PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9463486-7	1998	Enzymatically active hST1B2 was expressed in the bacterial expression vector pKK233-2 for kinetic characterization and in the bacterial expression vector pQE-31, which generates a histidine-tagged fusion protein for the generation of antibodies.	Histidine	180-189	sulfotransferase family 1B member 1	Homo sapiens	21-27
10375162-3	1999	ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively.	4-nitrophenol	128-141	sulfotransferase family 1B member 1	Homo sapiens	0-5
10375162-3	1999	ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively.	Dopamine	159-167	sulfotransferase family 1B member 1	Homo sapiens	0-5
10375162-3	1999	ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively.	Estradiol	185-199	sulfotransferase family 1B member 1	Homo sapiens	0-5
10375162-3	1999	ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively.	Dehydroepiandrosterone	220-242	sulfotransferase family 1B member 1	Homo sapiens	0-5
10375162-7	1999	In addition, studies of thermal stability and 2,6-dichloro-4-nitrophenol (DCNP) inhibition showed that ST1B2 was thermostable and more DCNP resistant than other forms of ST. Affinities for a co-factor, phosphoadenosine 5"-phosphosulfate, also differed 9-fold among 5 different forms of ST.	2,6-dichloro-4-nitrophenol	46-72	sulfotransferase family 1B member 1	Homo sapiens	103-108
10375162-7	1999	In addition, studies of thermal stability and 2,6-dichloro-4-nitrophenol (DCNP) inhibition showed that ST1B2 was thermostable and more DCNP resistant than other forms of ST. Affinities for a co-factor, phosphoadenosine 5"-phosphosulfate, also differed 9-fold among 5 different forms of ST.	2,6-dichloro-4-nitrophenol	74-78	sulfotransferase family 1B member 1	Homo sapiens	103-108
10375162-7	1999	In addition, studies of thermal stability and 2,6-dichloro-4-nitrophenol (DCNP) inhibition showed that ST1B2 was thermostable and more DCNP resistant than other forms of ST. Affinities for a co-factor, phosphoadenosine 5"-phosphosulfate, also differed 9-fold among 5 different forms of ST.	2,6-dichloro-4-nitrophenol	135-139	sulfotransferase family 1B member 1	Homo sapiens	103-108
10375162-7	1999	In addition, studies of thermal stability and 2,6-dichloro-4-nitrophenol (DCNP) inhibition showed that ST1B2 was thermostable and more DCNP resistant than other forms of ST. Affinities for a co-factor, phosphoadenosine 5"-phosphosulfate, also differed 9-fold among 5 different forms of ST.	phosphoadenosine 5"-phosphosulfate	202-236	sulfotransferase family 1B member 1	Homo sapiens	103-108
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	aryl	81-85	sulfotransferase family 1B member 1	Homo sapiens	233-238
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	aryl	81-85	sulfotransferase family 1B member 1	Homo sapiens	251-256
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	Phenol	86-92	sulfotransferase family 1B member 1	Homo sapiens	233-238
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	Phenol	86-92	sulfotransferase family 1B member 1	Homo sapiens	251-256
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	Alcohols	105-112	sulfotransferase family 1B member 1	Homo sapiens	233-238
10220276-3	1999	The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively.	Alcohols	105-112	sulfotransferase family 1B member 1	Homo sapiens	251-256
11906176-6	2002	With the exception of SULT1B1, SULT1C1, and SULT4A1, all of the human SULTs studied catalyzed the sulfate conjugation of CEs.	Estrogens, Catechol	121-124	sulfotransferase family 1B member 1	Homo sapiens	22-29
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	Phenols	32-39	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	1-naphthol	48-58	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	4-nitrophenol	63-76	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	3,3'-diiodothyronine	109-129	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	Triiodothyronine	131-147	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	Triiodothyronine	157-173	sulfotransferase family 1B member 1	Homo sapiens	10-16
9463486-8	1998	Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3"-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.	Thyroxine	179-188	sulfotransferase family 1B member 1	Homo sapiens	10-16
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	monobutyl phthalate	0-19	sulfotransferase family 1B member 1	Homo sapiens	120-127
9443824-6	1997	ST1B1 and ST1B2 showed higher affinities for formation of T3 sulfate (apparent Km 40.2 and 63.5 microM, respectively) than did thermostable phenol sulfotransferase ST1A3 (apparent Km 413 microM) or thermolabile phenol sulfotransferase ST1A5 (apparent Km 180 microM).	t3 sulfate	58-68	sulfotransferase family 1B member 1	Homo sapiens	0-5
9443824-6	1997	ST1B1 and ST1B2 showed higher affinities for formation of T3 sulfate (apparent Km 40.2 and 63.5 microM, respectively) than did thermostable phenol sulfotransferase ST1A3 (apparent Km 413 microM) or thermolabile phenol sulfotransferase ST1A5 (apparent Km 180 microM).	t3 sulfate	58-68	sulfotransferase family 1B member 1	Homo sapiens	10-15
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 1B member 1	Homo sapiens	109-116
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	Defensamide	27-30	sulfotransferase family 1B member 1	Homo sapiens	120-127
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	mono-n-octyl phthalate	32-35	sulfotransferase family 1B member 1	Homo sapiens	120-127
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	Monocyclohexyl phthalate	37-62	sulfotransferase family 1B member 1	Homo sapiens	120-127
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	Monocyclohexyl phthalate	64-68	sulfotransferase family 1B member 1	Homo sapiens	120-127
35528018-7	2022	Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1.	mono-(2-ethylhexyl)phthalate	75-79	sulfotransferase family 1B member 1	Homo sapiens	120-127
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 1B member 1	Homo sapiens	118-125
35528018-11	2022	In silico docking method was utilized to understand the inhibition mechanism of SULT1B1 by phthalate monoesters.	phthalic acid	91-100	sulfotransferase family 1B member 1	Homo sapiens	80-87
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 1B member 1	Homo sapiens	122-129
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 1B member 1	Homo sapiens	133-140
35069453-5	2021	SULT1A1 and SULT1B1 were demonstrated to be the most vulnerable SULT isoforms towards BPs" inhibition.	bps	86-89	sulfotransferase family 1B member 1	Homo sapiens	12-19
28084139-2	2018	Human cytosolic sulfotransferase 1B1 (SULT1B1) sulfates small phenolic compounds and bioactivates polycyclic aromatic hydrocarbons.	Sulfates	47-55	sulfotransferase family 1B member 1	Homo sapiens	38-45
28084139-2	2018	Human cytosolic sulfotransferase 1B1 (SULT1B1) sulfates small phenolic compounds and bioactivates polycyclic aromatic hydrocarbons.	Polycyclic Aromatic Hydrocarbons	98-130	sulfotransferase family 1B member 1	Homo sapiens	38-45
28084139-5	2018	While cloning SULT1B1 from human endometrial specimens, an allelic variant resulting in valine instead of leucine at the 145th amino acid position (L145V) was detected.	Valine	88-94	sulfotransferase family 1B member 1	Homo sapiens	14-21
28084139-5	2018	While cloning SULT1B1 from human endometrial specimens, an allelic variant resulting in valine instead of leucine at the 145th amino acid position (L145V) was detected.	Leucine	106-113	sulfotransferase family 1B member 1	Homo sapiens	14-21
28214288-3	2017	The product of the fraction of an oral YH4808 dose entering the gut wall and the fraction of YH4808 passing on to the portal circulation was larger in subjects carrying the variants of the CHST3, SLC15A1, and SULT1B1 genes.	YH4808	39-45	sulfotransferase family 1B member 1	Homo sapiens	209-216
28214288-3	2017	The product of the fraction of an oral YH4808 dose entering the gut wall and the fraction of YH4808 passing on to the portal circulation was larger in subjects carrying the variants of the CHST3, SLC15A1, and SULT1B1 genes.	YH4808	93-99	sulfotransferase family 1B member 1	Homo sapiens	209-216
26663444-2	2016	A systematic analysis revealed that of the 13 known human SULTs, SULT1A1 SULT1A2, SULTA3, and SULT1B1 are capable of mediating the sulfation of benzyl alcohol.	Benzyl Alcohol	144-158	sulfotransferase family 1B member 1	Homo sapiens	94-101
23894158-3	2013	1-OH-MC was efficiently activated by human (h) SULT1B1 (2400 revertants/nmol), weakly activated by hSULT1C3 and hSULT2A1 (2-9 revertants/nmol), but not activated by the other hSULTs studied (1A2, 1A3, 1C2 and 1E1).	1-oh-mc	0-7	sulfotransferase family 1B member 1	Homo sapiens	47-54
23894158-8	2013	Docking analyses indicated that 1- and 2-OH-MC might bind to the active site of hSULT1A1 and hSULT1B1, but only for (S)-2-OH-MC/hSULT1A1 and (R)-1-OH-MC/hSULT1B1 with an orientation suitable for catalysis.	1- and 2-oh-mc	32-46	sulfotransferase family 1B member 1	Homo sapiens	93-101
25676631-7	2015	SULT1B1 is only responsible for sulfonation of curcumin.	Curcumin	47-55	sulfotransferase family 1B member 1	Homo sapiens	0-7
24743514-7	2014	In the presence of human NAD(P)H: quinone oxidoreductase, the ability of aristolochic acid I to bind DNA covalently was increased significantly by addition of PAPS and SULT1B1.	aristolochic acid I	73-92	sulfotransferase family 1B member 1	Homo sapiens	168-175
24743514-8	2014	We conclude from these studies that AL-NOHs, formed following partial nitroreduction of aristolochic acids, serve as substrates for SULT1B1, producing N-sulfated esters, which, in turn, are converted to highly active species that react with DNA and, potentially, cellular proteins, resulting in the genotoxicity and nephrotoxicity associated with ingestion of aristolochic acids by humans.	al-nohs	36-43	sulfotransferase family 1B member 1	Homo sapiens	132-139
24743514-8	2014	We conclude from these studies that AL-NOHs, formed following partial nitroreduction of aristolochic acids, serve as substrates for SULT1B1, producing N-sulfated esters, which, in turn, are converted to highly active species that react with DNA and, potentially, cellular proteins, resulting in the genotoxicity and nephrotoxicity associated with ingestion of aristolochic acids by humans.	Aristolochic Acids	88-106	sulfotransferase family 1B member 1	Homo sapiens	132-139
24743514-8	2014	We conclude from these studies that AL-NOHs, formed following partial nitroreduction of aristolochic acids, serve as substrates for SULT1B1, producing N-sulfated esters, which, in turn, are converted to highly active species that react with DNA and, potentially, cellular proteins, resulting in the genotoxicity and nephrotoxicity associated with ingestion of aristolochic acids by humans.	n-sulfated esters	151-168	sulfotransferase family 1B member 1	Homo sapiens	132-139
24743514-8	2014	We conclude from these studies that AL-NOHs, formed following partial nitroreduction of aristolochic acids, serve as substrates for SULT1B1, producing N-sulfated esters, which, in turn, are converted to highly active species that react with DNA and, potentially, cellular proteins, resulting in the genotoxicity and nephrotoxicity associated with ingestion of aristolochic acids by humans.	Aristolochic Acids	360-378	sulfotransferase family 1B member 1	Homo sapiens	132-139
23894158-8	2013	Docking analyses indicated that 1- and 2-OH-MC might bind to the active site of hSULT1A1 and hSULT1B1, but only for (S)-2-OH-MC/hSULT1A1 and (R)-1-OH-MC/hSULT1B1 with an orientation suitable for catalysis.	1- and 2-oh-mc	32-46	sulfotransferase family 1B member 1	Homo sapiens	153-161
16413005-7	2006	Some OH-PCBs with various inhibitory potencies with human liver cytosol were selected for study with recombinant human SULT1A1 and SULT1B1.	oh-pcbs	5-12	sulfotransferase family 1B member 1	Homo sapiens	131-138
23894158-11	2013	Inhibition of the SULT1B1 enzymes was moderate, strongest for 1-OH-MC/hSULT1B1.	1-oh-mc	62-69	sulfotransferase family 1B member 1	Homo sapiens	18-25
20056724-7	2010	Based on expression levels SULT1A3 and SULT1B1 also will probably play a role in the sulfo-conjugation of hesperetin in vivo.	Parathion	85-90	sulfotransferase family 1B member 1	Homo sapiens	39-46
19548878-9	2009	The KYNA derivatives 5,7-dichlorokynurenic acid and L689,560 exhibited preferential inhibitory effects on hSULT1A1 and hSULT1B1 respectively.	5,7-dichlorokynurenic acid	21-47	sulfotransferase family 1B member 1	Homo sapiens	119-127
19548878-9	2009	The KYNA derivatives 5,7-dichlorokynurenic acid and L689,560 exhibited preferential inhibitory effects on hSULT1A1 and hSULT1B1 respectively.	4-Chloro-4'-methoxybutyrophenone	52-56	sulfotransferase family 1B member 1	Homo sapiens	119-127
19548878-10	2009	Interestingly, gavestinel, another KYNA derivative, was found to be an extremely potent inhibitor of hSULT1B1.	3-(2-((phenylamino)carbonyl)ethenyl)-4,6-dichloroindole-2-carboxylic acid	15-25	sulfotransferase family 1B member 1	Homo sapiens	101-109
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 1B member 1	Homo sapiens	88-95
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 1B member 1	Homo sapiens	273-281
16804942-0	2006	Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3"- 5"-diphosphate (PAP).	adenosine 3'-phosphate-5'-phosphate	102-130	sulfotransferase family 1B member 1	Homo sapiens	46-53
16804942-0	2006	Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3"- 5"-diphosphate (PAP).	pap	132-135	sulfotransferase family 1B member 1	Homo sapiens	46-53
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 1B member 1	Homo sapiens	223-230
16305588-6	2005	O-DMN was sulphated by SULT1A1, SULT1B1 and SULT1E1.	o-dmn	0-5	sulfotransferase family 1B member 1	Homo sapiens	32-39
15929889-12	2005	The OH-PCBs tested were generally poor inhibitors of SULT1A3- and SULT1B1-dependent activity with 3-OH-BaP.	oh-pcbs	4-11	sulfotransferase family 1B member 1	Homo sapiens	66-73
15929889-12	2005	The OH-PCBs tested were generally poor inhibitors of SULT1A3- and SULT1B1-dependent activity with 3-OH-BaP.	3-hydroxybenzo(a)pyrene	98-106	sulfotransferase family 1B member 1	Homo sapiens	66-73
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 1B member 1	Homo sapiens	73-80
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 1B member 1	Homo sapiens	73-80
14609733-8	2003	Furthermore, sulfation of 4-nitrophenol by purified recombinant SULT1B1 was significant at concentrations of 4-nitrophenol less than 10 microM.	4-nitrophenol	26-39	sulfotransferase family 1B member 1	Homo sapiens	64-71
14609733-8	2003	Furthermore, sulfation of 4-nitrophenol by purified recombinant SULT1B1 was significant at concentrations of 4-nitrophenol less than 10 microM.	4-nitrophenol	109-122	sulfotransferase family 1B member 1	Homo sapiens	64-71
14609733-11	2003	We believe that in human liver other SULT isoforms (particularly SULT1B1) contribute to the sulfation of 4-nitrophenol.	4-nitrophenol	105-118	sulfotransferase family 1B member 1	Homo sapiens	65-72