PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22517357-6	2012	Although the active secretory flux of oxalate across mouse duodenum was strongly inhibited (>90%) by addition of the disulfonic stilbene DIDS to the basolateral solution, secretion was unaffected by changes in medium concentrations of sulfate and bicarbonate, key substrates for Sat1-mediated anion exchange.	Oxalates	38-45	spermidine/spermine N1-acetyl transferase 1	Mus musculus	282-286	
17693766-4	2007	RECENT FINDINGS: In proximal tubules, Slc26a1 (Sat-1) mediates sulfate and oxalate transport across the basolateral membrane, while Slc26a6 (CFEX, Pat-1) mediates a variety of anion exchange at the apical membrane to facilitate transcellular sodium chloride absorption.	Oxalates	75-82	spermidine/spermine N1-acetyl transferase 1	Mus musculus	47-52	
30383413-1	2019	The anion exchanger SAT-1 [sulfate anion transporter 1 (Slc26a1)] is considered an important regulator of oxalate and sulfate homeostasis, but the mechanistic basis of these critical roles remain undetermined.	Oxalates	106-113	spermidine/spermine N1-acetyl transferase 1	Mus musculus	20-25	
30383413-11	2019	NEW & NOTEWORTHY SAT-1 is a membrane-bound transport protein expressed in the intestine, liver, and kidney, where it is widely considered essential for the excretion of oxalate, a potentially toxic waste metabolite.	Oxalates	169-176	spermidine/spermine N1-acetyl transferase 1	Mus musculus	17-22	
30383413-12	2019	Previously, calcium oxalate kidney stone formation by the SAT-1-knockout mouse generated the hypothesis that SAT-1 has a major role in oxalate excretion via the intestine.	Oxalates	20-27	spermidine/spermine N1-acetyl transferase 1	Mus musculus	58-63	
30383413-12	2019	Previously, calcium oxalate kidney stone formation by the SAT-1-knockout mouse generated the hypothesis that SAT-1 has a major role in oxalate excretion via the intestine.	Oxalates	20-27	spermidine/spermine N1-acetyl transferase 1	Mus musculus	109-114