PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22077213-2	2011	It was shown that testosterone and androsterone have a high constant of binding to the membranes (K(b)   10(6) M(-1)), whereas K(b)"s for DHEA and DHEAS are 2 orders of magnitude lower.	Androsterone	35-47	sulfotransferase family 2A member 1	Homo sapiens	147-152	
7589785-5	1995	This recombinant cell line allowed determination of the substrate specificity and kinetic properties of this enzyme towards various steroid hormones, and by comparison of these activities with human liver cytosol we have shown that HST is the major sulphotransferase responsible for the sulphation of DHEA, androsterone and pregnenolone in man and that, functionally, the hepatic and adrenal enzymes are very similar.	Androsterone	307-319	sulfotransferase family 2A member 1	Homo sapiens	232-235	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	12-24	sulfotransferase family 2A member 1	Homo sapiens	64-103	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	12-24	sulfotransferase family 2A member 1	Homo sapiens	105-112	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	26-29	sulfotransferase family 2A member 1	Homo sapiens	64-103	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	26-29	sulfotransferase family 2A member 1	Homo sapiens	105-112	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	173-176	sulfotransferase family 2A member 1	Homo sapiens	64-103	
14573603-0	2004	Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.	Androsterone	173-176	sulfotransferase family 2A member 1	Homo sapiens	105-112	
14573603-5	2004	The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition.	Androsterone	47-50	sulfotransferase family 2A member 1	Homo sapiens	23-30	
14573603-5	2004	The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition.	Androsterone	99-102	sulfotransferase family 2A member 1	Homo sapiens	23-30	
8943792-1	1996	Human dehydroepiandrosterone sulfotransferase (DHEA-ST) catalyzes the sulfonation of DHEA, cholesterol, pregnenolone as well as androsterone.	Androsterone	16-28	sulfotransferase family 2A member 1	Homo sapiens	47-54	
18042734-4	2008	In addition, Met-137 was proposed to regulate the binding orientations of DHEA and ADT in SULT2A1.	Androsterone	83-86	sulfotransferase family 2A member 1	Homo sapiens	90-97	
18042734-5	2008	Complete elimination or regeneration of substrate inhibition for SULT2A1 with DHEA or ADT as substrate, respectively, was demonstrated with the mutations of Met-137 on Y238A mutant.	Androsterone	86-89	sulfotransferase family 2A member 1	Homo sapiens	65-72