithramycin, an inhibitor of the transcription factor stimulating protein 1 (Sp1), was able to restore coffee-reduced SULT1E1 gene expression.	Plicamycin	0-11	sulfotransferase family 1E member 1	Homo sapiens	118-125
22564759-7	2012	UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively.	4-hydroxy-3-methoxyethylamphetamine	59-63	sulfotransferase family 1E member 1	Homo sapiens	104-111
22564759-7	2012	UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively.	3,4-dihydroxyethylamphetamine	132-136	sulfotransferase family 1E member 1	Homo sapiens	104-111
22564759-7	2012	UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively.	4-hydroxy-3-methoxyethylamphetamine	141-145	sulfotransferase family 1E member 1	Homo sapiens	104-111
22434874-6	2012	4-OH TOR sulfation was significantly correlated (r = 0.98, P < 0.0001) with beta-naphthol sulfation (diagnostic for SULT1A1) but not with 17beta estradiol sulfation, a diagnostic substrate for SULT1E1(r = 0.09, P = 0.34).	4-oh tor	0-8	sulfotransferase family 1E member 1	Homo sapiens	196-203
22434874-7	2012	Examination of recombinant sulfotransferases (SULTs) revealed that SULT1A1 and SULT1E1 catalyzed 4-OH TOR sulfation, with apparent Km values of 2.6 and 6.4 muM and Vmax values of 8.5 and 5.5 nmol x min(-1) x mg protein(-1), respectively.	4-oh tor	97-105	sulfotransferase family 1E member 1	Homo sapiens	79-86
22369716-5	2012	Melatonin acts like a SEEM, inhibiting expression and activity of P450 aromatase, estrogen sulfatase and type 1, 17beta- hydroxysteroid dehydrogenase, but stimulating that of estrogen sulfotransferase.	Melatonin	0-9	sulfotransferase family 1E member 1	Homo sapiens	175-200
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	Progesterone	24-36	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	Mifepristone	98-103	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	Mifepristone	105-117	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	13beta-methyl 19-nor-steroid	123-131	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	4-nonylphenol	160-173	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	bisphenol A	175-186	sulfotransferase family 1E member 1	Homo sapiens	40-47
22414680-11	2012	The agonistic effect of progesterone on SULT1E1 mRNA was concentration-dependently antagonized by RU486 (mifepristone) and ZK137316 and, with lower potency, by 4-nonylphenol, bisphenol A and apigenin.	Apigenin	191-199	sulfotransferase family 1E member 1	Homo sapiens	40-47
22197379-2	2012	Human estrogen sulfotransferase (SULT1E1) is a broad-specificity enzyme that detoxifies a variety of chemicals, including estrogens, by the transfer of sulfate.	Sulfates	152-159	sulfotransferase family 1E member 1	Homo sapiens	6-31
22197379-2	2012	Human estrogen sulfotransferase (SULT1E1) is a broad-specificity enzyme that detoxifies a variety of chemicals, including estrogens, by the transfer of sulfate.	Sulfates	152-159	sulfotransferase family 1E member 1	Homo sapiens	33-40
22197379-6	2012	Such an assay enabled the isolation of SULT1E1 mutants with enhanced or wild-type activity toward an estrogen acceptor and significantly reduced activity for phenol or coumarin type of acceptors, leading to up to 3 orders of magnitude increase in specificity.	Phenol	158-164	sulfotransferase family 1E member 1	Homo sapiens	39-46
22197379-6	2012	Such an assay enabled the isolation of SULT1E1 mutants with enhanced or wild-type activity toward an estrogen acceptor and significantly reduced activity for phenol or coumarin type of acceptors, leading to up to 3 orders of magnitude increase in specificity.	coumarin	168-176	sulfotransferase family 1E member 1	Homo sapiens	39-46
21989950-9	2012	Direct sulfation of brivanib was catalyzed by multiple SULT enzymes, including SULT1A1, SULT1B1, SULT2A1, SULT1A3, and SULT1E1.	brivanib	20-28	sulfotransferase family 1E member 1	Homo sapiens	119-126
21828262-3	2011	Pulse-chase labeling experiments with 5-bromouridine demonstrated that the confluence-mediated increase in SULT1E1 expression was due to increased mRNA synthesis.	5-bromouridine	38-52	sulfotransferase family 1E member 1	Homo sapiens	107-114
21913674-3	2011	Among their biological effects, OHPCBs have been shown to alter the metabolism of endocrine hormones, including inhibition of mammalian cytosolic sulfotransferases (SULTs) that are responsible for the inactivation of thyroid hormones and phenolic steroids (i.e., hSULT1A1, hSULT1B1, and hSULT1E1).	ohpcbs	32-38	sulfotransferase family 1E member 1	Homo sapiens	287-295
24683427-2	2011	The major sulfotransferase (SULT) isoforms that conjugate steroids in humans are SULT1E1, SULT2A1, and SULT2B1b.	Steroids	58-66	sulfotransferase family 1E member 1	Homo sapiens	81-88
21764778-2	2011	Given our finding that PXR activation by rifampicin (RIF) represses the estrogen sulfotransferase (SULT1E1) gene in human primary hepatocytes and hepatocellular carcinoma Huh7 cells, here we have investigated the molecular mechanism of this repression.	Rifampin	41-51	sulfotransferase family 1E member 1	Homo sapiens	99-106
21764778-2	2011	Given our finding that PXR activation by rifampicin (RIF) represses the estrogen sulfotransferase (SULT1E1) gene in human primary hepatocytes and hepatocellular carcinoma Huh7 cells, here we have investigated the molecular mechanism of this repression.	Rifampin	53-56	sulfotransferase family 1E member 1	Homo sapiens	99-106
21871995-7	2011	It should be remembered that patients presenting with chest pain and showing benign pattern of NISTE (eg, "early repolarization" or STE secondary to left ventricular hypertrophy) may have true ischemic pain and non-STE myocardial infarction or even STEMI on top of the baseline benign pattern.	niste	95-100	sulfotransferase family 1E member 1	Homo sapiens	132-135
21642242-10	2011	While no differences in the increase in MPA and CD41 expression were observed after EST-1 and EST-2, ADP stimulation after EST-2 induced a lower increase in MPA (+18.3+-8.1% vs +27.9+-9.7%, p<0.001) and CD41 (+18.3+-9.2% vs +27.2+-12.4%, p<0.001) than after EST-1.	Adenosine Diphosphate	101-104	sulfotransferase family 1E member 1	Homo sapiens	264-269
21073915-2	2011	Estrone is locally produced from circulating inactive estrone sulfate by steroid sulfatase (STS), while estrone is inversely inactivated into estrone sulfate by estrogen sulfotransferase (EST).	estrone sulfate	142-157	sulfotransferase family 1E member 1	Homo sapiens	161-186
21543429-1	2011	CONTEXT AND OBJECTIVE: Estrogen sulfotransferase (EST) catalyzes the inactivation of estrone and estradiol in numerous tissues.	Estrone	85-92	sulfotransferase family 1E member 1	Homo sapiens	23-48
21543429-1	2011	CONTEXT AND OBJECTIVE: Estrogen sulfotransferase (EST) catalyzes the inactivation of estrone and estradiol in numerous tissues.	Estrone	85-92	sulfotransferase family 1E member 1	Homo sapiens	50-53
21543429-1	2011	CONTEXT AND OBJECTIVE: Estrogen sulfotransferase (EST) catalyzes the inactivation of estrone and estradiol in numerous tissues.	Estradiol	97-106	sulfotransferase family 1E member 1	Homo sapiens	23-48
21543429-1	2011	CONTEXT AND OBJECTIVE: Estrogen sulfotransferase (EST) catalyzes the inactivation of estrone and estradiol in numerous tissues.	Estradiol	97-106	sulfotransferase family 1E member 1	Homo sapiens	50-53
21543429-2	2011	Animal studies suggest that EST modulates glucose and lipid metabolism in adipose tissue, but it is unknown whether EST is expressed in human adipose tissue and, if so, how its expression relates to features of the metabolic syndrome.	Glucose	42-49	sulfotransferase family 1E member 1	Homo sapiens	28-31
21417257-2	2011	The present study investigated the phase II metabolism of feruloylquinic acids with selected human sulfotransferases (SULT1A1 and SULT1E1) and uridine 5"-diphosphoglucuronosyltransferases (UGT1A1 and UGT1A9).	1,3-di-O-feruloylquinic acid	58-78	sulfotransferase family 1E member 1	Homo sapiens	130-137
21417257-4	2011	Following incubation with human SULT1A1 or SULT1E1, formation of 5-O-feruloylquinic acid 4"-O-sulfate was confirmed by matching its HPLC and MS data with those of the authentic standard.	5-o-feruloylquinic acid 4"-o-sulfate	65-101	sulfotransferase family 1E member 1	Homo sapiens	43-50
21385053-2	2011	Additionally, melatonin stimulates the expression of the estrogen sulfotransferase, SULT1E1.	Melatonin	14-23	sulfotransferase family 1E member 1	Homo sapiens	57-82
21385053-2	2011	Additionally, melatonin stimulates the expression of the estrogen sulfotransferase, SULT1E1.	Melatonin	14-23	sulfotransferase family 1E member 1	Homo sapiens	84-91
21720030-3	2011	In the breast cancer tissue, 17beta-estradiol (E(2)) is inactivated by sulfation and the expression level of estrogen sulfotransferase (SULT1E1) is inversely correlated with its malignancy.	Estradiol	29-45	sulfotransferase family 1E member 1	Homo sapiens	109-134
21720030-3	2011	In the breast cancer tissue, 17beta-estradiol (E(2)) is inactivated by sulfation and the expression level of estrogen sulfotransferase (SULT1E1) is inversely correlated with its malignancy.	Estradiol	29-45	sulfotransferase family 1E member 1	Homo sapiens	136-143
21720030-8	2011	Significant induction of estrogen sulfotransferase activity was observed in calcium-differentiated NHEK cells (0.58+-0.07 (pmol/min/mg protein)).	Calcium	76-83	sulfotransferase family 1E member 1	Homo sapiens	25-50
19954949-6	2010	Assessment of activity using a panel of recombinant human SULTs showed that SULT1A1 is most active in the sulfation of caffeic, dihydrocaffeic and isoferulic acids, while SULT1E1 is most active in the sulfation of ferulic and dihydroferulic acids.	dihydroferulic acid	226-246	sulfotransferase family 1E member 1	Homo sapiens	171-178
20609400-1	2010	Stephanoside E (STE) and its aglycone Stephanthraniline A (STA) isolated from the stems of Stephanotis mucronata (Blanco) Merr.	stephanoside E	0-14	sulfotransferase family 1E member 1	Homo sapiens	16-19
20505544-4	2010	RESULTS: In EA women, SULT1E1 variant carriers had lower levels of dehydroepiandrosterone sulfate, and SULT1A1 variant carriers had lower levels of estradiol, dehydroepiandrosterone sulfate, and testosterone compared with women who did not carry these variant alleles.	Dehydroepiandrosterone Sulfate	67-97	sulfotransferase family 1E member 1	Homo sapiens	22-29
20304798-3	2010	In vitro sulfation assays showed alkyl and aryl substitutions to a fused heterocyclic system modeled after beta-naphthol (betaN), based on compounds that interact with the estrogen receptor, rendered several molecules with enhanced specificity for SULT1E1 over SULT1A1*1, SULT1A1*2, SULT1A3, and SULT2A1.	2-naphthol	107-120	sulfotransferase family 1E member 1	Homo sapiens	248-255
20304798-3	2010	In vitro sulfation assays showed alkyl and aryl substitutions to a fused heterocyclic system modeled after beta-naphthol (betaN), based on compounds that interact with the estrogen receptor, rendered several molecules with enhanced specificity for SULT1E1 over SULT1A1*1, SULT1A1*2, SULT1A3, and SULT2A1.	2-naphthol	122-127	sulfotransferase family 1E member 1	Homo sapiens	248-255
20304798-4	2010	Several 6-hydroxy-2-arylbenzothiazoles tested demonstrated excellent affinity--V(max)/K(m) ratios-and specificity for SULT1E1.	6-hydroxy-2-arylbenzothiazoles	8-38	sulfotransferase family 1E member 1	Homo sapiens	118-125
20304798-11	2010	Because this and other members of this family presenting specificity for SULT1E1 can be labeled with carbon-11 or fluorine-18, in vivo assays of SULT1E1 functional activity are now feasible in humans.	Carbon-11	101-110	sulfotransferase family 1E member 1	Homo sapiens	73-80
20304798-11	2010	Because this and other members of this family presenting specificity for SULT1E1 can be labeled with carbon-11 or fluorine-18, in vivo assays of SULT1E1 functional activity are now feasible in humans.	Carbon-11	101-110	sulfotransferase family 1E member 1	Homo sapiens	145-152
20304798-11	2010	Because this and other members of this family presenting specificity for SULT1E1 can be labeled with carbon-11 or fluorine-18, in vivo assays of SULT1E1 functional activity are now feasible in humans.	Fluorine-18	114-125	sulfotransferase family 1E member 1	Homo sapiens	73-80
19308726-9	2010	Treatment with the histone deacetylase inhibitor trichostatin A (TSA) induced SULT1E1 and CYP19 mRNA but suppressed CYP1B1, STS, COMT, 17betaHSD1, and 17betaHSD2 mRNA in MCF10A lineage cell lines.	trichostatin A	49-63	sulfotransferase family 1E member 1	Homo sapiens	78-85
19308726-9	2010	Treatment with the histone deacetylase inhibitor trichostatin A (TSA) induced SULT1E1 and CYP19 mRNA but suppressed CYP1B1, STS, COMT, 17betaHSD1, and 17betaHSD2 mRNA in MCF10A lineage cell lines.	trichostatin A	65-68	sulfotransferase family 1E member 1	Homo sapiens	78-85
19897460-7	2010	MPA after ADP stimulation increased more significantly at peak EST-1 compared with peak EST-2 (p<0.001).	Adenosine Diphosphate	10-13	sulfotransferase family 1E member 1	Homo sapiens	63-68
20823587-5	2010	In searching for the mechanism underlying the decrease of the sulfation of 17beta-estradiol and 4-methoxyestradiol, we demonstrated in an in vitro nitration experiment, that the human cytosolic sulfotransferase isoform 1E1 (SULT1E1), a major estrogen-sulfating enzyme, lost its estrogen-sulfating activity proportionately to the degree of nitration on tyrosine residues.	Estradiol	75-91	sulfotransferase family 1E member 1	Homo sapiens	224-231
20823587-5	2010	In searching for the mechanism underlying the decrease of the sulfation of 17beta-estradiol and 4-methoxyestradiol, we demonstrated in an in vitro nitration experiment, that the human cytosolic sulfotransferase isoform 1E1 (SULT1E1), a major estrogen-sulfating enzyme, lost its estrogen-sulfating activity proportionately to the degree of nitration on tyrosine residues.	4-methoxyestradiol	96-114	sulfotransferase family 1E member 1	Homo sapiens	224-231
19646966-5	2009	Enzyme activities were assessed using the following substrates: 4-nitrophenol for SULT1A1, dopamine for SULT1A3, 17beta-estradiol for SULT1E1, and dehydroepiandrosterone for SULT2A1.	Estradiol	113-129	sulfotransferase family 1E member 1	Homo sapiens	134-141
19589875-6	2009	SULT2A1 and SULT1E1 sulfated both the 3- and 24-hydroxyls to form the 24-OHChol-3, 24-disulfate.	24-ohchol-3, 24-disulfate	70-95	sulfotransferase family 1E member 1	Homo sapiens	12-19
19131519-6	2009	In human liver S9, quercetin, a highly selective inhibitor of SULT1A1 and SULT1E1, inhibited O-demethyl apixaban sulfate formation by 99%; 2,6-dichloro-4-nitrophenol, another inhibitor of SULT1A1, also inhibited this reaction by >90%; estrone, a competitive inhibitor for SULT1E1, had no effect on this reaction.	Quercetin	19-28	sulfotransferase family 1E member 1	Homo sapiens	74-81
19131519-6	2009	In human liver S9, quercetin, a highly selective inhibitor of SULT1A1 and SULT1E1, inhibited O-demethyl apixaban sulfate formation by 99%; 2,6-dichloro-4-nitrophenol, another inhibitor of SULT1A1, also inhibited this reaction by >90%; estrone, a competitive inhibitor for SULT1E1, had no effect on this reaction.	Quercetin	19-28	sulfotransferase family 1E member 1	Homo sapiens	275-282
19131519-6	2009	In human liver S9, quercetin, a highly selective inhibitor of SULT1A1 and SULT1E1, inhibited O-demethyl apixaban sulfate formation by 99%; 2,6-dichloro-4-nitrophenol, another inhibitor of SULT1A1, also inhibited this reaction by >90%; estrone, a competitive inhibitor for SULT1E1, had no effect on this reaction.	O-Demethyl apixaban sulfate	93-120	sulfotransferase family 1E member 1	Homo sapiens	74-81
19350454-5	2009	Hesperetin and eriodictyol are potent inhibitors of purified hSULT1A1, hSULT1A3, hSULT1E1, and hSULT2A1.	hesperetin	0-10	sulfotransferase family 1E member 1	Homo sapiens	81-89
19350454-5	2009	Hesperetin and eriodictyol are potent inhibitors of purified hSULT1A1, hSULT1A3, hSULT1E1, and hSULT2A1.	eriodictyol	15-26	sulfotransferase family 1E member 1	Homo sapiens	81-89
19429440-4	2009	SULT1E1 is responsible for the inactivation of beta-estradiol (E2) at physiological concentrations via conjugation with sulfonate.	Estradiol	47-61	sulfotransferase family 1E member 1	Homo sapiens	0-7
19429440-4	2009	SULT1E1 is responsible for the inactivation of beta-estradiol (E2) at physiological concentrations via conjugation with sulfonate.	sulfonate	120-129	sulfotransferase family 1E member 1	Homo sapiens	0-7
19250194-1	2009	Steroid sulfatase (STS) hydrolyses biologically inactive estrogen sulfates to active estrogens, while estrogen sulfotransferase (EST) sulfonates estrogens to estrogen sulfates.	estrogen sulfates	158-175	sulfotransferase family 1E member 1	Homo sapiens	102-127
19250196-6	2009	The estrogen sulfotransferase (SULT1E1), which acts at nanomolar concentration of estradiol, can inactivate most of this hormone present in the normal breast; however, in the breast cancer cells, the sulfotransferase denoted as SULT1A1 is mainly present, and this acts at micromolar concentrations of E(2).	Estradiol	82-91	sulfotransferase family 1E member 1	Homo sapiens	4-29
19250196-6	2009	The estrogen sulfotransferase (SULT1E1), which acts at nanomolar concentration of estradiol, can inactivate most of this hormone present in the normal breast; however, in the breast cancer cells, the sulfotransferase denoted as SULT1A1 is mainly present, and this acts at micromolar concentrations of E(2).	Estradiol	82-91	sulfotransferase family 1E member 1	Homo sapiens	31-38
19250210-0	2009	16alpha-hydroxyestrone inhibits estrogen sulfotransferase activity in human liver cancer cells.	16-hydroxyestrone	0-22	sulfotransferase family 1E member 1	Homo sapiens	32-57
18831980-2	2009	SULT1E1 is responsible for the sulfation and inactivation of beta-estradiol (E2) at physiological concentrations.	Estradiol	61-75	sulfotransferase family 1E member 1	Homo sapiens	0-7
18831980-2	2009	SULT1E1 is responsible for the sulfation and inactivation of beta-estradiol (E2) at physiological concentrations.	Estradiol	77-79	sulfotransferase family 1E member 1	Homo sapiens	0-7
19219749-0	2009	Trans-resveratrol-mediated inhibition of beta-oestradiol conjugation in MCF-7 cells stably expressing human sulfotransferases SULT1A1 or SULT1E1, and human liver microsomes.	Resveratrol	0-17	sulfotransferase family 1E member 1	Homo sapiens	137-144
19219749-5	2009	The combination of E2 and resveratrol did have a proliferative effect in cells expressing SULT1E1, but not in those expressing SULT1A1.	Resveratrol	26-37	sulfotransferase family 1E member 1	Homo sapiens	90-97
19219749-8	2009	The results corroborate the reported significant inhibition of SULT1E1-mediated E2 sulfation in vitro by resveratrol.	Resveratrol	105-116	sulfotransferase family 1E member 1	Homo sapiens	63-70
18440760-3	2008	In estrogen-sensitive tissues, e.g. the female breast, estrone sulfate (E1S), present at high concentrations in the circulation, is converted into the biologically active estrone (E1) by steroid sulfatase (STS) and again reverted into E1S by estrogen sulfotransferase (SULT1E1) providing a local estrogen storage.	estrone sulfate	55-70	sulfotransferase family 1E member 1	Homo sapiens	269-276
19075592-4	2008	As melatonin reduces the activity and expression of aromatase, sulfatase and 17beta-hydroxysteroid dehydrogenase and increases the activity and expression of estrogen sulfotransferase, it may protect mammary tissue from excessive estrogenic effects.	Melatonin	3-12	sulfotransferase family 1E member 1	Homo sapiens	158-183
18634814-5	2008	Genistein, on the other hand, inhibited ST1E1 and UGT1A1 expressions, and led to 17beta-estradiol cellular retention.	Genistein	0-9	sulfotransferase family 1E member 1	Homo sapiens	40-45
18486495-1	2008	PURPOSE: To evaluate the efficacy and tolerability of Levetiracetam as an add-on therapy in patients with startle epilepsy (StEp).	Levetiracetam	54-67	sulfotransferase family 1E member 1	Homo sapiens	124-128
18794126-4	2008	In this study, we show that activation of glucocorticoid receptor (GR) by dexamethasone (DEX) induced the expression and activity of estrogen sulfotransferase (SULT1E1 or EST), an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor.	Dexamethasone	74-87	sulfotransferase family 1E member 1	Homo sapiens	133-158
18794126-4	2008	In this study, we show that activation of glucocorticoid receptor (GR) by dexamethasone (DEX) induced the expression and activity of estrogen sulfotransferase (SULT1E1 or EST), an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor.	Dexamethasone	74-87	sulfotransferase family 1E member 1	Homo sapiens	160-167
18794126-4	2008	In this study, we show that activation of glucocorticoid receptor (GR) by dexamethasone (DEX) induced the expression and activity of estrogen sulfotransferase (SULT1E1 or EST), an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor.	Dexamethasone	89-92	sulfotransferase family 1E member 1	Homo sapiens	133-158
18794126-4	2008	In this study, we show that activation of glucocorticoid receptor (GR) by dexamethasone (DEX) induced the expression and activity of estrogen sulfotransferase (SULT1E1 or EST), an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor.	Dexamethasone	89-92	sulfotransferase family 1E member 1	Homo sapiens	160-167
18794126-6	2008	We further showed that the mouse and human SULT1E1 genes are transcriptional targets of GR and deletion of Sult1e1/Est in mice abolished the DEX effect on estrogen responses.	Dexamethasone	141-144	sulfotransferase family 1E member 1	Homo sapiens	43-50
18794126-6	2008	We further showed that the mouse and human SULT1E1 genes are transcriptional targets of GR and deletion of Sult1e1/Est in mice abolished the DEX effect on estrogen responses.	Dexamethasone	141-144	sulfotransferase family 1E member 1	Homo sapiens	107-114
18298468-6	2008	Physiologic concentrations of melatonin also stimulate the activity and expression of estrogen sulfotransferase (EST), the enzyme responsible for the formation of the biologically inactive estrogen sulfates.	Melatonin	30-39	sulfotransferase family 1E member 1	Homo sapiens	86-111
18298468-6	2008	Physiologic concentrations of melatonin also stimulate the activity and expression of estrogen sulfotransferase (EST), the enzyme responsible for the formation of the biologically inactive estrogen sulfates.	Melatonin	30-39	sulfotransferase family 1E member 1	Homo sapiens	113-116
18298468-6	2008	Physiologic concentrations of melatonin also stimulate the activity and expression of estrogen sulfotransferase (EST), the enzyme responsible for the formation of the biologically inactive estrogen sulfates.	estrogen sulfates	189-206	sulfotransferase family 1E member 1	Homo sapiens	86-111
18298468-6	2008	Physiologic concentrations of melatonin also stimulate the activity and expression of estrogen sulfotransferase (EST), the enzyme responsible for the formation of the biologically inactive estrogen sulfates.	estrogen sulfates	189-206	sulfotransferase family 1E member 1	Homo sapiens	113-116
18298468-7	2008	The level of EST mRNA steady-state of cells treated with melatonin was three times higher than that in control cells.	Melatonin	57-66	sulfotransferase family 1E member 1	Homo sapiens	13-16
18298468-8	2008	These findings which document that melatonin has an inhibitory effect on STS and 17beta-HSD1 and a stimulatory effect on EST, in combination with its previously described antiaromatase effect, can open up new and interesting possibilities in clinical applications of melatonin in breast cancer.	Melatonin	35-44	sulfotransferase family 1E member 1	Homo sapiens	121-124
18472171-3	2008	Electrophoretical profiles revealed four bands of esterase activity against alpha-naphthyl acetate; which were dubbed EST-1 to EST-4.	alpha-naphthyl acetate	76-98	sulfotransferase family 1E member 1	Homo sapiens	118-123
18473744-6	2008	SULTs 1A3 and 2A1 were less strongly inhibited by flavonoids or isoflavonoids although tricin (3",5"-dimethoxy-4",5,7-trihydroxyflavone is a competitive inhibitor of SULT 1E1 with an inhibition constant of approximately 1 nM.	tricin	95-135	sulfotransferase family 1E member 1	Homo sapiens	166-174
18473744-8	2008	Phthalates (used as plasticisers) inhibited SULTs 1E1 and 2A1.	phthalic acid	0-10	sulfotransferase family 1E member 1	Homo sapiens	44-61
18379081-9	2008	Enzymatic assays revealed that, five (SULT1A1, SULT1A2, SULT1A3, SULT1C4, and SULT1E1) of eleven known human SULTs tested could use CEs and methoxyestrogens (MEs) as substrates, with SULT1E1 displaying the strongest sulfating activity.	Estrogens, Catechol	132-135	sulfotransferase family 1E member 1	Homo sapiens	78-85
18379081-9	2008	Enzymatic assays revealed that, five (SULT1A1, SULT1A2, SULT1A3, SULT1C4, and SULT1E1) of eleven known human SULTs tested could use CEs and methoxyestrogens (MEs) as substrates, with SULT1E1 displaying the strongest sulfating activity.	Estrogens, Catechol	132-135	sulfotransferase family 1E member 1	Homo sapiens	183-190
18379081-9	2008	Enzymatic assays revealed that, five (SULT1A1, SULT1A2, SULT1A3, SULT1C4, and SULT1E1) of eleven known human SULTs tested could use CEs and methoxyestrogens (MEs) as substrates, with SULT1E1 displaying the strongest sulfating activity.	2-(N-morpholino)ethanesulfonic acid	158-161	sulfotransferase family 1E member 1	Homo sapiens	78-85
18232020-4	2008	RESULTS: Of 10 heterologously expressed SULT isoforms examined, SULT1A1, SULT1A3/4, SULT1E1, and SULT2A1 all catalyzed the formation of APAP sulfate with K(m) values of 2.4, 1.5, 1.9, and 3.7 mM, respectively.	apap sulfate	136-148	sulfotransferase family 1E member 1	Homo sapiens	84-91
17933522-1	2008	Some endocrine disrupting compounds such as phthalates and phenols act non-genomically by inhibiting the sulfotransferase (SULT 1E1 and SULT 1A1) isoforms which inactivate estrogens by sulfonation.	phthalic acid	44-54	sulfotransferase family 1E member 1	Homo sapiens	123-131
17933522-1	2008	Some endocrine disrupting compounds such as phthalates and phenols act non-genomically by inhibiting the sulfotransferase (SULT 1E1 and SULT 1A1) isoforms which inactivate estrogens by sulfonation.	Phenols	59-66	sulfotransferase family 1E member 1	Homo sapiens	123-131
17933522-3	2008	In particular, the plasticisers 4-n-octyl- and 4-n-nonyl-phenol inhibit SULT 1E1 with IC(50) values of 0.16 microM vs. 10nM estradiol while the 2-substituted chlorophenols show similar values.	4-n-octyl- and 4-n-nonyl-phenol	32-63	sulfotransferase family 1E member 1	Homo sapiens	72-80
17933522-3	2008	In particular, the plasticisers 4-n-octyl- and 4-n-nonyl-phenol inhibit SULT 1E1 with IC(50) values of 0.16 microM vs. 10nM estradiol while the 2-substituted chlorophenols show similar values.	Estradiol	124-133	sulfotransferase family 1E member 1	Homo sapiens	72-80
17933522-4	2008	Flavonoids are also SULT inhibitors; tricin is a competitive inhibitor of SULT 1E1 with a K(i) of 1.5+/-0.8 nM.	tricin	37-43	sulfotransferase family 1E member 1	Homo sapiens	74-82
17954528-7	2008	Resveratrol inhibited E2 sulfation with estimated K(i) values of 1.1 microM (liver), 0.6 microM (jejunum), and 2.3 microM (SULT1E1), concentrations that could be pharmacologically relevant.	Resveratrol	0-11	sulfotransferase family 1E member 1	Homo sapiens	123-130
17954528-9	2008	These findings also imply that resveratrol may inhibit the metabolism of other estrogen analogs or therapeutic agents such as ethinylestradiol or dietary components that are also substrates for SULT1E1.	Resveratrol	31-42	sulfotransferase family 1E member 1	Homo sapiens	194-201
17661084-1	2008	PURPOSE: Intratumoral estradiol levels in postmenopausal women with breast cancer are thought to be mainly regulated by the aromatase-mediated conversion from androgens and estrogen sulfotransferase (EST)-mediated reduction of bioavailability.	Estradiol	22-31	sulfotransferase family 1E member 1	Homo sapiens	173-198
17921479-6	2007	Only 17beta-HSD type 2 and EST genes showed sensitivity to progesterone in normal endometrium.	Progesterone	59-71	sulfotransferase family 1E member 1	Homo sapiens	27-30
17662596-8	2007	Raloxifene monosulfation was catalyzed by at least seven SULT isoforms and SULT1E1 also synthesizes raloxifene disulfate.	raloxifene monosulfation	0-24	sulfotransferase family 1E member 1	Homo sapiens	75-82
17662596-8	2007	Raloxifene monosulfation was catalyzed by at least seven SULT isoforms and SULT1E1 also synthesizes raloxifene disulfate.	raloxifene disulfate	100-120	sulfotransferase family 1E member 1	Homo sapiens	75-82
17662596-9	2007	SULT1E1 forms both monosulfates in a ratio of approximately 8:1 with the more abundant monosulfate migrating on HPLC identical to the SULT2A1 synthesized monosulfate.	monosulfates	19-31	sulfotransferase family 1E member 1	Homo sapiens	0-7
17662596-9	2007	SULT1E1 forms both monosulfates in a ratio of approximately 8:1 with the more abundant monosulfate migrating on HPLC identical to the SULT2A1 synthesized monosulfate.	monosulfate	19-30	sulfotransferase family 1E member 1	Homo sapiens	0-7
17662596-9	2007	SULT1E1 forms both monosulfates in a ratio of approximately 8:1 with the more abundant monosulfate migrating on HPLC identical to the SULT2A1 synthesized monosulfate.	monosulfate	87-98	sulfotransferase family 1E member 1	Homo sapiens	0-7
17230544-2	2007	E2 is inactivated to 17beta-estradiol-sulfate through estrogen sulfotransferase (SULT1E1).	estradiol-3-sulfate	21-45	sulfotransferase family 1E member 1	Homo sapiens	54-79
17230544-2	2007	E2 is inactivated to 17beta-estradiol-sulfate through estrogen sulfotransferase (SULT1E1).	estradiol-3-sulfate	21-45	sulfotransferase family 1E member 1	Homo sapiens	81-88
17266938-6	2007	In this study, we used amino acid modification, manipulation of intracellular redox state, and site-directed mutagenesis to study the redox regulation of human SULTs and specifically the mechanism of hSULT1E1 inhibitory regulation by oxidized glutathione (GSSG).	Glutathione	243-254	sulfotransferase family 1E member 1	Homo sapiens	200-208
17266938-6	2007	In this study, we used amino acid modification, manipulation of intracellular redox state, and site-directed mutagenesis to study the redox regulation of human SULTs and specifically the mechanism of hSULT1E1 inhibitory regulation by oxidized glutathione (GSSG).	Glutathione Disulfide	256-260	sulfotransferase family 1E member 1	Homo sapiens	200-208
17266938-8	2007	GSSG inactivated hSULT1E1 activity in an efficient, time- and concentration-dependant manner.	Glutathione Disulfide	0-4	sulfotransferase family 1E member 1	Homo sapiens	17-25
17266938-9	2007	The co-enzyme adenosine 3"-phosphate 5"-phosphosulfate protected hSULT1E1 from GSSG-associated inactivation.	Phosphoadenosine Phosphosulfate	14-54	sulfotransferase family 1E member 1	Homo sapiens	65-73
17266938-9	2007	The co-enzyme adenosine 3"-phosphate 5"-phosphosulfate protected hSULT1E1 from GSSG-associated inactivation.	Glutathione Disulfide	79-83	sulfotransferase family 1E member 1	Homo sapiens	65-73
17266938-10	2007	A reduced glutathione (GSH) inducer (N-acetyl cysteine) significantly increased while a GSH depletor (buthionine sulfoxamine) significantly decreased hSULT1E1 activity, but both failed to affect the amount of hSULT1E1 protein in human hepatocyte carcinoma Hep G2 cells.	Glutathione	88-91	sulfotransferase family 1E member 1	Homo sapiens	150-158
17266938-10	2007	A reduced glutathione (GSH) inducer (N-acetyl cysteine) significantly increased while a GSH depletor (buthionine sulfoxamine) significantly decreased hSULT1E1 activity, but both failed to affect the amount of hSULT1E1 protein in human hepatocyte carcinoma Hep G2 cells.	Buthionine Sulfoximine	102-124	sulfotransferase family 1E member 1	Homo sapiens	150-158
17266938-11	2007	Crystal structure suggested that no Cys residues exist near the active sites of hSULT1A1, hSULT1A3, and hSULT2A1, but Cys residues do exist within the active site of hSULT1E1.	Cysteine	118-121	sulfotransferase family 1E member 1	Homo sapiens	166-174
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	Quercetin	114-123	sulfotransferase family 1E member 1	Homo sapiens	77-84
17293380-4	2007	The enzyme kinetics of SULT1A1 allozymes and SULT1E1 were characterized for the polyphenolic substrates apigenin, chrysin, epicatechin, quercetin, and resveratrol.	chrysin	114-121	sulfotransferase family 1E member 1	Homo sapiens	45-52
17293380-4	2007	The enzyme kinetics of SULT1A1 allozymes and SULT1E1 were characterized for the polyphenolic substrates apigenin, chrysin, epicatechin, quercetin, and resveratrol.	Catechin	123-134	sulfotransferase family 1E member 1	Homo sapiens	45-52
17293380-4	2007	The enzyme kinetics of SULT1A1 allozymes and SULT1E1 were characterized for the polyphenolic substrates apigenin, chrysin, epicatechin, quercetin, and resveratrol.	Quercetin	136-145	sulfotransferase family 1E member 1	Homo sapiens	45-52
17293380-4	2007	The enzyme kinetics of SULT1A1 allozymes and SULT1E1 were characterized for the polyphenolic substrates apigenin, chrysin, epicatechin, quercetin, and resveratrol.	Resveratrol	151-162	sulfotransferase family 1E member 1	Homo sapiens	45-52
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	chrysin	105-112	sulfotransferase family 1E member 1	Homo sapiens	77-84
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	chrysin	105-112	sulfotransferase family 1E member 1	Homo sapiens	192-199
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	Quercetin	114-123	sulfotransferase family 1E member 1	Homo sapiens	192-199
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	Resveratrol	128-139	sulfotransferase family 1E member 1	Homo sapiens	77-84
17293380-10	2007	Altered cellular proliferation was observed in MCF-7 cells stably expressing SULT1E1 upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1.	Resveratrol	128-139	sulfotransferase family 1E member 1	Homo sapiens	192-199
17204552-12	2007	T1AM, the most active thyronamine pharmacologically, was associated with the greatest SULT activity of the thyronamines tested in the liver pool and in both the expressed SULT1A3 and SULT1E1 preparations.	T1AM	0-4	sulfotransferase family 1E member 1	Homo sapiens	183-190
17160708-11	2006	On the other hand, Est-1 can be upregulated by H2O2 via an antioxidant response element in the promoter.	Hydrogen Peroxide	47-51	sulfotransferase family 1E member 1	Homo sapiens	19-24
16899461-1	2006	Kinetic isotope effects have been measured for the estrogen sulfotransferase-catalyzed sulfuryl (SO3) transfer from p-nitrophenyl sulfate to the 5"-phosphoryl group of 3"-phosphoadenosine 5"-phosphate.	4-nitrophenyl sulfate	116-137	sulfotransferase family 1E member 1	Homo sapiens	51-76
16899461-1	2006	Kinetic isotope effects have been measured for the estrogen sulfotransferase-catalyzed sulfuryl (SO3) transfer from p-nitrophenyl sulfate to the 5"-phosphoryl group of 3"-phosphoadenosine 5"-phosphate.	adenosine 3'-phosphate-5'-phosphate	168-200	sulfotransferase family 1E member 1	Homo sapiens	51-76
16914110-1	2006	Human estrogen sulfotransferase (SULT1E1) is involved in the regulation of 17beta-estradiol responsiveness and is believed to protect peripheral tissues from excessive estrogenic effects.	Estradiol	75-91	sulfotransferase family 1E member 1	Homo sapiens	6-31
16914110-1	2006	Human estrogen sulfotransferase (SULT1E1) is involved in the regulation of 17beta-estradiol responsiveness and is believed to protect peripheral tissues from excessive estrogenic effects.	Estradiol	75-91	sulfotransferase family 1E member 1	Homo sapiens	33-40
16914110-4	2006	In this article, we describe the development and validation of an assay for the inhibition of human SULT1E1 that is rapid and simple and that uses the nonradioactive and noncarcinogenic 1-hydroxypyrene.	1-hydroxypyrene	186-201	sulfotransferase family 1E member 1	Homo sapiens	100-107
16914110-6	2006	Time- and protein-dependent formation of pyrene 1-sulfate was investigated, and enzyme kinetics was determined (K(m)=6.4+/-0.8 nM and V(max)=158+/-19 pmol/min/microg SULT1E1).	pyrene 1-sulfate	41-57	sulfotransferase family 1E member 1	Homo sapiens	166-173
17073578-7	2006	Nimesulide, meclofenamate, and piroxicam were more selective towards SULT1A1 inhibition, while sulindac and ibuprofen were more selective towards SULT1E1 inhibition.	Sulindac	95-103	sulfotransferase family 1E member 1	Homo sapiens	146-153
17073578-7	2006	Nimesulide, meclofenamate, and piroxicam were more selective towards SULT1A1 inhibition, while sulindac and ibuprofen were more selective towards SULT1E1 inhibition.	Ibuprofen	108-117	sulfotransferase family 1E member 1	Homo sapiens	146-153
16857224-0	2006	Regulation of SULT1E1 expression in Ishikawa adenocarcinoma cells by tibolone.	tibolone	69-77	sulfotransferase family 1E member 1	Homo sapiens	14-21
16857224-5	2006	Human endometrium and Ishikawa endometrial adenocarcinoma cells express SULT1E1 that efficiently sulfates both 3-OH tibolone metabolites and has trace activity with tibolone but no activity with the Delta4-isomer.	Sulfates	97-105	sulfotransferase family 1E member 1	Homo sapiens	72-79
16857224-5	2006	Human endometrium and Ishikawa endometrial adenocarcinoma cells express SULT1E1 that efficiently sulfates both 3-OH tibolone metabolites and has trace activity with tibolone but no activity with the Delta4-isomer.	3-oh tibolone	111-124	sulfotransferase family 1E member 1	Homo sapiens	72-79
16857224-5	2006	Human endometrium and Ishikawa endometrial adenocarcinoma cells express SULT1E1 that efficiently sulfates both 3-OH tibolone metabolites and has trace activity with tibolone but no activity with the Delta4-isomer.	tibolone	116-124	sulfotransferase family 1E member 1	Homo sapiens	72-79
16857224-6	2006	Treatment of Ishikawa cells with all four tibolone compounds resulted in the induction of SULT1E1 activity similar to the induction by progesterone.	tibolone	42-50	sulfotransferase family 1E member 1	Homo sapiens	90-97
16857224-7	2006	The induction of SULT1E1 was inhibited by RU486 indicating a role for the progesterone receptor.	Mifepristone	42-47	sulfotransferase family 1E member 1	Homo sapiens	17-24
16857224-8	2006	Sulfation of the tibolone compounds by Ishikawa cells and Ishikawa cells expressing physiological levels of SULT1E1 activity resulted in the sulfation of tibolone and the 3-OH metabolites but not Delta4-tibolone.	tibolone	17-25	sulfotransferase family 1E member 1	Homo sapiens	108-115
16857224-8	2006	Sulfation of the tibolone compounds by Ishikawa cells and Ishikawa cells expressing physiological levels of SULT1E1 activity resulted in the sulfation of tibolone and the 3-OH metabolites but not Delta4-tibolone.	tibolone	154-162	sulfotransferase family 1E member 1	Homo sapiens	108-115
16857224-8	2006	Sulfation of the tibolone compounds by Ishikawa cells and Ishikawa cells expressing physiological levels of SULT1E1 activity resulted in the sulfation of tibolone and the 3-OH metabolites but not Delta4-tibolone.	3-oh	171-175	sulfotransferase family 1E member 1	Homo sapiens	108-115
16879988-7	2006	Anti-progestin, RU486, reversed the induction of SULT1E1 and PRL by progesterone or Tib.	Mifepristone	16-21	sulfotransferase family 1E member 1	Homo sapiens	49-56
16879988-7	2006	Anti-progestin, RU486, reversed the induction of SULT1E1 and PRL by progesterone or Tib.	Progesterone	68-80	sulfotransferase family 1E member 1	Homo sapiens	49-56
16879988-7	2006	Anti-progestin, RU486, reversed the induction of SULT1E1 and PRL by progesterone or Tib.	tibolone	84-87	sulfotransferase family 1E member 1	Homo sapiens	49-56
16931338-4	2006	BPA is a substrate for estrogen sulfotransferase, and bisphenol A sulfate (BPAS) and disulfate are substrates for estrone sulfatase.	bisphenol A	0-3	sulfotransferase family 1E member 1	Homo sapiens	23-48
16381672-6	2006	SULT1E1 displayed the lowest Km (0.2 microM) for 4-OHT sulfation and SULT2A1 the lowest (0.3 microM) for raloxifene sulfation.	4,17 beta-dihydroxy-4-androstene-3-one	49-54	sulfotransferase family 1E member 1	Homo sapiens	0-7
16381672-6	2006	SULT1E1 displayed the lowest Km (0.2 microM) for 4-OHT sulfation and SULT2A1 the lowest (0.3 microM) for raloxifene sulfation.	Raloxifene Hydrochloride	105-115	sulfotransferase family 1E member 1	Homo sapiens	0-7
16381672-7	2006	SULT1E1 was the only isoform exhibiting detectable levels of raloxifene disulfation activity.	Raloxifene Hydrochloride	61-71	sulfotransferase family 1E member 1	Homo sapiens	0-7
16381672-8	2006	Modeling of the interactions of raloxifene in the active site of SULT1E1 indicates that both hydroxyl groups of raloxifene can be readily positioned in proximity to the sulfonyl group of 3"-phosphoadenosine 5"-phosphosulfate and the catalytically important His107 residue.	Raloxifene Hydrochloride	32-42	sulfotransferase family 1E member 1	Homo sapiens	65-72
16381672-8	2006	Modeling of the interactions of raloxifene in the active site of SULT1E1 indicates that both hydroxyl groups of raloxifene can be readily positioned in proximity to the sulfonyl group of 3"-phosphoadenosine 5"-phosphosulfate and the catalytically important His107 residue.	Raloxifene Hydrochloride	112-122	sulfotransferase family 1E member 1	Homo sapiens	65-72
16381672-8	2006	Modeling of the interactions of raloxifene in the active site of SULT1E1 indicates that both hydroxyl groups of raloxifene can be readily positioned in proximity to the sulfonyl group of 3"-phosphoadenosine 5"-phosphosulfate and the catalytically important His107 residue.	Phosphoadenosine Phosphosulfate	187-224	sulfotransferase family 1E member 1	Homo sapiens	65-72
16381672-11	2006	In contrast, raloxifene sulfation was detectable only in secretory phase cytosols in association with SULT1E1 activity.	Raloxifene Hydrochloride	13-23	sulfotransferase family 1E member 1	Homo sapiens	102-109
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	0-25
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	32-40
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	44-47
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrone sulfate	147-162	sulfotransferase family 1E member 1	Homo sapiens	0-25
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrone sulfate	147-162	sulfotransferase family 1E member 1	Homo sapiens	32-40
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	estrone sulfate	147-162	sulfotransferase family 1E member 1	Homo sapiens	44-47
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	Estrone	147-154	sulfotransferase family 1E member 1	Homo sapiens	0-25
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	Estrone	147-154	sulfotransferase family 1E member 1	Homo sapiens	32-40
16755106-11	2006	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, while steroid sulfatase (STS) hydrolyzes estrone sulfate (E1-S) to estrone.	Estrone	147-154	sulfotransferase family 1E member 1	Homo sapiens	44-47
16305588-6	2005	O-DMN was sulphated by SULT1A1, SULT1B1 and SULT1E1.	o-dmn	0-5	sulfotransferase family 1E member 1	Homo sapiens	44-51
16305588-11	2005	The role of the side-chain in O-DMN sulphation was studied using a series of structurally related beta-naphthol compounds as substrates for SULT1A1 and SULT1E1.	2-naphthol	98-111	sulfotransferase family 1E member 1	Homo sapiens	152-159
16266779-0	2005	Non-genomic effects of endocrine disrupters: inhibition of estrogen sulfotransferase by phenols and chlorinated phenols.	Phenols	88-95	sulfotransferase family 1E member 1	Homo sapiens	59-84
16266779-0	2005	Non-genomic effects of endocrine disrupters: inhibition of estrogen sulfotransferase by phenols and chlorinated phenols.	Phenols	112-119	sulfotransferase family 1E member 1	Homo sapiens	59-84
16266779-3	2005	Here, we show that 2, x-substituted phenols are potent inhibitors of estrogen sulfotransferase with IC(50) values at low- or sub-micromolar levels.	2, x-substituted phenols	19-43	sulfotransferase family 1E member 1	Homo sapiens	69-94
16300378-0	2005	Bioactivation of dibrominated biphenyls by cytochrome P450 activity to metabolites with estrogenic activity and estrogen sulfotransferase inhibition capacity.	diphenyl	30-39	sulfotransferase family 1E member 1	Homo sapiens	112-137
16300378-11	2005	The strongest hEST inhibition was found with 4-OH-3,4"-DBB (EC50 = 40 nM).	4-oh-3,4"-dbb	45-58	sulfotransferase family 1E member 1	Homo sapiens	14-18
15929889-3	2005	At concentrations > 0.15 microM, 3-OH-BaP inhibited its own sulfonation in cytosol fractions that were genotyped for SULT1A1 variants, as well as with expressed SULT1A1*1, SULT1A1*2, and SULT1E1, but not with SULT1A3 or SULT1B1.	3-hydroxybenzo(a)pyrene	36-44	sulfotransferase family 1E member 1	Homo sapiens	190-197
15929889-10	2005	The OH-PCBs tested inhibited sulfonation of 3-OH-BaP by SULT1E1, but the order of inhibitory potency was different than for SULT1A1.	oh-pcbs	4-11	sulfotransferase family 1E member 1	Homo sapiens	56-63
15929889-10	2005	The OH-PCBs tested inhibited sulfonation of 3-OH-BaP by SULT1E1, but the order of inhibitory potency was different than for SULT1A1.	3-hydroxybenzo(a)pyrene	44-52	sulfotransferase family 1E member 1	Homo sapiens	56-63
15929889-11	2005	SULT1E1 inhibitory potency correlated with the dihedral angle of the OH-PCBs.	oh-pcbs	69-76	sulfotransferase family 1E member 1	Homo sapiens	0-7
15522178-1	2004	BACKGROUND & OBJECTIVE: Estrogen sulfotransferase (EST) is an enzyme which metabolizes estrogen into inactive estrogen sulphate.	Adenosine Monophosphate	12-15	sulfotransferase family 1E member 1	Homo sapiens	28-53
15522178-1	2004	BACKGROUND & OBJECTIVE: Estrogen sulfotransferase (EST) is an enzyme which metabolizes estrogen into inactive estrogen sulphate.	Adenosine Monophosphate	12-15	sulfotransferase family 1E member 1	Homo sapiens	55-58
15522178-1	2004	BACKGROUND & OBJECTIVE: Estrogen sulfotransferase (EST) is an enzyme which metabolizes estrogen into inactive estrogen sulphate.	estrogen sulphate	114-131	sulfotransferase family 1E member 1	Homo sapiens	28-53
15522178-1	2004	BACKGROUND & OBJECTIVE: Estrogen sulfotransferase (EST) is an enzyme which metabolizes estrogen into inactive estrogen sulphate.	estrogen sulphate	114-131	sulfotransferase family 1E member 1	Homo sapiens	55-58
15483196-0	2004	Sulfotransferase 1E1 is a low km isoform mediating the 3-O-sulfation of ethinyl estradiol.	Ethinyl Estradiol	72-89	sulfotransferase family 1E member 1	Homo sapiens	0-20
15483196-7	2004	When these IC50 values were compared with those derived from expressed enzyme, inhibition of EE-SULT was consistent with the SULT1E1 (DCNP, IC50 = 20 microM; quercetin, IC50 = 0.6 microM), but not SULT1A3 (DCNP, IC50 = 12.4; quercetin, IC50 = 7 microM).	dcnp	134-138	sulfotransferase family 1E member 1	Homo sapiens	125-132
15483196-8	2004	Moreover, when estrone (which selectively inhibits expressed SULT1E1 and SULT1A3) was included in intestinal incubations, the high-affinity component of the Eadie-Hofstee plot for EE sulfation was inhibited, converting the plot from biphasic to monophasic.	Estrone	15-22	sulfotransferase family 1E member 1	Homo sapiens	61-68
15269185-7	2004	Studies of 3-OH-BaP sulfonation by expressed human SULT1A1*1, SULT1A1*2, SULT1B1, and SULT1E1 showed that triclosan inhibited the activities of each of these purified enzymes with IC50 concentrations between 2.09 and 7.5 microM.	3-hydroxybenzo(a)pyrene	11-19	sulfotransferase family 1E member 1	Homo sapiens	86-93
15269185-7	2004	Studies of 3-OH-BaP sulfonation by expressed human SULT1A1*1, SULT1A1*2, SULT1B1, and SULT1E1 showed that triclosan inhibited the activities of each of these purified enzymes with IC50 concentrations between 2.09 and 7.5 microM.	Triclosan	106-115	sulfotransferase family 1E member 1	Homo sapiens	86-93
15355916-2	2004	Steroid sulfatase hydrolyzes biologically inactive estrogen sulfates to active estrogens, whereas estrogen sulfotransferase sulfonates estrogens to estrogen sulfates.	estrogen sulfates	148-165	sulfotransferase family 1E member 1	Homo sapiens	98-123
15487807-8	2004	Quercetin, a flavonoid present in edible fruit, vegetable and wine, was a potent inhibitor of human liver SULT1A1 and estrogen sulfotransferase (EST) activities and the sulfation of resveratrol.	Quercetin	0-9	sulfotransferase family 1E member 1	Homo sapiens	118-143
15487807-8	2004	Quercetin, a flavonoid present in edible fruit, vegetable and wine, was a potent inhibitor of human liver SULT1A1 and estrogen sulfotransferase (EST) activities and the sulfation of resveratrol.	Flavonoids	13-22	sulfotransferase family 1E member 1	Homo sapiens	118-143
15499189-11	2004	A kinetic study for 7,4"-disulfate formation of DZ and GS from their 7- and 4"-monosulfates indicated that SULT1E1 most efficiently catalyzed both reactions among human SULTs.	7,4"-disulfate	20-34	sulfotransferase family 1E member 1	Homo sapiens	107-114
15499189-11	2004	A kinetic study for 7,4"-disulfate formation of DZ and GS from their 7- and 4"-monosulfates indicated that SULT1E1 most efficiently catalyzed both reactions among human SULTs.	7- and 4"-monosulfates	69-91	sulfotransferase family 1E member 1	Homo sapiens	107-114
15145448-6	2004	SULT1E1 conjugated both 3-OH-tibolone metabolites and tibolone itself slightly.	3-oh-tibolone	24-37	sulfotransferase family 1E member 1	Homo sapiens	0-7
15145448-6	2004	SULT1E1 conjugated both 3-OH-tibolone metabolites and tibolone itself slightly.	tibolone	29-37	sulfotransferase family 1E member 1	Homo sapiens	0-7
15095932-4	2004	DATA SYNTHESIS: For the patient with ST-segment elevation (STE) ACS, nonenteric-coated aspirin should be initiated immediately, if possible before arrival at the emergency department.	Aspirin	87-94	sulfotransferase family 1E member 1	Homo sapiens	59-62
14750408-10	2004	Dobutamine stress echocardiography revealed myocardial ischemia in the infarct region in 30% in the Convex ST-E group and 75% in the Concave ST-E group(p < 0.05).	Dobutamine	0-10	sulfotransferase family 1E member 1	Homo sapiens	107-111
14750408-10	2004	Dobutamine stress echocardiography revealed myocardial ischemia in the infarct region in 30% in the Convex ST-E group and 75% in the Concave ST-E group(p < 0.05).	Dobutamine	0-10	sulfotransferase family 1E member 1	Homo sapiens	141-145
14981909-0	2003	Effect of nomegestrol acetate on human estrogen sulfotransferase activity in the hormone-dependent MCF-7 and T-47D breast cancer cell lines.	nomegestrol acetate	10-29	sulfotransferase family 1E member 1	Homo sapiens	39-64
14981909-8	2003	In conclusion, the stimulation provoked at low doses by nomegestrol acetate on the estrogen sulfotransferase activity involved in the biosynthesis of the biologically inactive estrogen sulfates in hormone-dependent breast cancer cells is an important effect of this progestin and can open attractive clinical applications.	nomegestrol acetate	56-75	sulfotransferase family 1E member 1	Homo sapiens	83-108
14570759-6	2003	Acetonitrile, a commonly used solvent in cytochrome P450 studies, inhibited SULT1A1 activities (approximately 40%) at 0.4% (v/v), but activated SULT1E1-mediated 1-hydroxypyrene sulfation approximately 2.6-fold.	acetonitrile	0-12	sulfotransferase family 1E member 1	Homo sapiens	144-151
14570759-6	2003	Acetonitrile, a commonly used solvent in cytochrome P450 studies, inhibited SULT1A1 activities (approximately 40%) at 0.4% (v/v), but activated SULT1E1-mediated 1-hydroxypyrene sulfation approximately 2.6-fold.	1-hydroxypyrene	161-176	sulfotransferase family 1E member 1	Homo sapiens	144-151
14570759-7	2003	Assuming a two-site kinetic model, studies revealed that solvent affected Vmax1, Vmax2, and the Ki value of 1-hydroxypyrene sulfation mediated by SULT1E1.	1-hydroxypyrene	108-123	sulfotransferase family 1E member 1	Homo sapiens	146-153
12920175-4	2003	SULT1E1 sulfated fewer catechols.	Catechols	23-32	sulfotransferase family 1E member 1	Homo sapiens	0-7
14623543-1	2003	Steroid sulfatase (STS) hydrolyzes inactive estrone sulfate (E1-S) to estrone (E1), while estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to estrogen sulfates.	estrone sulfate	44-59	sulfotransferase family 1E member 1	Homo sapiens	90-115
14623543-1	2003	Steroid sulfatase (STS) hydrolyzes inactive estrone sulfate (E1-S) to estrone (E1), while estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to estrogen sulfates.	estrogen sulfates	168-185	sulfotransferase family 1E member 1	Homo sapiens	90-115
14623543-1	2003	Steroid sulfatase (STS) hydrolyzes inactive estrone sulfate (E1-S) to estrone (E1), while estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to estrogen sulfates.	estrogen sulfates	168-185	sulfotransferase family 1E member 1	Homo sapiens	122-130
14623543-1	2003	Steroid sulfatase (STS) hydrolyzes inactive estrone sulfate (E1-S) to estrone (E1), while estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to estrogen sulfates.	estrogen sulfates	168-185	sulfotransferase family 1E member 1	Homo sapiens	134-137
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	Alkanesulfonates	54-64	sulfotransferase family 1E member 1	Homo sapiens	0-25
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	Alkanesulfonates	54-64	sulfotransferase family 1E member 1	Homo sapiens	32-40
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	Alkanesulfonates	54-64	sulfotransferase family 1E member 1	Homo sapiens	44-47
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	0-25
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	32-40
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	estrogen sulfates	87-104	sulfotransferase family 1E member 1	Homo sapiens	44-47
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	estrone sulfate	149-164	sulfotransferase family 1E member 1	Homo sapiens	0-25
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	estrone sulfate	149-164	sulfotransferase family 1E member 1	Homo sapiens	44-47
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	Estrone	149-156	sulfotransferase family 1E member 1	Homo sapiens	0-25
12782580-1	2003	Estrogen sulfotransferase (EST; SULT 1E1 or STE gene) sulfonates estrogens to inactive estrogen sulfates, whereas steroid sulfatase (STS) hydrolyzes estrone sulfate to estrone.	Estrone	149-156	sulfotransferase family 1E member 1	Homo sapiens	44-47
12782487-0	2003	Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase.	Polychlorinated Biphenyls	44-68	sulfotransferase family 1E member 1	Homo sapiens	132-157
12782487-1	2003	Certain hydroxylated polychlorinated biphenyls (OH-PCBs) inhibit the human estrogen sulfotransferase (hEST) at subnanomolar concentrations, suggesting a possible pathway for PCB toxicity due to environmental exposure in humans.	Polychlorinated Biphenyls	21-46	sulfotransferase family 1E member 1	Homo sapiens	75-100
12782487-1	2003	Certain hydroxylated polychlorinated biphenyls (OH-PCBs) inhibit the human estrogen sulfotransferase (hEST) at subnanomolar concentrations, suggesting a possible pathway for PCB toxicity due to environmental exposure in humans.	Polychlorinated Biphenyls	21-46	sulfotransferase family 1E member 1	Homo sapiens	102-106
12782487-1	2003	Certain hydroxylated polychlorinated biphenyls (OH-PCBs) inhibit the human estrogen sulfotransferase (hEST) at subnanomolar concentrations, suggesting a possible pathway for PCB toxicity due to environmental exposure in humans.	oh-pcbs	48-55	sulfotransferase family 1E member 1	Homo sapiens	75-100
12782487-1	2003	Certain hydroxylated polychlorinated biphenyls (OH-PCBs) inhibit the human estrogen sulfotransferase (hEST) at subnanomolar concentrations, suggesting a possible pathway for PCB toxicity due to environmental exposure in humans.	oh-pcbs	48-55	sulfotransferase family 1E member 1	Homo sapiens	102-106
12782487-2	2003	To address the structural basis of the inhibition, we have determined the crystal structure of hEST in the presence of the sulfuryl donor product 3 -phosphoadenosine 5 -phosphate and the OH-PCB 4,4 -OH 3,5,3,5 -tetraCB.	adenosine 3'-phosphate-5'-phosphate	146-178	sulfotransferase family 1E member 1	Homo sapiens	95-99
12782487-5	2003	The crystal structure of hEST with the OH-PCB bound gives physical evidence that certain OH-PCBs can mimic binding of estrogenic compounds in biological systems.	oh-pcbs	89-96	sulfotransferase family 1E member 1	Homo sapiens	25-29
12515476-0	2003	Synthesis of a bisubstrate analogue targeting estrogen sulfotransferase.	bisubstrate	15-26	sulfotransferase family 1E member 1	Homo sapiens	46-71
12124314-2	2002	Experiments using the recombinant sulfotransferases and human liver cytosols indicated that phenol sulfotransferase (ST1A3) and estrogen sulfotransferase (ST1E4) were the sulfotransferases most active toward troglitazone.	Troglitazone	208-220	sulfotransferase family 1E member 1	Homo sapiens	128-153
21782608-5	2002	4-Hydroxylonazolac was conjugated in the cell lines expressing the following enzymes, in this order, human SULT1E1>1A1 (*1>*V)>1A2 (*1>*2)>1A3.	Hydroxylonazolac	0-18	sulfotransferase family 1E member 1	Homo sapiens	107-114
12095948-1	2002	Using purified human type 1 estrogen sulfotransferase (hEST1), we show that the best substrate for this enzyme is 2-hydroxy-catecholestrogen.	2-hydroxy-catecholestrogen	114-140	sulfotransferase family 1E member 1	Homo sapiens	28-53
12095948-1	2002	Using purified human type 1 estrogen sulfotransferase (hEST1), we show that the best substrate for this enzyme is 2-hydroxy-catecholestrogen.	2-hydroxy-catecholestrogen	114-140	sulfotransferase family 1E member 1	Homo sapiens	55-60
12095948-4	2002	Indeed, hEST1 may also be involved in the production of stable precursors for local steroid biosynthesis or in the activation of promutagenic estrogen metabolites into carcinogens.	Steroids	84-91	sulfotransferase family 1E member 1	Homo sapiens	8-13
11884392-1	2002	Estrogen sulfotransferase (EST) transfers the sulfate group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to estrogenic steroids.	Sulfates	46-53	sulfotransferase family 1E member 1	Homo sapiens	0-25
11884392-1	2002	Estrogen sulfotransferase (EST) transfers the sulfate group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to estrogenic steroids.	Phosphoadenosine Phosphosulfate	65-102	sulfotransferase family 1E member 1	Homo sapiens	0-25
11884392-1	2002	Estrogen sulfotransferase (EST) transfers the sulfate group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to estrogenic steroids.	Phosphoadenosine Phosphosulfate	104-108	sulfotransferase family 1E member 1	Homo sapiens	0-25
11884392-1	2002	Estrogen sulfotransferase (EST) transfers the sulfate group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to estrogenic steroids.	Steroids	124-132	sulfotransferase family 1E member 1	Homo sapiens	0-25
11906176-7	2002	SULT1E1 had the lowest apparent K(m) values, 0.31, 0.18, 0.27, and 0.22 microM for 4-OHE1, 4-OHE2, 2-OHE1, and 2-OHE2, respectively.	4-hydroxyestrone	83-89	sulfotransferase family 1E member 1	Homo sapiens	0-7
11906176-7	2002	SULT1E1 had the lowest apparent K(m) values, 0.31, 0.18, 0.27, and 0.22 microM for 4-OHE1, 4-OHE2, 2-OHE1, and 2-OHE2, respectively.	4-ohe2	91-97	sulfotransferase family 1E member 1	Homo sapiens	0-7
11906176-7	2002	SULT1E1 had the lowest apparent K(m) values, 0.31, 0.18, 0.27, and 0.22 microM for 4-OHE1, 4-OHE2, 2-OHE1, and 2-OHE2, respectively.	2-hydroxyestrone	99-105	sulfotransferase family 1E member 1	Homo sapiens	0-7
11906176-7	2002	SULT1E1 had the lowest apparent K(m) values, 0.31, 0.18, 0.27, and 0.22 microM for 4-OHE1, 4-OHE2, 2-OHE1, and 2-OHE2, respectively.	2-hydroxyestradiol	111-117	sulfotransferase family 1E member 1	Homo sapiens	0-7
11889178-7	2002	We found marked inhibition of SULT1E1 by various PHAH-OHs, in particular by compounds with two adjacent halogen substituents around the hydroxyl group that were effective at (sub)nanomolar concentrations.	Halogens	104-111	sulfotransferase family 1E member 1	Homo sapiens	30-37
15618673-4	2002	However, k(cat)/K(m) values observed indicated that these phytoestrogens were sulfated predominantly by SULT1A1 and SULT1E1 with K(m) values of 0.3 and 0.7 microM for GS and 1.9 and 3.4 microM for DZ, respectively.	daidzein	197-199	sulfotransferase family 1E member 1	Homo sapiens	116-123
15618673-5	2002	DZ and GS strongly inhibited the sulfation of the endogenous substrate, beta-estradiol, by SULT1E1 in a non-competitive manner with K(i) values of 14 and 7 microM, respectively, suggesting that these phytoestrogens might affect tissue levels of beta-estradiol in the human.	Estradiol	72-86	sulfotransferase family 1E member 1	Homo sapiens	91-98
15618673-5	2002	DZ and GS strongly inhibited the sulfation of the endogenous substrate, beta-estradiol, by SULT1E1 in a non-competitive manner with K(i) values of 14 and 7 microM, respectively, suggesting that these phytoestrogens might affect tissue levels of beta-estradiol in the human.	Estradiol	245-259	sulfotransferase family 1E member 1	Homo sapiens	91-98
15618673-7	2002	High k(cat)/K(m) values were observed for the sulfation of BPA by SULT1A1, NP by SULT1A1 and SULT1E1, and t-OP by SULT1E1 and SULT2A1.	bisphenol A	59-62	sulfotransferase family 1E member 1	Homo sapiens	93-100
15618673-7	2002	High k(cat)/K(m) values were observed for the sulfation of BPA by SULT1A1, NP by SULT1A1 and SULT1E1, and t-OP by SULT1E1 and SULT2A1.	bisphenol A	59-62	sulfotransferase family 1E member 1	Homo sapiens	114-121
12481303-9	2002	Human phenol-sulfating sulfotransferase and human estrogen sulfotransferase are the major enzymes for the sulfation of 4-OH-TAM.	hydroxytamoxifen	119-127	sulfotransferase family 1E member 1	Homo sapiens	50-75
11795394-7	2001	The finding that certain hydroxylated polychlorinated biphenyls are potent inhibitors of the human estrogen sulfotransferase enzyme raises the possibility that environmental chemicals can cause endocrine disruption by enhancing endogenous estrogen activity through inhibition of steroid transformation enzymes such as estrogen sulfotransferase.	Polychlorinated Biphenyls	38-63	sulfotransferase family 1E member 1	Homo sapiens	99-124
11795394-7	2001	The finding that certain hydroxylated polychlorinated biphenyls are potent inhibitors of the human estrogen sulfotransferase enzyme raises the possibility that environmental chemicals can cause endocrine disruption by enhancing endogenous estrogen activity through inhibition of steroid transformation enzymes such as estrogen sulfotransferase.	Polychlorinated Biphenyls	38-63	sulfotransferase family 1E member 1	Homo sapiens	318-343
11795394-7	2001	The finding that certain hydroxylated polychlorinated biphenyls are potent inhibitors of the human estrogen sulfotransferase enzyme raises the possibility that environmental chemicals can cause endocrine disruption by enhancing endogenous estrogen activity through inhibition of steroid transformation enzymes such as estrogen sulfotransferase.	Steroids	279-286	sulfotransferase family 1E member 1	Homo sapiens	99-124
11795394-7	2001	The finding that certain hydroxylated polychlorinated biphenyls are potent inhibitors of the human estrogen sulfotransferase enzyme raises the possibility that environmental chemicals can cause endocrine disruption by enhancing endogenous estrogen activity through inhibition of steroid transformation enzymes such as estrogen sulfotransferase.	Steroids	279-286	sulfotransferase family 1E member 1	Homo sapiens	318-343
11358677-3	2001	We overexpressed hEST1 in Escherichia coli in fusion with GST, then purified the enzyme using a glutathione affinity column, and obtained GST-free enzyme by digestion with thrombin.	Glutathione	96-107	sulfotransferase family 1E member 1	Homo sapiens	17-22
11358677-4	2001	Using [35S]-phosphosadenosine phosphosulfate (PAPS) as cofactor, we showed that hEST1 efficiently metabolizes the transformation of 2-OH-E2 and 2-OH-E1.	[35s]-phosphosadenosine phosphosulfate	6-44	sulfotransferase family 1E member 1	Homo sapiens	80-85
11358677-4	2001	Using [35S]-phosphosadenosine phosphosulfate (PAPS) as cofactor, we showed that hEST1 efficiently metabolizes the transformation of 2-OH-E2 and 2-OH-E1.	PAPS	46-50	sulfotransferase family 1E member 1	Homo sapiens	80-85
11358677-4	2001	Using [35S]-phosphosadenosine phosphosulfate (PAPS) as cofactor, we showed that hEST1 efficiently metabolizes the transformation of 2-OH-E2 and 2-OH-E1.	2-hydroxyestradiol	132-139	sulfotransferase family 1E member 1	Homo sapiens	80-85
11358677-4	2001	Using [35S]-phosphosadenosine phosphosulfate (PAPS) as cofactor, we showed that hEST1 efficiently metabolizes the transformation of 2-OH-E2 and 2-OH-E1.	2-hydroxyestrone	144-151	sulfotransferase family 1E member 1	Homo sapiens	80-85
11159808-6	2001	This coupled assay uses the sulfation of 17beta-[(3)H]estradiol catalyzed by recombinant human SULT1E1 to measure PAPS, which has been generated by PAPSS during the initial step of the assay.	17beta-[(3)h]estradiol	41-63	sulfotransferase family 1E member 1	Homo sapiens	95-102
11159808-7	2001	SULT1E1 proved to be ideal for this application both because of its relative resistance to inhibition by ATP, a substrate for the PAPSS-catalyzed step, and because of its low K(m) values for both PAPS (58 nM) and estradiol (29 nM).	Adenosine Triphosphate	105-108	sulfotransferase family 1E member 1	Homo sapiens	0-7
11159808-7	2001	SULT1E1 proved to be ideal for this application both because of its relative resistance to inhibition by ATP, a substrate for the PAPSS-catalyzed step, and because of its low K(m) values for both PAPS (58 nM) and estradiol (29 nM).	Estradiol	213-222	sulfotransferase family 1E member 1	Homo sapiens	0-7
10913346-2	2000	Analysis of calcium flow in transfected cells, along with sequence analysis, revealed that the EST encoded a functionally inactive protein, lacking the segment corresponding to the C-terminal part of the putative receptor protein.	Calcium	12-19	sulfotransferase family 1E member 1	Homo sapiens	95-98
11070355-0	2000	Quercetin and resveratrol potently reduce estrogen sulfotransferase activity in normal human mammary epithelial cells.	Quercetin	0-9	sulfotransferase family 1E member 1	Homo sapiens	42-67
11070355-0	2000	Quercetin and resveratrol potently reduce estrogen sulfotransferase activity in normal human mammary epithelial cells.	Resveratrol	14-25	sulfotransferase family 1E member 1	Homo sapiens	42-67
11070355-2	2000	In the present study we examined the inhibitory effect of the dietary polyphenols quercetin and resveratrol on EST activity, i.e. 17beta-estradiol (E2) sulfation.	polyphenols quercetin	70-91	sulfotransferase family 1E member 1	Homo sapiens	111-114
11070355-2	2000	In the present study we examined the inhibitory effect of the dietary polyphenols quercetin and resveratrol on EST activity, i.e. 17beta-estradiol (E2) sulfation.	Resveratrol	96-107	sulfotransferase family 1E member 1	Homo sapiens	111-114
11070355-2	2000	In the present study we examined the inhibitory effect of the dietary polyphenols quercetin and resveratrol on EST activity, i.e. 17beta-estradiol (E2) sulfation.	Estradiol	130-146	sulfotransferase family 1E member 1	Homo sapiens	111-114
11070355-4	2000	In fact, both polyphenols could serve as substrates for EST.	Polyphenols	14-25	sulfotransferase family 1E member 1	Homo sapiens	56-59
11070355-6	2000	The mean baseline EST activity (E2 sulfate formation) in the HME cells was 4.4 pmol/h per mg protein.	e2 sulfate	32-42	sulfotransferase family 1E member 1	Homo sapiens	18-21
10803601-0	2000	Potent inhibition of estrogen sulfotransferase by hydroxylated PCB metabolites: a novel pathway explaining the estrogenic activity of PCBs.	Polychlorinated Biphenyls	134-138	sulfotransferase family 1E member 1	Homo sapiens	21-46
10803601-4	2000	In the present study we demonstrate that various environmentally relevant PCB-OHs are extremely potent inhibitors of human estrogen sulfotransferase, strongly suggesting that they indirectly induce estrogenic activity by increasing estradiol bioavailability in target tissues.	Estradiol	232-241	sulfotransferase family 1E member 1	Homo sapiens	123-148
10623578-3	2000	Among the other six sulfotransferases, the simple phenol (P)-form phenol sulfotransferase and estrogen sulfotransferase appeared to be considerably more active toward environmental estrogens than the other four sulfotransferases.	Phenol	50-56	sulfotransferase family 1E member 1	Homo sapiens	94-119
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	126-163	sulfotransferase family 1E member 1	Homo sapiens	0-25
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	126-163	sulfotransferase family 1E member 1	Homo sapiens	27-30
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	165-169	sulfotransferase family 1E member 1	Homo sapiens	0-25
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	165-169	sulfotransferase family 1E member 1	Homo sapiens	27-30
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Sulfates	156-163	sulfotransferase family 1E member 1	Homo sapiens	0-25
10659700-1	1999	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfoconjugation and inactivation of estrogens using 3"-phosphoadenosine-5"-phosphosulfate (PAPS) as an activated sulfate donor.	Sulfates	156-163	sulfotransferase family 1E member 1	Homo sapiens	27-30
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Pregnenolone	108-120	sulfotransferase family 1E member 1	Homo sapiens	55-58
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Pregnenolone	108-120	sulfotransferase family 1E member 1	Homo sapiens	88-91
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Estradiol	125-134	sulfotransferase family 1E member 1	Homo sapiens	55-58
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Estradiol	125-134	sulfotransferase family 1E member 1	Homo sapiens	88-91
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Sulfates	209-216	sulfotransferase family 1E member 1	Homo sapiens	55-58
10659700-2	1999	A finding of undetermined significance in the study of EST has been that the guinea pig EST is able to bind pregnenolone and estradiol with high affinity in the presence of PAP, the reaction by-product of the sulfate donor PAPS.	Sulfates	209-216	sulfotransferase family 1E member 1	Homo sapiens	88-91
10659700-5	1999	We found that, in the presence of PAP, both recombinant mouse and human EST were able to bind estradiol with high affinity but only the human EST was able to bind pregnenolone.	Phosphoadenosine Phosphosulfate	34-37	sulfotransferase family 1E member 1	Homo sapiens	72-75
10659700-5	1999	We found that, in the presence of PAP, both recombinant mouse and human EST were able to bind estradiol with high affinity but only the human EST was able to bind pregnenolone.	Pregnenolone	163-175	sulfotransferase family 1E member 1	Homo sapiens	142-145
10659700-7	1999	Furthermore, we demonstrate that the promiscuity of human EST in steroid binding is mirrored by a correspondingly low substrate specificity in its enzymatic activity as a sulfotransferase.	Steroids	65-72	sulfotransferase family 1E member 1	Homo sapiens	58-61
10541560-7	1999	Our results with normal endometrium support in-vitro data showing that SULT1E1 expression is regulated by progesterone.	Progesterone	106-118	sulfotransferase family 1E member 1	Homo sapiens	71-78
10514486-0	1999	Substrate gating confers steroid specificity to estrogen sulfotransferase.	Steroids	25-32	sulfotransferase family 1E member 1	Homo sapiens	48-73
10514486-1	1999	Estrogen sulfotransferase (EST) exhibits a high substrate specificity and catalytic efficiency toward estrogens such as estradiol (E2) but insignificant ability to sulfate hydroxysteroids such as dehydroepiandrosterone (DHEA).	Estradiol	120-129	sulfotransferase family 1E member 1	Homo sapiens	0-25
10514486-1	1999	Estrogen sulfotransferase (EST) exhibits a high substrate specificity and catalytic efficiency toward estrogens such as estradiol (E2) but insignificant ability to sulfate hydroxysteroids such as dehydroepiandrosterone (DHEA).	Estradiol	131-133	sulfotransferase family 1E member 1	Homo sapiens	0-25
10514486-1	1999	Estrogen sulfotransferase (EST) exhibits a high substrate specificity and catalytic efficiency toward estrogens such as estradiol (E2) but insignificant ability to sulfate hydroxysteroids such as dehydroepiandrosterone (DHEA).	sulfate hydroxysteroids	164-187	sulfotransferase family 1E member 1	Homo sapiens	0-25
10514486-1	1999	Estrogen sulfotransferase (EST) exhibits a high substrate specificity and catalytic efficiency toward estrogens such as estradiol (E2) but insignificant ability to sulfate hydroxysteroids such as dehydroepiandrosterone (DHEA).	Dehydroepiandrosterone	196-218	sulfotransferase family 1E member 1	Homo sapiens	0-25
10514486-1	1999	Estrogen sulfotransferase (EST) exhibits a high substrate specificity and catalytic efficiency toward estrogens such as estradiol (E2) but insignificant ability to sulfate hydroxysteroids such as dehydroepiandrosterone (DHEA).	Dehydroepiandrosterone	220-224	sulfotransferase family 1E member 1	Homo sapiens	0-25
10464296-9	1999	These findings, together with those on the crystal structure of estrogen sulfotransferase and heparan sulfate N-deacetylase/sulfotransferase, suggest that Lys(128) may be close to the 3-hydroxyl group of beta-glucuronic acid in a HNK-1 acceptor.	Lysine	155-158	sulfotransferase family 1E member 1	Homo sapiens	64-89
10464296-9	1999	These findings, together with those on the crystal structure of estrogen sulfotransferase and heparan sulfate N-deacetylase/sulfotransferase, suggest that Lys(128) may be close to the 3-hydroxyl group of beta-glucuronic acid in a HNK-1 acceptor.	beta-glucuronic acid	204-224	sulfotransferase family 1E member 1	Homo sapiens	64-89
10404840-4	1999	Here we demonstrate for the first time that SULT1E1 catalyzes the facile sulfation of the prohormone T4, the active hormone T3 and the metabolites rT3 and 3,3"-diiodothyronine (3,3"-T2) with preference for rT3 approximately 3,3"-T2 > T3 approximately T4.	3"-diiodothyronine	157-175	sulfotransferase family 1E member 1	Homo sapiens	44-51
10404840-4	1999	Here we demonstrate for the first time that SULT1E1 catalyzes the facile sulfation of the prohormone T4, the active hormone T3 and the metabolites rT3 and 3,3"-diiodothyronine (3,3"-T2) with preference for rT3 approximately 3,3"-T2 > T3 approximately T4.	3,3'-diiodothyronine	177-184	sulfotransferase family 1E member 1	Homo sapiens	44-51
9882778-10	1999	Among the 4 patients with persistent dobutamine-induced STE, 1 patient had persistent ischemia and 2 showed worsening of resting regional function.	Dobutamine	37-47	sulfotransferase family 1E member 1	Homo sapiens	56-59
9882778-11	1999	Although dobutamine-induced STE in patients with old Q-wave infarction referred for CABG cannot identify patients with a higher prevalence of ischemia, the lack of reinduction of this pattern after CABG correlates with absent reinduction of ischemia in most of patients.	Dobutamine	9-19	sulfotransferase family 1E member 1	Homo sapiens	28-31
9855023-0	1998	Bioactivation of the cooked food mutagen N-hydroxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by estrogen sulfotransferase in cultured human mammary epithelial cells.	n-hydroxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine	41-98	sulfotransferase family 1E member 1	Homo sapiens	102-127
9855023-3	1998	The objective of this study was to determine the involvement of estrogen sulfotransferase (EST), the only sulfotransferase identified in HME cells, in the further bioactivation of N-OH-PhIP.	2-hydroxyamino-1-methyl-6-phenylimidazo(4,5-b)pyridine	180-189	sulfotransferase family 1E member 1	Homo sapiens	64-89
9765259-1	1998	Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis.	Vanadates	23-31	sulfotransferase family 1E member 1	Homo sapiens	43-68
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	Phosphoadenosine Phosphosulfate	79-119	sulfotransferase family 1E member 1	Homo sapiens	0-25
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	PAPS	121-125	sulfotransferase family 1E member 1	Homo sapiens	0-25
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	3alpha-phenol	134-147	sulfotransferase family 1E member 1	Homo sapiens	0-25
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	Steroids	168-176	sulfotransferase family 1E member 1	Homo sapiens	0-25
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	Estradiol	185-194	sulfotransferase family 1E member 1	Homo sapiens	0-25
9765259-2	1998	Estrogen sulfotransferase (EST) catalyzes transfer of the 5"-sulfuryl group of adenosine 3"-phosphate 5"-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2).	Estradiol	196-198	sulfotransferase family 1E member 1	Homo sapiens	0-25
9655902-1	1998	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the sulfonation of estrogens at the 3-hydroxyl position by use of 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	135-172	sulfotransferase family 1E member 1	Homo sapiens	0-25
9636676-6	1998	The rates of sulfation of the preferred enantiomers were high, similar to those for the prototype substrates of hEST (beta-estradiol) and hHST (dehydroepiandrosterone).	Estradiol	118-132	sulfotransferase family 1E member 1	Homo sapiens	112-116
9636676-7	1998	Moreover, after a 30-min incubation of S-1-HEP with hEST, 95% of the recovered alcohol showed the R-configuration, indicating that several cycles of sulfation and hydrolysis had led to the depletion of one enantiomer and to the enrichment of the other enantiomer.	Alcohols	79-86	sulfotransferase family 1E member 1	Homo sapiens	52-56
9556564-1	1998	Estrogen sulfotransferase (EST) catalyzes the transfer of the sulfuryl group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to 17beta-estradiol (E2).	Phosphoadenosine Phosphosulfate	82-119	sulfotransferase family 1E member 1	Homo sapiens	0-25
9556564-1	1998	Estrogen sulfotransferase (EST) catalyzes the transfer of the sulfuryl group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to 17beta-estradiol (E2).	Phosphoadenosine Phosphosulfate	121-125	sulfotransferase family 1E member 1	Homo sapiens	0-25
9556564-1	1998	Estrogen sulfotransferase (EST) catalyzes the transfer of the sulfuryl group from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to 17beta-estradiol (E2).	Estradiol	130-146	sulfotransferase family 1E member 1	Homo sapiens	0-25
9495883-1	1998	Estrogen sulfotransferase (EST) catalyzes the specific sulfonation of estrogen at the 3"-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	113-150	sulfotransferase family 1E member 1	Homo sapiens	0-25
9495883-1	1998	Estrogen sulfotransferase (EST) catalyzes the specific sulfonation of estrogen at the 3"-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	113-150	sulfotransferase family 1E member 1	Homo sapiens	27-30
9495883-1	1998	Estrogen sulfotransferase (EST) catalyzes the specific sulfonation of estrogen at the 3"-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Sulfates	143-150	sulfotransferase family 1E member 1	Homo sapiens	0-25
9495883-1	1998	Estrogen sulfotransferase (EST) catalyzes the specific sulfonation of estrogen at the 3"-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Sulfates	143-150	sulfotransferase family 1E member 1	Homo sapiens	27-30
9495883-8	1998	Interestingly, paired-group analysis revealed a statistically significant difference in the hepatic expression of EST protein and activity between alcohol users and nonusers.	Alcohols	147-154	sulfotransferase family 1E member 1	Homo sapiens	114-117
9495883-12	1998	The potential correlation between alcohol consumption and hepatic EST expression deserves further evaluation.	Alcohols	34-41	sulfotransferase family 1E member 1	Homo sapiens	66-69
9566749-0	1998	Expression of human estrogen sulfotransferase in Salmonella typhimurium: differences between hHST and hEST in the enantioselective activation of 1-hydroxyethylpyrene to a mutagen.	1-(1-Pyrenyl)ethanol	145-165	sulfotransferase family 1E member 1	Homo sapiens	20-45
9566749-0	1998	Expression of human estrogen sulfotransferase in Salmonella typhimurium: differences between hHST and hEST in the enantioselective activation of 1-hydroxyethylpyrene to a mutagen.	1-(1-Pyrenyl)ethanol	145-165	sulfotransferase family 1E member 1	Homo sapiens	102-106
9348232-1	1997	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the specific sulfonation of estrogens at the 3-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	140-177	sulfotransferase family 1E member 1	Homo sapiens	0-25
9348232-1	1997	Estrogen sulfotransferase (EST) is a cytosolic enzyme that catalyzes the specific sulfonation of estrogens at the 3-hydroxyl position using 3"-phosphoadenosine-5"-phosphosulfate as an activated sulfate donor.	Phosphoadenosine Phosphosulfate	140-177	sulfotransferase family 1E member 1	Homo sapiens	27-30
9068609-5	1997	These enzymes are two forms of phenol ST (PST), the phenol-sulfating and the monoamine-sulfating forms of PST (P-PST and M-PST, respectively), an estrogen sulfotransferase (EST), and a hydroxysteroid ST, dehydroepiandrosterone ST (DHEA-ST).	Phenol	31-37	sulfotransferase family 1E member 1	Homo sapiens	146-171
8943792-9	1996	Estrogen sulfotransferase catalyzes the conversion of estrone and estradiol to their inactive sulfated forms and could thus play a major role in the control of estrogen levels in target tissues.	Estrone	54-61	sulfotransferase family 1E member 1	Homo sapiens	0-25
8943792-9	1996	Estrogen sulfotransferase catalyzes the conversion of estrone and estradiol to their inactive sulfated forms and could thus play a major role in the control of estrogen levels in target tissues.	Estradiol	66-75	sulfotransferase family 1E member 1	Homo sapiens	0-25
8943792-10	1996	Recently, using a probe derived from bovine estrogen sulfotransferase, we have cloned a cDNA and gene that we first named human estrogen sulfotransferase (hEST) since the expressed enzyme is able to transform estrone to estrone sulfate.	Estrone	209-216	sulfotransferase family 1E member 1	Homo sapiens	128-153
8943792-10	1996	Recently, using a probe derived from bovine estrogen sulfotransferase, we have cloned a cDNA and gene that we first named human estrogen sulfotransferase (hEST) since the expressed enzyme is able to transform estrone to estrone sulfate.	Estrone	209-216	sulfotransferase family 1E member 1	Homo sapiens	155-159
8943792-10	1996	Recently, using a probe derived from bovine estrogen sulfotransferase, we have cloned a cDNA and gene that we first named human estrogen sulfotransferase (hEST) since the expressed enzyme is able to transform estrone to estrone sulfate.	estrone sulfate	220-235	sulfotransferase family 1E member 1	Homo sapiens	128-153
8943792-10	1996	Recently, using a probe derived from bovine estrogen sulfotransferase, we have cloned a cDNA and gene that we first named human estrogen sulfotransferase (hEST) since the expressed enzyme is able to transform estrone to estrone sulfate.	estrone sulfate	220-235	sulfotransferase family 1E member 1	Homo sapiens	155-159
8625916-0	1996	Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone.	Progesterone	85-97	sulfotransferase family 1E member 1	Homo sapiens	14-39
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Estradiol	112-114	sulfotransferase family 1E member 1	Homo sapiens	0-25
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Estradiol	112-114	sulfotransferase family 1E member 1	Homo sapiens	27-31
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Estrone	119-126	sulfotransferase family 1E member 1	Homo sapiens	0-25
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Estrone	119-126	sulfotransferase family 1E member 1	Homo sapiens	27-31
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Steroids	237-244	sulfotransferase family 1E member 1	Homo sapiens	0-25
8625916-4	1996	Estrogen sulfotransferase (hEST), a distinct form of human cytosolic sulfotransferase (ST) with an affinity for E2 and estrone at low nanomolar concentrations, has recently been cloned and expressed in mammalian cells and in bacteria (J Steroid Biochem Mol Biol 52:529, 1995).	Steroids	237-244	sulfotransferase family 1E member 1	Homo sapiens	27-31
8625916-6	1996	This report describes the specific induction of hEST in human Ishikawa endometrial adenocarcinoma cells by progesterone as a model for the increases in estrogen sulfation observed in women during the secretory phase of the menstrual cycle.	Progesterone	107-119	sulfotransferase family 1E member 1	Homo sapiens	48-52
8625916-11	1996	The induction of hEST by progesterone was inhibited by RU-486, indicating that progesterone is acting via the progesterone receptor.	Progesterone	25-37	sulfotransferase family 1E member 1	Homo sapiens	17-21
8625916-11	1996	The induction of hEST by progesterone was inhibited by RU-486, indicating that progesterone is acting via the progesterone receptor.	Mifepristone	55-61	sulfotransferase family 1E member 1	Homo sapiens	17-21
8625916-11	1996	The induction of hEST by progesterone was inhibited by RU-486, indicating that progesterone is acting via the progesterone receptor.	Progesterone	79-91	sulfotransferase family 1E member 1	Homo sapiens	17-21
7779757-4	1995	Purified hEST-1 migrated with an apparent molecular mass of 35,000 Da during SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	77-80	sulfotransferase family 1E member 1	Homo sapiens	9-15
7779757-4	1995	Purified hEST-1 migrated with an apparent molecular mass of 35,000 Da during SDS-polyacrylamide gel electrophoresis.	polyacrylamide gels	81-99	sulfotransferase family 1E member 1	Homo sapiens	9-15
7779757-10	1995	hEST-1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM.	Sulfates	17-25	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-10	1995	hEST-1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM.	Estradiol	26-40	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-10	1995	hEST-1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM.	Estrone	45-52	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Dehydroepiandrosterone	21-43	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Pregnenolone	45-57	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Ethinyl Estradiol	59-75	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	1-naphthol	81-91	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Hydrocortisone	142-150	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Testosterone	152-164	sulfotransferase family 1E member 1	Homo sapiens	0-6
7779757-11	1995	hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.	Dopamine	169-177	sulfotransferase family 1E member 1	Homo sapiens	0-6
7980593-4	1994	Using molecular techniques, point mutations that substituted alanines for the putative critical residues were introduced into the cDNA for estrogen sulfotransferase.	Alanine	61-69	sulfotransferase family 1E member 1	Homo sapiens	139-164
7966997-7	1994	Plasma norepinephrine levels increased significantly at maximal workload in STE patients, as compared to the other groups.	Norepinephrine	7-21	sulfotransferase family 1E member 1	Homo sapiens	76-79
8187949-6	1994	Transfection of expression vectors encoding human estrogen sulfotransferase and dehydroepiandrosterone (DHEA) sulfotransferase in human adrenal adenocarcinoma SW-13 cells indicates that estrogen sulfotransferase transforms estrone more specifically, whereas DHEA sulfotransferase is more specific for DHEA and pregnenolone.	Estrone	223-230	sulfotransferase family 1E member 1	Homo sapiens	50-75
8187949-6	1994	Transfection of expression vectors encoding human estrogen sulfotransferase and dehydroepiandrosterone (DHEA) sulfotransferase in human adrenal adenocarcinoma SW-13 cells indicates that estrogen sulfotransferase transforms estrone more specifically, whereas DHEA sulfotransferase is more specific for DHEA and pregnenolone.	Estrone	223-230	sulfotransferase family 1E member 1	Homo sapiens	186-211
8187949-6	1994	Transfection of expression vectors encoding human estrogen sulfotransferase and dehydroepiandrosterone (DHEA) sulfotransferase in human adrenal adenocarcinoma SW-13 cells indicates that estrogen sulfotransferase transforms estrone more specifically, whereas DHEA sulfotransferase is more specific for DHEA and pregnenolone.	Dehydroepiandrosterone	104-108	sulfotransferase family 1E member 1	Homo sapiens	186-211
8187949-6	1994	Transfection of expression vectors encoding human estrogen sulfotransferase and dehydroepiandrosterone (DHEA) sulfotransferase in human adrenal adenocarcinoma SW-13 cells indicates that estrogen sulfotransferase transforms estrone more specifically, whereas DHEA sulfotransferase is more specific for DHEA and pregnenolone.	Pregnenolone	310-322	sulfotransferase family 1E member 1	Homo sapiens	50-75
8187949-6	1994	Transfection of expression vectors encoding human estrogen sulfotransferase and dehydroepiandrosterone (DHEA) sulfotransferase in human adrenal adenocarcinoma SW-13 cells indicates that estrogen sulfotransferase transforms estrone more specifically, whereas DHEA sulfotransferase is more specific for DHEA and pregnenolone.	Pregnenolone	310-322	sulfotransferase family 1E member 1	Homo sapiens	186-211
1582375-3	1992	Investigation of the thermostability and inhibition by 2,6-dichloro-4-nitrophenol (DCNP) of the 1-naphthol and estrone sulfotransferase (ST) activities revealed that the estrone ST activity was more thermolabile and more readily inhibited by DCNP than was the 1-naphthol ST activity.	2,6-dichloro-4-nitrophenol	55-81	sulfotransferase family 1E member 1	Homo sapiens	111-135
1582375-3	1992	Investigation of the thermostability and inhibition by 2,6-dichloro-4-nitrophenol (DCNP) of the 1-naphthol and estrone sulfotransferase (ST) activities revealed that the estrone ST activity was more thermolabile and more readily inhibited by DCNP than was the 1-naphthol ST activity.	2,6-dichloro-4-nitrophenol	83-87	sulfotransferase family 1E member 1	Homo sapiens	111-135
1582375-3	1992	Investigation of the thermostability and inhibition by 2,6-dichloro-4-nitrophenol (DCNP) of the 1-naphthol and estrone sulfotransferase (ST) activities revealed that the estrone ST activity was more thermolabile and more readily inhibited by DCNP than was the 1-naphthol ST activity.	2,6-dichloro-4-nitrophenol	242-246	sulfotransferase family 1E member 1	Homo sapiens	111-135
1582375-3	1992	Investigation of the thermostability and inhibition by 2,6-dichloro-4-nitrophenol (DCNP) of the 1-naphthol and estrone sulfotransferase (ST) activities revealed that the estrone ST activity was more thermolabile and more readily inhibited by DCNP than was the 1-naphthol ST activity.	1-naphthol	260-270	sulfotransferase family 1E member 1	Homo sapiens	111-135
34154468-6	2022	The ester bond formation between 3,5-dihydroxydecanoic acid and mannitol or arabitol is catalyzed by the esterase (Est1).	3,5-dihydroxydecanoic acid	33-59	sulfotransferase family 1E member 1	Homo sapiens	115-119
34154468-6	2022	The ester bond formation between 3,5-dihydroxydecanoic acid and mannitol or arabitol is catalyzed by the esterase (Est1).	Mannitol	64-72	sulfotransferase family 1E member 1	Homo sapiens	115-119
34154468-6	2022	The ester bond formation between 3,5-dihydroxydecanoic acid and mannitol or arabitol is catalyzed by the esterase (Est1).	arabitol	76-84	sulfotransferase family 1E member 1	Homo sapiens	115-119
34740292-8	2021	The inhibition kinetic parameters (Ki) were 1.73 muM and 1.81 muM for the inhibition of 4"-OH-PCB106 towards SULT1B1 and SULT1E1, respectively.	4"-oh-pcb106	88-100	sulfotransferase family 1E member 1	Homo sapiens	121-128
34325320-4	2021	SULT1E1 was site-specifically immobilized on transparent glass slides via a hexahistidine-tag in a multi-step procedure.	His-His-His-His-His-His	76-89	sulfotransferase family 1E member 1	Homo sapiens	0-7
34269579-0	2021	Mapping Chromone-3-Phenylcarboxamide Pharmacophore: Quid Est Veritas?	chromone-3-phenylcarboxamide	8-36	sulfotransferase family 1E member 1	Homo sapiens	57-60
34157297-6	2021	For the sulfotransferase gene, phosphorylated nuclear receptors ERalpha and RORalpha, at Ser212 and Ser100, respectively, bind their response elements to activate the SULT1E1 promoter in women.	ZP120	100-106	sulfotransferase family 1E member 1	Homo sapiens	167-174
35528018-9	2022	MOP was chosen as the representative phthalate monoester to determine the inhibition kinetic parameters (K i) towards SULT1B1 and SULT1E1.	mono-n-octyl phthalate	0-3	sulfotransferase family 1E member 1	Homo sapiens	130-137
35281274-4	2022	The optimized protocol was then successfully transferred to other sulfonation reactions catalyzed by SULT2A1, SULT1E1, or SULT1B1.	sulfonation	66-77	sulfotransferase family 1E member 1	Homo sapiens	110-117
35059953-5	2022	Results from Western blotting showed that Ox-LDL induces the protein expression of both SULT1E1 and peroxisome proliferator-activated receptor (PPAR) gamma in human umbilical vein endothelial cells (HUVECs), and then that a PPARgamma antagonist GW9662, but not a PPARalpha antagonist GW6471, inhibited the protein expression of SULT1E1 induced by Ox-LDL.	2-chloro-5-nitrobenzanilide	245-251	sulfotransferase family 1E member 1	Homo sapiens	88-95
35059953-5	2022	Results from Western blotting showed that Ox-LDL induces the protein expression of both SULT1E1 and peroxisome proliferator-activated receptor (PPAR) gamma in human umbilical vein endothelial cells (HUVECs), and then that a PPARgamma antagonist GW9662, but not a PPARalpha antagonist GW6471, inhibited the protein expression of SULT1E1 induced by Ox-LDL.	GW 6471	284-290	sulfotransferase family 1E member 1	Homo sapiens	88-95
35069453-2	2021	The study aimed to investigate the potential inhibitory capability of BPs on four human sulfotransferase isoforms (SULT1A1, SULT1A3, SULT1B1 and SULT1E1) and interpret how to interfere with endocrine hormone metabolism.	bps	70-73	sulfotransferase family 1E member 1	Homo sapiens	145-152
2519212-5	1989	Progesterone added in the medium induced an increase of estrone sulfotransferase in the proliferative endometrium.	Progesterone	0-12	sulfotransferase family 1E member 1	Homo sapiens	56-80
2519212-9	1989	Ishikawa cell line increased estrone sulfotransferase activity with progesterone, somewhat like the physiological conditions.	Progesterone	68-80	sulfotransferase family 1E member 1	Homo sapiens	29-53
3208995-0	1988	Metabolic fate of estradiol in human mammary cancer cells in culture: estrogen sulfate formation and cooperativity exhibited by estrogen sulfotransferase.	Estradiol	18-27	sulfotransferase family 1E member 1	Homo sapiens	128-153
3208995-5	1988	Accumulation of estrogen sulfates resulted from attainment of a steady state between synthesis catalysed by estrogen sulfotransferase and degradation catalysed by estrogen sulfatase.	estrogen sulfates	16-33	sulfotransferase family 1E member 1	Homo sapiens	108-133
6580511-3	1983	However, the average value of the ESFT activity, expressed in nmol of estradiol-3-sulfate (E2S) formed from estradiol (E2)/mg of cytosol protein per hr, was found to be significantly higher in ER +/PGR + tumors (n = 26, 0.18 +/- 0.15, means +/- SD) than in ER -/PGR - tumors (n = 31, 0.08 +/- 0.06, P less than 0.005).	estradiol-3-sulfate	70-89	sulfotransferase family 1E member 1	Homo sapiens	34-38
6580511-3	1983	However, the average value of the ESFT activity, expressed in nmol of estradiol-3-sulfate (E2S) formed from estradiol (E2)/mg of cytosol protein per hr, was found to be significantly higher in ER +/PGR + tumors (n = 26, 0.18 +/- 0.15, means +/- SD) than in ER -/PGR - tumors (n = 31, 0.08 +/- 0.06, P less than 0.005).	Estradiol	91-94	sulfotransferase family 1E member 1	Homo sapiens	34-38
6580511-3	1983	However, the average value of the ESFT activity, expressed in nmol of estradiol-3-sulfate (E2S) formed from estradiol (E2)/mg of cytosol protein per hr, was found to be significantly higher in ER +/PGR + tumors (n = 26, 0.18 +/- 0.15, means +/- SD) than in ER -/PGR - tumors (n = 31, 0.08 +/- 0.06, P less than 0.005).	Estradiol	70-79	sulfotransferase family 1E member 1	Homo sapiens	34-38
6951831-0	1982	Induction of estrogen sulfotransferase in the human endometrium by progesterone in organ culture.	Progesterone	67-79	sulfotransferase family 1E member 1	Homo sapiens	13-38
6951831-2	1982	Whether it plays a similar role in the induction of estrogen sulfotransferase is not known, although this is likely, since estrone sulfate is the main metabolite of E2 when incubated with secretory, but not proliferative, human endometrium.	estrone sulfate	123-138	sulfotransferase family 1E member 1	Homo sapiens	52-77
6951831-4	1982	Estrogen sulfotransferase activity was not detectable in the cytosol of proliferative tissue when cultured in the absence of hormone, but was induced by culture in the presence of progesterone to a value (mean +/- SEM) of 19.7 +/- 5.3 pmol E2-3-sulfate h-1 mg cytosol protein-1.	Progesterone	180-192	sulfotransferase family 1E member 1	Homo sapiens	0-25
6951831-4	1982	Estrogen sulfotransferase activity was not detectable in the cytosol of proliferative tissue when cultured in the absence of hormone, but was induced by culture in the presence of progesterone to a value (mean +/- SEM) of 19.7 +/- 5.3 pmol E2-3-sulfate h-1 mg cytosol protein-1.	e2-3-sulfate	240-252	sulfotransferase family 1E member 1	Homo sapiens	0-25
33665770-2	2021	Recently we reported that a YKEG sequence in human SULT1E1 (hSULT1E1) corresponding to residues 61-64 can bind specifically to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis; its major oxidative lipid component lysophosphatidylcholine (LPC), and its structurally similar lipid, platelet-activating factor (PAF).	Lysophosphatidylcholines	271-294	sulfotransferase family 1E member 1	Homo sapiens	51-58
33665770-2	2021	Recently we reported that a YKEG sequence in human SULT1E1 (hSULT1E1) corresponding to residues 61-64 can bind specifically to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis; its major oxidative lipid component lysophosphatidylcholine (LPC), and its structurally similar lipid, platelet-activating factor (PAF).	Lysophosphatidylcholines	271-294	sulfotransferase family 1E member 1	Homo sapiens	60-68
33665770-2	2021	Recently we reported that a YKEG sequence in human SULT1E1 (hSULT1E1) corresponding to residues 61-64 can bind specifically to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis; its major oxidative lipid component lysophosphatidylcholine (LPC), and its structurally similar lipid, platelet-activating factor (PAF).	Lysophosphatidylcholines	296-299	sulfotransferase family 1E member 1	Homo sapiens	51-58
33665770-2	2021	Recently we reported that a YKEG sequence in human SULT1E1 (hSULT1E1) corresponding to residues 61-64 can bind specifically to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis; its major oxidative lipid component lysophosphatidylcholine (LPC), and its structurally similar lipid, platelet-activating factor (PAF).	Lysophosphatidylcholines	296-299	sulfotransferase family 1E member 1	Homo sapiens	60-68
33665770-5	2021	Results from a sulfating activity assay of hSULT1E1 using 1-hydroxypyrene as the substrate demonstrated that Ox-LDL, LPC, and PAF markedly decreased the sulfating activity of hSULT1E1, whereas native LDL and 1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC) as one of the oxidized phosphatidylcholines showed the opposite effect.	1-hydroxypyrene	58-73	sulfotransferase family 1E member 1	Homo sapiens	43-51
33665770-5	2021	Results from a sulfating activity assay of hSULT1E1 using 1-hydroxypyrene as the substrate demonstrated that Ox-LDL, LPC, and PAF markedly decreased the sulfating activity of hSULT1E1, whereas native LDL and 1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC) as one of the oxidized phosphatidylcholines showed the opposite effect.	1-hydroxypyrene	58-73	sulfotransferase family 1E member 1	Homo sapiens	175-183
33665770-5	2021	Results from a sulfating activity assay of hSULT1E1 using 1-hydroxypyrene as the substrate demonstrated that Ox-LDL, LPC, and PAF markedly decreased the sulfating activity of hSULT1E1, whereas native LDL and 1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC) as one of the oxidized phosphatidylcholines showed the opposite effect.	1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine	208-267	sulfotransferase family 1E member 1	Homo sapiens	175-183
33665770-5	2021	Results from a sulfating activity assay of hSULT1E1 using 1-hydroxypyrene as the substrate demonstrated that Ox-LDL, LPC, and PAF markedly decreased the sulfating activity of hSULT1E1, whereas native LDL and 1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC) as one of the oxidized phosphatidylcholines showed the opposite effect.	1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphorylcholine	269-274	sulfotransferase family 1E member 1	Homo sapiens	175-183
33665770-5	2021	Results from a sulfating activity assay of hSULT1E1 using 1-hydroxypyrene as the substrate demonstrated that Ox-LDL, LPC, and PAF markedly decreased the sulfating activity of hSULT1E1, whereas native LDL and 1-palmitoyl-2-(5"-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC) as one of the oxidized phosphatidylcholines showed the opposite effect.	Phosphatidylcholines	299-319	sulfotransferase family 1E member 1	Homo sapiens	175-183
33884828-8	2021	In conclusion, BMSC-derived exosomal miR-338-3p delays the development of HCC by down-regulating EST1, providing a new promising treatment target for HCC.	mir-338-3p	37-47	sulfotransferase family 1E member 1	Homo sapiens	97-101
33524392-2	2021	Hydroxylated PCBs (OH-PCBs) are major PCB metabolites and high-affinity inhibitors of human estrogen sulfotransferase (SULT1E1), which sulfonates estrogens and thus prevents them from binding to and activating their receptors.	hydroxylated pcbs	0-17	sulfotransferase family 1E member 1	Homo sapiens	92-117
33524392-2	2021	Hydroxylated PCBs (OH-PCBs) are major PCB metabolites and high-affinity inhibitors of human estrogen sulfotransferase (SULT1E1), which sulfonates estrogens and thus prevents them from binding to and activating their receptors.	hydroxylated pcbs	0-17	sulfotransferase family 1E member 1	Homo sapiens	119-126
33524392-2	2021	Hydroxylated PCBs (OH-PCBs) are major PCB metabolites and high-affinity inhibitors of human estrogen sulfotransferase (SULT1E1), which sulfonates estrogens and thus prevents them from binding to and activating their receptors.	oh-pcbs	19-26	sulfotransferase family 1E member 1	Homo sapiens	92-117
33524392-2	2021	Hydroxylated PCBs (OH-PCBs) are major PCB metabolites and high-affinity inhibitors of human estrogen sulfotransferase (SULT1E1), which sulfonates estrogens and thus prevents them from binding to and activating their receptors.	oh-pcbs	19-26	sulfotransferase family 1E member 1	Homo sapiens	119-126
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	oh-pcb1	132-139	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	oh-pcb1	132-139	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	4"-oh-2,6-dichlorobiphenol	141-167	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	4"-oh-2,6-dichlorobiphenol	141-167	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	Estradiol	189-198	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	Estradiol	189-198	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	Estradiol	200-202	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	Estradiol	200-202	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	pap	208-211	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	pap	208-211	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	3"-phosphoadenosine-5-phosphosulfate	213-249	sulfotransferase family 1E member 1	Homo sapiens	70-77
33524392-4	2021	Here, for the first time, the molecular basis of OH-PCB inhibition of SULT1E1 is revealed in a structure of SULT1E1 in complex with OH-PCB1 (4"-OH-2,6-dichlorobiphenol) and its substrates, estradiol (E2) and PAP (3"-phosphoadenosine-5-phosphosulfate).	3"-phosphoadenosine-5-phosphosulfate	213-249	sulfotransferase family 1E member 1	Homo sapiens	108-115
33524392-8	2021	These OH-PCB resistant mutants were used in stable transfectant studies to demonstrate that OH-PCBs regulate estrogen receptors in cultured human cell lines by binding the OH-PCB binding pocket of SULT1E1.	oh-pcbs	92-99	sulfotransferase family 1E member 1	Homo sapiens	197-204
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	Estradiol	58-74	sulfotransferase family 1E member 1	Homo sapiens	16-23
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	Estradiol	58-74	sulfotransferase family 1E member 1	Homo sapiens	122-129
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	afimoxifene	76-94	sulfotransferase family 1E member 1	Homo sapiens	16-23
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	afimoxifene	76-94	sulfotransferase family 1E member 1	Homo sapiens	122-129
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	Diethylstilbestrol	100-118	sulfotransferase family 1E member 1	Homo sapiens	16-23
33064293-0	2021	Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17beta-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.	Diethylstilbestrol	100-118	sulfotransferase family 1E member 1	Homo sapiens	122-129
33064293-1	2021	BACKGROUND AND OBJECTIVES: Previous studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17beta-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans.	Estradiol	188-204	sulfotransferase family 1E member 1	Homo sapiens	146-153
33064293-1	2021	BACKGROUND AND OBJECTIVES: Previous studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17beta-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans.	Estradiol	206-208	sulfotransferase family 1E member 1	Homo sapiens	146-153
33064293-1	2021	BACKGROUND AND OBJECTIVES: Previous studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17beta-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans.	afimoxifene	211-229	sulfotransferase family 1E member 1	Homo sapiens	146-153
33064293-1	2021	BACKGROUND AND OBJECTIVES: Previous studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17beta-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans.	afimoxifene	231-244	sulfotransferase family 1E member 1	Homo sapiens	146-153
33064293-1	2021	BACKGROUND AND OBJECTIVES: Previous studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17beta-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans.	Diethylstilbestrol	251-269	sulfotransferase family 1E member 1	Homo sapiens	146-153
33064293-2	2021	It is an interesting question whether the genetic polymorphisms of SULT1E1, the gene that encodes the SULT1E1 enzyme, may impact on the metabolism of E2 and these two drug compounds through sulfation.	Estradiol	150-152	sulfotransferase family 1E member 1	Homo sapiens	67-74
33064293-2	2021	It is an interesting question whether the genetic polymorphisms of SULT1E1, the gene that encodes the SULT1E1 enzyme, may impact on the metabolism of E2 and these two drug compounds through sulfation.	Estradiol	150-152	sulfotransferase family 1E member 1	Homo sapiens	102-109
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Estradiol	187-189	sulfotransferase family 1E member 1	Homo sapiens	84-91
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Estradiol	187-189	sulfotransferase family 1E member 1	Homo sapiens	162-169
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	afimoxifene	191-204	sulfotransferase family 1E member 1	Homo sapiens	84-91
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	afimoxifene	191-204	sulfotransferase family 1E member 1	Homo sapiens	162-169
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Diethylstilbestrol	210-228	sulfotransferase family 1E member 1	Homo sapiens	84-91
33064293-3	2021	METHODS: In this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Diethylstilbestrol	210-228	sulfotransferase family 1E member 1	Homo sapiens	162-169
33064293-5	2021	RESULTS: Purified SULT1E1 allozymes were shown to display differential sulfating activities toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Estradiol	99-101	sulfotransferase family 1E member 1	Homo sapiens	18-25
33064293-5	2021	RESULTS: Purified SULT1E1 allozymes were shown to display differential sulfating activities toward E2, 4OH-tamoxifen, and diethylstilbestrol.	afimoxifene	103-116	sulfotransferase family 1E member 1	Homo sapiens	18-25
33064293-5	2021	RESULTS: Purified SULT1E1 allozymes were shown to display differential sulfating activities toward E2, 4OH-tamoxifen, and diethylstilbestrol.	Diethylstilbestrol	122-140	sulfotransferase family 1E member 1	Homo sapiens	18-25
33064293-6	2021	Kinetic analysis revealed further distinct Km (reflecting substrate affinity) and Vmax (reflecting catalytic activity) values of the five SULT1E1 allozymes with E2, 4OH-tamoxifen, and diethylstilbestrol as substrates.	Estradiol	161-163	sulfotransferase family 1E member 1	Homo sapiens	138-145
33064293-6	2021	Kinetic analysis revealed further distinct Km (reflecting substrate affinity) and Vmax (reflecting catalytic activity) values of the five SULT1E1 allozymes with E2, 4OH-tamoxifen, and diethylstilbestrol as substrates.	afimoxifene	165-178	sulfotransferase family 1E member 1	Homo sapiens	138-145
33064293-6	2021	Kinetic analysis revealed further distinct Km (reflecting substrate affinity) and Vmax (reflecting catalytic activity) values of the five SULT1E1 allozymes with E2, 4OH-tamoxifen, and diethylstilbestrol as substrates.	Diethylstilbestrol	184-202	sulfotransferase family 1E member 1	Homo sapiens	138-145
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estradiol	87-89	sulfotransferase family 1E member 1	Homo sapiens	136-143
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estradiol	87-89	sulfotransferase family 1E member 1	Homo sapiens	289-296
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estradiol	217-219	sulfotransferase family 1E member 1	Homo sapiens	136-143
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estradiol	217-219	sulfotransferase family 1E member 1	Homo sapiens	289-296
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estetrol	221-224	sulfotransferase family 1E member 1	Homo sapiens	136-143
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Estetrol	221-224	sulfotransferase family 1E member 1	Homo sapiens	289-296
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Tamoxifen	225-234	sulfotransferase family 1E member 1	Homo sapiens	136-143
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Tamoxifen	225-234	sulfotransferase family 1E member 1	Homo sapiens	289-296
33064293-7	2021	CONCLUSIONS: Taken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.	Diethylstilbestrol	240-258	sulfotransferase family 1E member 1	Homo sapiens	136-143
32897507-7	2020	Results suggest, tocopherol is more inductive to monoamine-SULT (MPST) and Dehydroepiandrosterone-SULT (DHEAST) compared to that of tocotrienol (inconsistent change in PPST, phenol sulfotransferase/MPST/EST, estrogen sulfotransferase).	Tocopherols	17-27	sulfotransferase family 1E member 1	Homo sapiens	208-233
32521045-8	2020	RESULTS: With PaCO2 -est1, the mean difference between the partial pressure of carbon dioxide, and the estimated carbon dioxide was 0.08 kPa (SE +- 0.003); with PaCO2 -est2 the difference was 0.036 kPa (SE +- 0.009).	Carbon Dioxide	79-93	sulfotransferase family 1E member 1	Homo sapiens	21-25
32521045-8	2020	RESULTS: With PaCO2 -est1, the mean difference between the partial pressure of carbon dioxide, and the estimated carbon dioxide was 0.08 kPa (SE +- 0.003); with PaCO2 -est2 the difference was 0.036 kPa (SE +- 0.009).	Carbon Dioxide	113-127	sulfotransferase family 1E member 1	Homo sapiens	21-25
32798464-0	2020	PXR Phosphorylated at Ser350 transduces a glucose signal to repress the estrogen sulfotransferase gene in human liver cells and fasting signal in mouse livers.	Glucose	42-49	sulfotransferase family 1E member 1	Homo sapiens	72-97
32798464-2	2020	Here, we have demonstrated how nuclear receptor PXR regulated the SULT1E1 gene in response to glucose in human hepatoma-derived cells and in response to fasting in mouse livers.	Glucose	94-101	sulfotransferase family 1E member 1	Homo sapiens	66-73
32633098-4	2020	Results from polyacrylamide gel electrophoresis and western blotting demonstrated that hSULT1E1 specifically binds to Ox-LDL and its major lipid component (lysophosphatidylcholine; LPC), and platelet-activating factor (PAF), which bears a marked resemblance to LPC in terms of structure and activity.	polyacrylamide	13-27	sulfotransferase family 1E member 1	Homo sapiens	87-95
32633098-4	2020	Results from polyacrylamide gel electrophoresis and western blotting demonstrated that hSULT1E1 specifically binds to Ox-LDL and its major lipid component (lysophosphatidylcholine; LPC), and platelet-activating factor (PAF), which bears a marked resemblance to LPC in terms of structure and activity.	Lysophosphatidylcholines	156-179	sulfotransferase family 1E member 1	Homo sapiens	87-95
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	fluorescein isothiocyanate	26-52	sulfotransferase family 1E member 1	Homo sapiens	98-106
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	fluorescein isothiocyanate	26-52	sulfotransferase family 1E member 1	Homo sapiens	147-155
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	Fluorescein-5-isothiocyanate	54-58	sulfotransferase family 1E member 1	Homo sapiens	98-106
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	Fluorescein-5-isothiocyanate	54-58	sulfotransferase family 1E member 1	Homo sapiens	147-155
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	decapeptide	68-79	sulfotransferase family 1E member 1	Homo sapiens	98-106
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	decapeptide	68-79	sulfotransferase family 1E member 1	Homo sapiens	147-155
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	Fluorescein-5-isothiocyanate	93-97	sulfotransferase family 1E member 1	Homo sapiens	98-106
32633098-5	2020	Moreover, an N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK; FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 specifically binds to Ox-LDL, LPC, and PAF.	Fluorescein-5-isothiocyanate	93-97	sulfotransferase family 1E member 1	Homo sapiens	147-155
32633098-7	2020	In addition, FITC-hSULT1E1-P10 could be used as an efficient fluorescent probe for the detection of Ox-LDL, LPC, and PAF, which could facilitate the mechanistic study, identification, diagnosis, prevention, and treatment of atherosclerosis.	Fluorescein-5-isothiocyanate	13-17	sulfotransferase family 1E member 1	Homo sapiens	18-26
32686824-2	2020	Human fetal, but not adult, livers express appreciable amounts of SULT1E1 protein, which is mimicked in human hepatoma-derived HepG2 cells cultured in high glucose (450 mg/dl) medium.	Glucose	156-163	sulfotransferase family 1E member 1	Homo sapiens	66-73
32830792-11	2020	The cytotoxicity of Dox to EST1-overexpressing K562/ADR cells was enhanced by olmutinib.	Doxorubicin	20-23	sulfotransferase family 1E member 1	Homo sapiens	27-31
32830792-11	2020	The cytotoxicity of Dox to EST1-overexpressing K562/ADR cells was enhanced by olmutinib.	olmutinib	78-87	sulfotransferase family 1E member 1	Homo sapiens	27-31
32903464-0	2020	Analysis of Drug Metabolizing Gene Panel in Osteosarcoma Patients Identifies Association Between Variants in SULT1E1, CYP2B6 and CYP4F8 and Methotrexate Levels and Toxicities.	Methotrexate	140-152	sulfotransferase family 1E member 1	Homo sapiens	109-116
32903464-8	2020	Genetic variant rs3736599 in the 5"-untranslated region of SULT1E1 was associated with lower 48 hour methotrexate plasma levels [coef -0.313 (95% CI -0.459 - -0.167); p = 2.60 x 10-5].	Methotrexate	101-113	sulfotransferase family 1E member 1	Homo sapiens	59-66
32903464-12	2020	This is the first study to identify genetic variants in SULT1E1, CYP2B6, and CYP4F8 to be associated with methotrexate pharmacokinetics and toxicities.	Methotrexate	106-118	sulfotransferase family 1E member 1	Homo sapiens	56-63
32640069-6	2020	Estrogen sulfotransferase and 17beta-hydroxysteroid dehydrogenase were identified as potentially subject to inhibition by the investigated urolithins.	urolithins	139-149	sulfotransferase family 1E member 1	Homo sapiens	0-25
32449069-5	2020	Our present review demonstrates that ROS dependent regulation of Nrf-2 is one of the most important determinants of E2 regulation by altering SULT1E1 expression.	ros	37-40	sulfotransferase family 1E member 1	Homo sapiens	142-149
32372097-19	2020	COCs expanded rapidly in the presence of testosterone during LH administration, and ovulation-related genes, namely, Areg, Ereg, Ptgs2, Sult1e1, Ptx3 and Tnfaip6, were strongly expressed in the COCs and GCs.	Testosterone	41-53	sulfotransferase family 1E member 1	Homo sapiens	136-143
32158360-1	2020	Background: Estrogen sulfotransferase catalyzes conjugation of sulfuryl-group to estradiol/estrone and regulates E2 availability/activity via estrogen-receptor or non-receptor mediated pathways.	Estradiol	81-90	sulfotransferase family 1E member 1	Homo sapiens	12-37
32158360-1	2020	Background: Estrogen sulfotransferase catalyzes conjugation of sulfuryl-group to estradiol/estrone and regulates E2 availability/activity via estrogen-receptor or non-receptor mediated pathways.	Estrone	91-98	sulfotransferase family 1E member 1	Homo sapiens	12-37
31896193-9	2020	The most differentially-expressed genes upon PFOA coincubation were ITGB8, KLF5, WNT11, SULT1E1, ALPPL2 and G0S2 (all p < 0.01).	perfluorooctanoic acid	45-49	sulfotransferase family 1E member 1	Homo sapiens	88-95
31884462-0	2020	Probing Estrogen Sulfotransferase-Mediated Inflammation with [11C]-PiB in the Living Human Brain.	diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo(lmn)(3,8)phenanthroline-2,7-diacetate	61-70	sulfotransferase family 1E member 1	Homo sapiens	8-33
31884462-1	2020	BACKGROUND: 2-(4"- [11C]Methylaminophenyl)-6-hydroxybenzothiazole ([11C]-PiB), purportedly a specific imaging agent for cerebral amyloid-beta plaques, is a specific, high affinity substrate for estrogen sulfotransferase (SULT1E1), an enzyme that regulates estrogen homeostasis.	pib	12-65	sulfotransferase family 1E member 1	Homo sapiens	194-219
31884462-1	2020	BACKGROUND: 2-(4"- [11C]Methylaminophenyl)-6-hydroxybenzothiazole ([11C]-PiB), purportedly a specific imaging agent for cerebral amyloid-beta plaques, is a specific, high affinity substrate for estrogen sulfotransferase (SULT1E1), an enzyme that regulates estrogen homeostasis.	pib	12-65	sulfotransferase family 1E member 1	Homo sapiens	221-228
31884462-1	2020	BACKGROUND: 2-(4"- [11C]Methylaminophenyl)-6-hydroxybenzothiazole ([11C]-PiB), purportedly a specific imaging agent for cerebral amyloid-beta plaques, is a specific, high affinity substrate for estrogen sulfotransferase (SULT1E1), an enzyme that regulates estrogen homeostasis.	diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo(lmn)(3,8)phenanthroline-2,7-diacetate	67-76	sulfotransferase family 1E member 1	Homo sapiens	194-219
31884462-1	2020	BACKGROUND: 2-(4"- [11C]Methylaminophenyl)-6-hydroxybenzothiazole ([11C]-PiB), purportedly a specific imaging agent for cerebral amyloid-beta plaques, is a specific, high affinity substrate for estrogen sulfotransferase (SULT1E1), an enzyme that regulates estrogen homeostasis.	diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo(lmn)(3,8)phenanthroline-2,7-diacetate	67-76	sulfotransferase family 1E member 1	Homo sapiens	221-228
31884462-1	2020	BACKGROUND: 2-(4"- [11C]Methylaminophenyl)-6-hydroxybenzothiazole ([11C]-PiB), purportedly a specific imaging agent for cerebral amyloid-beta plaques, is a specific, high affinity substrate for estrogen sulfotransferase (SULT1E1), an enzyme that regulates estrogen homeostasis.	Estrogens	194-202	sulfotransferase family 1E member 1	Homo sapiens	221-228
31884462-2	2020	OBJECTIVE: In this work, we use positron emission tomography (PET) imaging with [11C]-PiB to assess the functional activity of SULT1E1 in the brain of moyamoya disease patients.	diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo(lmn)(3,8)phenanthroline-2,7-diacetate	80-89	sulfotransferase family 1E member 1	Homo sapiens	127-134
31884462-10	2020	CONCLUSION: Strong [11C]-PiB PET signal associated with intracranial inflammation in the moyamoya syndrome cohort and a single RRMS patient appears consistent with functional imaging of SULT1E1 activity in the human brain.	diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo(lmn)(3,8)phenanthroline-2,7-diacetate	19-28	sulfotransferase family 1E member 1	Homo sapiens	186-193
31336576-4	2019	M1 formation from catalposide was catalyzed by sulfotransferases (SULTs) 1C4, SULT1A1*1, SULT1A1*2, and SULT1E1.	catalposide	18-29	sulfotransferase family 1E member 1	Homo sapiens	104-111
30975319-4	2019	In comparison to St-G, St-E and PACl used individually as well as St-G and St-E dosed after PACl, the combination of the starch-based coagulants fed before PACl showed higher turbidity removal efficiency, which featured not only less optimal doses of both inorganic and organic coagulants but also lower residual turbidity.	Starch	121-127	sulfotransferase family 1E member 1	Homo sapiens	75-79
31115536-8	2019	Sulfotransferase family 1E member 1, cytochrome P450 family 3 subfamily A member 2, carbonic anhydrase 3, leukotriene C4 synthase and ADAM metallopeptidase domain 8 were the 5 candidate genes identified to be differentially expressed and involved in the metabolism of estrogens and bile acids and the regulation of inflammation and oxidative stress.	Bile Acids and Salts	282-292	sulfotransferase family 1E member 1	Homo sapiens	0-35
30802529-7	2019	GL cells treated with 10 nM DHT showed a 4-fold (p = 0.03) increase in expression of SULT1E1 and a 5-fold reduction in SRD5A1 (p = 0.03).	Dihydrotestosterone	28-31	sulfotransferase family 1E member 1	Homo sapiens	85-92
30822161-5	2019	SULT1E1 catalyzes the transfer of a sulfate group from 3"-phosphoadenosine-5"-phosphosulfate (PAPS) to any available hydroxyl group in estrogenic molecules.	Sulfates	36-43	sulfotransferase family 1E member 1	Homo sapiens	0-7
30822161-5	2019	SULT1E1 catalyzes the transfer of a sulfate group from 3"-phosphoadenosine-5"-phosphosulfate (PAPS) to any available hydroxyl group in estrogenic molecules.	Phosphoadenosine Phosphosulfate	55-92	sulfotransferase family 1E member 1	Homo sapiens	0-7
30822161-5	2019	SULT1E1 catalyzes the transfer of a sulfate group from 3"-phosphoadenosine-5"-phosphosulfate (PAPS) to any available hydroxyl group in estrogenic molecules.	Phosphoadenosine Phosphosulfate	94-98	sulfotransferase family 1E member 1	Homo sapiens	0-7
30822161-5	2019	SULT1E1 catalyzes the transfer of a sulfate group from 3"-phosphoadenosine-5"-phosphosulfate (PAPS) to any available hydroxyl group in estrogenic molecules.	Hydroxyl Radical	117-125	sulfotransferase family 1E member 1	Homo sapiens	0-7
30315444-9	2018	But the increase in the serum E2 level as noted in the ELISA data with impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression (immuno-blot data) were noticed with interfered hepatic free-thiols only in ENU and xenograft-E2 group compared to arsenic group.	Sulfhydryl Compounds	213-219	sulfotransferase family 1E member 1	Homo sapiens	97-122
30315444-9	2018	But the increase in the serum E2 level as noted in the ELISA data with impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression (immuno-blot data) were noticed with interfered hepatic free-thiols only in ENU and xenograft-E2 group compared to arsenic group.	Sulfhydryl Compounds	213-219	sulfotransferase family 1E member 1	Homo sapiens	124-131
30315444-9	2018	But the increase in the serum E2 level as noted in the ELISA data with impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression (immuno-blot data) were noticed with interfered hepatic free-thiols only in ENU and xenograft-E2 group compared to arsenic group.	Arsenic	267-274	sulfotransferase family 1E member 1	Homo sapiens	97-122
30315444-9	2018	But the increase in the serum E2 level as noted in the ELISA data with impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression (immuno-blot data) were noticed with interfered hepatic free-thiols only in ENU and xenograft-E2 group compared to arsenic group.	Arsenic	267-274	sulfotransferase family 1E member 1	Homo sapiens	124-131
30255609-12	2018	There were weak correlations between the iron turnover and 2D STE parameters.	Iron	41-45	sulfotransferase family 1E member 1	Homo sapiens	62-65
29929982-0	2018	Cholestasis-induced bile acid elevates estrogen level via farnesoid X receptor-mediated suppression of the estrogen sulfotransferase SULT1E1.	Bile Acids and Salts	20-29	sulfotransferase family 1E member 1	Homo sapiens	133-140
29436390-0	2018	Identification of Galeterone and Abiraterone as Inhibitors of Dehydroepiandrosterone Sulfonation Catalyzed by Human Hepatic Cytosol, SULT2A1, SULT2B1b, and SULT1E1.	3-hydroxy-17-(1H-benzimidazole-1-yl)androsta-5,16-diene	18-28	sulfotransferase family 1E member 1	Homo sapiens	156-163
29436390-0	2018	Identification of Galeterone and Abiraterone as Inhibitors of Dehydroepiandrosterone Sulfonation Catalyzed by Human Hepatic Cytosol, SULT2A1, SULT2B1b, and SULT1E1.	abiraterone	33-44	sulfotransferase family 1E member 1	Homo sapiens	156-163
29436390-0	2018	Identification of Galeterone and Abiraterone as Inhibitors of Dehydroepiandrosterone Sulfonation Catalyzed by Human Hepatic Cytosol, SULT2A1, SULT2B1b, and SULT1E1.	Dehydroepiandrosterone	62-84	sulfotransferase family 1E member 1	Homo sapiens	156-163
29436390-8	2018	In conclusion, galeterone and abiraterone are novel inhibitors of DHEA sulfonation, as determined in enzymatic incubations containing human tissue cytosol (liver or intestinal) or human recombinant SULT enzyme (SULT2A1, SULT2B1b, or SULT1E1).	3-hydroxy-17-(1H-benzimidazole-1-yl)androsta-5,16-diene	15-25	sulfotransferase family 1E member 1	Homo sapiens	233-240
29436390-8	2018	In conclusion, galeterone and abiraterone are novel inhibitors of DHEA sulfonation, as determined in enzymatic incubations containing human tissue cytosol (liver or intestinal) or human recombinant SULT enzyme (SULT2A1, SULT2B1b, or SULT1E1).	abiraterone	30-41	sulfotransferase family 1E member 1	Homo sapiens	233-240
29161598-10	2018	However, selenium supplementation led to elevations of selenium, Dio1 and TTR, and reductions of Ugt1a1, Sult1e1, CYP2b1, and TRHr.	Selenium	9-17	sulfotransferase family 1E member 1	Homo sapiens	105-112
29408762-0	2018	Hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 and SULT2A1.	Polychlorinated Biphenyls	69-94	sulfotransferase family 1E member 1	Homo sapiens	135-142
29408762-4	2018	The human estrogen sulfotransferase (SULT1E1) and alcohol/hydroxysteroid sulfotransferase (SULT2A1) catalyze the formation of steroid sulfates that are inactive at steroid hormone receptors.	steroid sulfates	126-142	sulfotransferase family 1E member 1	Homo sapiens	10-35
29408762-4	2018	The human estrogen sulfotransferase (SULT1E1) and alcohol/hydroxysteroid sulfotransferase (SULT2A1) catalyze the formation of steroid sulfates that are inactive at steroid hormone receptors.	steroid sulfates	126-142	sulfotransferase family 1E member 1	Homo sapiens	37-44
29408762-6	2018	Several congeners of lower chlorinated OH-PCBs relevant to airborne PCB exposures were potent inhibitors of SULT1E1 and SULT2A1 and thus have the potential to disrupt regulation of intracellular concentrations of the receptor-active steroid substrates for these enzymes.	oh-pcbs	39-46	sulfotransferase family 1E member 1	Homo sapiens	108-115
29408762-6	2018	Several congeners of lower chlorinated OH-PCBs relevant to airborne PCB exposures were potent inhibitors of SULT1E1 and SULT2A1 and thus have the potential to disrupt regulation of intracellular concentrations of the receptor-active steroid substrates for these enzymes.	Steroids	233-240	sulfotransferase family 1E member 1	Homo sapiens	108-115
29077781-5	2018	Results: A four-gene signature combining the expression levels of HLF, CXCL13, SULT1E1, and GBP1 was developed in baseline samples to predict the extent of lymphocytic infiltration after NACT.	nact	187-191	sulfotransferase family 1E member 1	Homo sapiens	79-86
30497730-9	2018	In patients classified as having inferior MI, an STE in lead III greater than STE in lead II favored RCA over Cx as the culprit artery with a sensitivity, specificity, positive and negative predictive value of 97%, 46.6%, 80% and 87.5%, respectively (P < 0.001; phi = 0.544).	RCA II	101-104	sulfotransferase family 1E member 1	Homo sapiens	49-52
30497730-9	2018	In patients classified as having inferior MI, an STE in lead III greater than STE in lead II favored RCA over Cx as the culprit artery with a sensitivity, specificity, positive and negative predictive value of 97%, 46.6%, 80% and 87.5%, respectively (P < 0.001; phi = 0.544).	RCA II	101-104	sulfotransferase family 1E member 1	Homo sapiens	78-81
28912067-1	2017	Sulfotransferase 1E1 (SULT1E1, also known as estrogen sulfotransferase) plays an important role in metabolism and detoxification of many endogenous and exogenous compounds (e.g., estrogens and flavonoids).	Flavonoids	193-203	sulfotransferase family 1E member 1	Homo sapiens	0-20
28912067-1	2017	Sulfotransferase 1E1 (SULT1E1, also known as estrogen sulfotransferase) plays an important role in metabolism and detoxification of many endogenous and exogenous compounds (e.g., estrogens and flavonoids).	Flavonoids	193-203	sulfotransferase family 1E member 1	Homo sapiens	22-29
28912067-1	2017	Sulfotransferase 1E1 (SULT1E1, also known as estrogen sulfotransferase) plays an important role in metabolism and detoxification of many endogenous and exogenous compounds (e.g., estrogens and flavonoids).	Flavonoids	193-203	sulfotransferase family 1E member 1	Homo sapiens	45-70
28866654-5	2017	We observed upregulation of Cyp19a1, Hsd17b1, Cyp1a1, Sult1e1 in the DEN-treated livers compared to the control-treated livers using real time PCR.	Diethylnitrosamine	69-72	sulfotransferase family 1E member 1	Homo sapiens	54-61
28866654-8	2017	In addition, the substantial increase in the Sult1e1 enzyme levels could lead to sulfate conjugation of hydroxyestrogen.	Sulfates	81-88	sulfotransferase family 1E member 1	Homo sapiens	45-52
28552400-5	2017	Celecoxib was shown to inhibit recombinant SULT1A1-catalyzed sulfonation of 10nM estrone and 4muM p-nitrophenol with IC50 values of 2.6 and 2.1muM, respectively, but did not inhibit SULT1E1-catalyzed estrone sulfonation.	Celecoxib	0-9	sulfotransferase family 1E member 1	Homo sapiens	182-189
28286122-5	2017	Two regioisomers of sulfated genistein were produced by E. coli cells expressing human SULT1A3, SULT1C4, or SULT1E1, and purified using Diaion HP20 resin, followed by high pressure liquid chromatography (HPLC).	Genistein	29-38	sulfotransferase family 1E member 1	Homo sapiens	108-115
28441724-7	2017	Metabolism of picroside II (M4) into M4 sulfate (M8) was catalyzed by SULT1A1, SULT1E1, SULT1A2, SULT1A3, and SULT1C4.	picroside II	14-26	sulfotransferase family 1E member 1	Homo sapiens	79-86
28441724-7	2017	Metabolism of picroside II (M4) into M4 sulfate (M8) was catalyzed by SULT1A1, SULT1E1, SULT1A2, SULT1A3, and SULT1C4.	m4 sulfate	37-47	sulfotransferase family 1E member 1	Homo sapiens	79-86
27854074-5	2017	Resveratrol and all its derivatives reduced also SULT1E1 mRNA transcript level.	Resveratrol	0-11	sulfotransferase family 1E member 1	Homo sapiens	49-56
27150425-8	2016	RESULTS: Six single nucleotide polymorphisms in the estrogen sulfotransferase gene SULT1E1 were associated with time to treatment failure on abiraterone acetate therapy after false discovery rate (q value) correction for multiple testing while controlling for Gleason score, age, level of alkaline phosphatase and prostate specific antigen at treatment initiation (q &lt;0.05).	Abiraterone Acetate	141-160	sulfotransferase family 1E member 1	Homo sapiens	52-77
27150425-8	2016	RESULTS: Six single nucleotide polymorphisms in the estrogen sulfotransferase gene SULT1E1 were associated with time to treatment failure on abiraterone acetate therapy after false discovery rate (q value) correction for multiple testing while controlling for Gleason score, age, level of alkaline phosphatase and prostate specific antigen at treatment initiation (q &lt;0.05).	Abiraterone Acetate	141-160	sulfotransferase family 1E member 1	Homo sapiens	83-90
27150425-9	2016	CONCLUSIONS: Single nucleotide polymorphisms in SULT1E1 were significantly associated with time to treatment failure in men on abiraterone acetate therapy.	Abiraterone Acetate	127-146	sulfotransferase family 1E member 1	Homo sapiens	48-55
27491884-7	2016	However, BPA-induced toxicity was alleviated in the presence of ADH (IC50, 337+-17.9muM), ALDH2 (335+-13.9muM), and SULT1E1 (318+-17.7muM) (p&lt;0.05).	bisphenol A	9-12	sulfotransferase family 1E member 1	Homo sapiens	116-123
27751297-2	2016	The classical electrocardiographic pattern of LMCA disease includes ST elevation (STE) in lead aVR in the presence of extensive ST depression (most prominent in leads I, II, and V4-6) with the STE in aVR&gt;=V1.	levomefolate calcium	46-50	sulfotransferase family 1E member 1	Homo sapiens	82-85
27751297-2	2016	The classical electrocardiographic pattern of LMCA disease includes ST elevation (STE) in lead aVR in the presence of extensive ST depression (most prominent in leads I, II, and V4-6) with the STE in aVR&gt;=V1.	levomefolate calcium	46-50	sulfotransferase family 1E member 1	Homo sapiens	193-196
26829336-12	2016	Findings for quercetin with regard to UGT2B7 and SULT2A1 and for kaempferol with regard to SULT1E1 and SULT2A1 suggested a mechanism based inhibition.	kaempferol	65-75	sulfotransferase family 1E member 1	Homo sapiens	91-98
27467388-8	2016	CONCLUSIONS: Among patients referred for ExECG for suspected CAD, exercise-induced STE in lead aVR was associated with a higher risk DTS, an increased likelihood of a positive ExECG, and referral for subsequent coronary angiography.	dibenzyl trisulfide	133-136	sulfotransferase family 1E member 1	Homo sapiens	83-86
27118027-0	2016	Pervanadate induces Mammalian Ste20 Kinase 3 (MST3) tyrosine phosphorylation but not activation.	pervanadate	0-11	sulfotransferase family 1E member 1	Homo sapiens	30-44
27118027-0	2016	Pervanadate induces Mammalian Ste20 Kinase 3 (MST3) tyrosine phosphorylation but not activation.	Tyrosine	52-60	sulfotransferase family 1E member 1	Homo sapiens	30-44
27133297-0	2016	Dexamethasone suppresses the growth of human non-small cell lung cancer via inducing estrogen sulfotransferase and inactivating estrogen.	Dexamethasone	0-13	sulfotransferase family 1E member 1	Homo sapiens	85-110
26758853-5	2016	Human sulfotransferases (SULTs) SULT1A1, SULT1A2, SULT1E1, and SULT2A1 are involved in the formation of lorcaserin N-sulfamate.	lorcaserin n-sulfamate	104-126	sulfotransferase family 1E member 1	Homo sapiens	50-57
26758853-7	2016	The order of intrinsic clearance for lorcaserin N-sulfamate is SULT1A1 &gt; SULT2A1 &gt; SULT1A2 &gt; SULT1E1.	lorcaserin n-sulfamate	37-59	sulfotransferase family 1E member 1	Homo sapiens	102-109
26891815-3	2016	STE was also found to induce significant amount ROS generation in SCC-25 cells.	ros	48-51	sulfotransferase family 1E member 1	Homo sapiens	0-3
26891815-6	2016	In all cases morin provided cytoprotection to STE challenged SCC-25 cells by augmenting STE induced ROS-dependent cytotoxic autophagy.	ros	100-103	sulfotransferase family 1E member 1	Homo sapiens	88-91
26723541-0	2016	Effects of steroid hormone on estrogen sulfotransferase and on steroid sulfatase expression in endometriosis tissue and stromal cells.	Steroids	11-26	sulfotransferase family 1E member 1	Homo sapiens	30-55
26723541-6	2016	The actions of female steroid hormones on SULT1E1 and STS expression were evidenced in endometriosis, revealed by increased expression levels in the luteal phase of the cycle.	Steroids	22-29	sulfotransferase family 1E member 1	Homo sapiens	42-49
26544119-4	2016	Kinetic parameters of SULT1A1, SULT1A3, SULT1C4, and SULT1E1 that showed stronger 6-gingerol-sulfating activity were determined.	gingerol	82-92	sulfotransferase family 1E member 1	Homo sapiens	53-60
27449410-4	2016	RESULTS: A systematic analysis revealed that six of the thirteen known human SULTs, SULT1A1 SULT1A2, SULTA3, SULT1B1, SULT1C4, and SULT1E1 showed considerable clioquinol/ iodoquinol-sulfating activity.	Clioquinol	159-169	sulfotransferase family 1E member 1	Homo sapiens	131-138
27449410-4	2016	RESULTS: A systematic analysis revealed that six of the thirteen known human SULTs, SULT1A1 SULT1A2, SULTA3, SULT1B1, SULT1C4, and SULT1E1 showed considerable clioquinol/ iodoquinol-sulfating activity.	Iodoquinol	171-181	sulfotransferase family 1E member 1	Homo sapiens	131-138
26666354-0	2015	Triclosan causes spontaneous abortion accompanied by decline of estrogen sulfotransferase activity in humans and mice.	Triclosan	0-9	sulfotransferase family 1E member 1	Homo sapiens	64-89
26458420-3	2015	Estrogen sulfatase (STS) converts inactive estrogen sulfates into active estrogens, whereas estrogen sulfotransferase (EST) sulfonates estrogens to estrogen sulfates.	Alkanesulfonates	124-134	sulfotransferase family 1E member 1	Homo sapiens	92-117
26458420-3	2015	Estrogen sulfatase (STS) converts inactive estrogen sulfates into active estrogens, whereas estrogen sulfotransferase (EST) sulfonates estrogens to estrogen sulfates.	estrogen sulfates	148-165	sulfotransferase family 1E member 1	Homo sapiens	92-117
25937633-0	2015	Intratumoral estrogen sulfotransferase induction contributes to the anti-breast cancer effects of the dithiocarbamate derivative TM208.	Dithiocarbamate	102-117	sulfotransferase family 1E member 1	Homo sapiens	13-38
25937633-0	2015	Intratumoral estrogen sulfotransferase induction contributes to the anti-breast cancer effects of the dithiocarbamate derivative TM208.	4-methylpiperazine-1-carbodithioc acid 3-cyano-3,3-diphenylpropyl ester hydrochloride	129-134	sulfotransferase family 1E member 1	Homo sapiens	13-38
26036805-7	2015	The agonistic effect of progesterone on SULT1E1 mRNA levels was concentration-dependently antagonized by RU486, UPA and ZK137316 as well as, with lower potency, apigenin.	Mifepristone	105-110	sulfotransferase family 1E member 1	Homo sapiens	40-47
25819444-0	2015	The effects of endoxifen and other major metabolites of tamoxifen on the sulfation of estradiol catalyzed by human cytosolic sulfotransferases hSULT1E1 and hSULT1A1*1.	Tamoxifen	56-65	sulfotransferase family 1E member 1	Homo sapiens	143-151
25819444-0	2015	The effects of endoxifen and other major metabolites of tamoxifen on the sulfation of estradiol catalyzed by human cytosolic sulfotransferases hSULT1E1 and hSULT1A1*1.	Estradiol	86-95	sulfotransferase family 1E member 1	Homo sapiens	143-151
25819444-3	2015	We hypothesized that endoxifen and perhaps other major metabolites of tamoxifen may affect the ability of human estrogen sulfotransferase 1E1 (hSULT1E1) and human phenol sulfotransferase 1A1 isoform 1 (hSULT1A1*1) to catalyze the sulfation of estradiol, an important mechanism in termination of estrogen signaling through loss of activity at estrogen receptors.	4-hydroxy-N-desmethyltamoxifen	21-30	sulfotransferase family 1E member 1	Homo sapiens	143-151
25819444-3	2015	We hypothesized that endoxifen and perhaps other major metabolites of tamoxifen may affect the ability of human estrogen sulfotransferase 1E1 (hSULT1E1) and human phenol sulfotransferase 1A1 isoform 1 (hSULT1A1*1) to catalyze the sulfation of estradiol, an important mechanism in termination of estrogen signaling through loss of activity at estrogen receptors.	Tamoxifen	70-79	sulfotransferase family 1E member 1	Homo sapiens	143-151
25819444-3	2015	We hypothesized that endoxifen and perhaps other major metabolites of tamoxifen may affect the ability of human estrogen sulfotransferase 1E1 (hSULT1E1) and human phenol sulfotransferase 1A1 isoform 1 (hSULT1A1*1) to catalyze the sulfation of estradiol, an important mechanism in termination of estrogen signaling through loss of activity at estrogen receptors.	Estradiol	243-252	sulfotransferase family 1E member 1	Homo sapiens	143-151
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	4-hydroxy-N-desmethyltamoxifen	27-36	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	N-desmethyltamoxifen	38-58	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	hydroxytamoxifen	71-89	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	4-ohtam	91-98	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	tamoxifen N-oxide	105-122	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-4	2015	Our results indicated that endoxifen, N-desmethyltamoxifen (N-desTAM), 4-hydroxytamoxifen (4-OHTAM), and tamoxifen-N-oxide were weak inhibitors of hSULT1E1 with Ki values ranging from 10 muM to 38 muM (i.e., over 1000 times higher than the 8.1 nM Km value for estradiol as substrate for the enzyme).	Estradiol	260-269	sulfotransferase family 1E member 1	Homo sapiens	147-155
25819444-5	2015	In contrast to the results with hSULT1E1, endoxifen and 4-OHTAM were significant inhibitors of the sulfation of 2.0 microM estradiol catalyzed by hSULT1A1*1, with IC50 values (9.9 muM and 1.6 muM, respectively) that were similar to the Km value (1.5 muM) for estradiol as substrate for this enzyme.	Estradiol	123-132	sulfotransferase family 1E member 1	Homo sapiens	32-40
25819444-6	2015	Additional investigation of the interaction of these metabolites with the two sulfotransferases revealed that endoxifen, 4-OHTAM, and N-desTAM were substrates for hSULT1E1 and hSULT1A1*1, although the relative catalytic efficiencies varied with both the substrate and the enzyme.	4-hydroxy-N-desmethyltamoxifen	110-119	sulfotransferase family 1E member 1	Homo sapiens	163-171
25819444-6	2015	Additional investigation of the interaction of these metabolites with the two sulfotransferases revealed that endoxifen, 4-OHTAM, and N-desTAM were substrates for hSULT1E1 and hSULT1A1*1, although the relative catalytic efficiencies varied with both the substrate and the enzyme.	4-ohtam	121-128	sulfotransferase family 1E member 1	Homo sapiens	163-171
25819444-6	2015	Additional investigation of the interaction of these metabolites with the two sulfotransferases revealed that endoxifen, 4-OHTAM, and N-desTAM were substrates for hSULT1E1 and hSULT1A1*1, although the relative catalytic efficiencies varied with both the substrate and the enzyme.	N-desmethyltamoxifen	134-142	sulfotransferase family 1E member 1	Homo sapiens	163-171
26419090-12	2015	Inhibition was reversible and competitive for most enzymes; mechanism-based inhibition was evident for UGT2B7 and SULT2A1 with regard to quercetin and for SULT1E1 with regard to kaempferol.	kaempferol	178-188	sulfotransferase family 1E member 1	Homo sapiens	155-162