PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12837971-1	2003	Glucuronide and glutathione conjugates have been reported to be substrates of multidrug resistance protein 2 (Mrp2), whereas sulfates of nonbile acid organic anions have never been reported as substrates of Mrp2.	Glucuronides	0-11	ATP binding cassette subfamily B member 4	Rattus norvegicus	78-108	
12837971-1	2003	Glucuronide and glutathione conjugates have been reported to be substrates of multidrug resistance protein 2 (Mrp2), whereas sulfates of nonbile acid organic anions have never been reported as substrates of Mrp2.	Glucuronides	0-11	ATP binding cassette subfamily B member 4	Rattus norvegicus	110-114	
11348857-1	2001	To examine the substrate specificity of an ATP-dependent organic anion transporter, the multidrug resistance protein 2, we examined the effects of various bile acid conjugates and organic anions on the biliary excretion of phenolphthalein glucuronide, a hydrophilic glucuronide conjugate, in rats.	Glucuronides	239-250	ATP binding cassette subfamily B member 4	Rattus norvegicus	88-118	
11348857-1	2001	To examine the substrate specificity of an ATP-dependent organic anion transporter, the multidrug resistance protein 2, we examined the effects of various bile acid conjugates and organic anions on the biliary excretion of phenolphthalein glucuronide, a hydrophilic glucuronide conjugate, in rats.	Glucuronides	266-277	ATP binding cassette subfamily B member 4	Rattus norvegicus	88-118	
14569083-1	2003	Previous studies with mutant transport-deficient rats (TR(-)), in which the multidrug resistance protein 2 (Mrp2) is lacking, have emphasized the importance of this transport protein in the biliary excretion of a wide variety of glutathione conjugates, glucuronides, and other organic anions.	Glucuronides	253-265	ATP binding cassette subfamily B member 4	Rattus norvegicus	76-106	
14569083-1	2003	Previous studies with mutant transport-deficient rats (TR(-)), in which the multidrug resistance protein 2 (Mrp2) is lacking, have emphasized the importance of this transport protein in the biliary excretion of a wide variety of glutathione conjugates, glucuronides, and other organic anions.	Glucuronides	253-265	ATP binding cassette subfamily B member 4	Rattus norvegicus	108-112	
14511769-8	2003	FLAP stimulates bile flow up to 24% in control rats, but secretion is nearly absent in TR- rats further supporting an efficient transport of FLAP glucuronides by Mrp2.	Glucuronides	146-158	ATP binding cassette subfamily B member 4	Rattus norvegicus	162-166	
14511769-10	2003	In summary, we found that FLAP glucuronides are substrates of Mrp2 effectively inhibiting the biliary excretion of bilirubin.	Glucuronides	31-43	ATP binding cassette subfamily B member 4	Rattus norvegicus	62-66