PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18930752-7	2008	PAH secretion across the monolayer consisted of the uptake of PAH across the basolateral membrane by OAT1 and OAT3 and the apical exit of PAH by a probenecid and MK571-sensitive route consistent with actions of MRP2 or MRP4.	p-Aminohippuric Acid	0-3	ATP binding cassette subfamily C member 2	Homo sapiens	211-215	
17498396-10	2007	MPAG strongly inhibited the uptake of PAH via both rMrp2 and hMRP2.	p-Aminohippuric Acid	38-41	ATP binding cassette subfamily C member 2	Homo sapiens	61-66	
10760098-0	2000	ATP-dependent para-aminohippurate transport by apical multidrug resistance protein MRP2.	p-Aminohippuric Acid	14-33	ATP binding cassette subfamily C member 2	Homo sapiens	83-87	
10760098-1	2000	BACKGROUND: Para-aminohippurate (PAH), a widely used model substrate for organic anion transport in proximal tubule epithelia, was investigated as a substrate for the apical multidrug resistance protein MRP2 (symbol ABCC2).	p-Aminohippuric Acid	12-31	ATP binding cassette subfamily C member 2	Homo sapiens	203-207	
10760098-1	2000	BACKGROUND: Para-aminohippurate (PAH), a widely used model substrate for organic anion transport in proximal tubule epithelia, was investigated as a substrate for the apical multidrug resistance protein MRP2 (symbol ABCC2).	p-Aminohippuric Acid	12-31	ATP binding cassette subfamily C member 2	Homo sapiens	216-221	
10760098-1	2000	BACKGROUND: Para-aminohippurate (PAH), a widely used model substrate for organic anion transport in proximal tubule epithelia, was investigated as a substrate for the apical multidrug resistance protein MRP2 (symbol ABCC2).	p-Aminohippuric Acid	33-36	ATP binding cassette subfamily C member 2	Homo sapiens	203-207	
10760098-1	2000	BACKGROUND: Para-aminohippurate (PAH), a widely used model substrate for organic anion transport in proximal tubule epithelia, was investigated as a substrate for the apical multidrug resistance protein MRP2 (symbol ABCC2).	p-Aminohippuric Acid	33-36	ATP binding cassette subfamily C member 2	Homo sapiens	216-221	
10760098-7	2000	The high-affinity substrate leukotriene C4 and the inhibitor of MRP-mediated transport, MK571, inhibited MRP2-mediated transport of PAH (100 nmol/L) with IC50 values of 3.3 and 4.0 micromol/L, respectively.	p-Aminohippuric Acid	132-135	ATP binding cassette subfamily C member 2	Homo sapiens	105-109	
10760098-8	2000	The nephrotoxic mycotoxin ochratoxin A inhibited MRP2-mediated PAH transport with an IC50 value of 58 micromol/L.	p-Aminohippuric Acid	63-66	ATP binding cassette subfamily C member 2	Homo sapiens	49-53	
10760098-10	2000	CONCLUSIONS: PAH is a good substrate for the ATP-dependent export pump MRP2.	p-Aminohippuric Acid	13-16	ATP binding cassette subfamily C member 2	Homo sapiens	71-75	
10760098-11	2000	The localization and function of MRP2 indicate that this unidirectional transport protein contributes to the secretion of PAH and other amphiphilic anions into the lumen of kidney proximal tubules.	p-Aminohippuric Acid	122-125	ATP binding cassette subfamily C member 2	Homo sapiens	33-37