PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29743239-3	2018	Human PAPSS2 mutations manifest with undetectable DHEA sulfate, androgen excess, and metabolic disease, suggesting that ubiquitous PAPSS1 cannot compensate for deficient PAPSS2 in supporting DHEA sulfation.	Dehydroepiandrosterone Sulfate	50-62	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	6-12	
35415222-14	2022	Discussion: PAPSS2 assists with the sulfonation of dehydroepiandrosterone (DHEA) to DHEA sulfate and the sulfonation of proteoglycans in the cartilage, necessary for endochondral bone formation.	Dehydroepiandrosterone Sulfate	84-96	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	12-18	
25594860-2	2015	Impaired DHEA sulfation is thought to increase the conversion of DHEA toward active androgens, a proposition supported by the previous report of a girl with inactivating PAPSS2 mutations who presented with low serum DHEA sulfate and androgen excess, clinically manifesting with premature pubarche and early-onset polycystic ovary syndrome.	Dehydroepiandrosterone Sulfate	216-228	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	170-176	
25594860-3	2015	PATIENTS AND METHODS: We investigated a family harboring two novel PAPSS2 mutations, including two compound heterozygous brothers presenting with disproportionate short stature, low serum DHEA sulfate, but normal serum androgens.	Dehydroepiandrosterone Sulfate	188-200	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	67-73