PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17110033-3	2007	Fluorescein (FL), a marker for paracellular permeability, is a substrate for the transport proteins organic anion transporter (OAT)-3 and multidrug resistance protein (MRP)-2 at the BBB.	Fluorescein	0-11	ATP binding cassette subfamily C member 2	Rattus norvegicus	138-174	
17110033-3	2007	Fluorescein (FL), a marker for paracellular permeability, is a substrate for the transport proteins organic anion transporter (OAT)-3 and multidrug resistance protein (MRP)-2 at the BBB.	Fluorescein	13-15	ATP binding cassette subfamily C member 2	Rattus norvegicus	138-174	
17110033-4	2007	Furthermore, MRP-2-mediated efflux of FL can be upregulated by glucose.	Fluorescein	38-40	ATP binding cassette subfamily C member 2	Rattus norvegicus	13-18	
15139520-0	2004	D-glucose triggers multidrug resistance-associated protein (MRP)-mediated secretion of fluorescein across rat jejunum in vitro.	Fluorescein	87-98	ATP binding cassette subfamily C member 2	Rattus norvegicus	19-58	
15139520-0	2004	D-glucose triggers multidrug resistance-associated protein (MRP)-mediated secretion of fluorescein across rat jejunum in vitro.	Fluorescein	87-98	ATP binding cassette subfamily C member 2	Rattus norvegicus	60-63	
15139520-1	2004	PURPOSE: To examine the transport characteristics of the multidrug resistance-associated protein (MRP) substrate fluorescein across the isolated rat small intestinal segments.	Fluorescein	113-124	ATP binding cassette subfamily C member 2	Rattus norvegicus	57-96	
15139520-1	2004	PURPOSE: To examine the transport characteristics of the multidrug resistance-associated protein (MRP) substrate fluorescein across the isolated rat small intestinal segments.	Fluorescein	113-124	ATP binding cassette subfamily C member 2	Rattus norvegicus	98-101	
15139520-7	2004	The polarization of fluorescein transport was almost completely abolished by MRP inhibitor, benzbromarone (50 or 100 microM, applied apically), and by MRP/P-glycoprotein inhibitor, verapamil (200 microM, applied apically).	Fluorescein	20-31	ATP binding cassette subfamily C member 2	Rattus norvegicus	77-80	
15139520-7	2004	The polarization of fluorescein transport was almost completely abolished by MRP inhibitor, benzbromarone (50 or 100 microM, applied apically), and by MRP/P-glycoprotein inhibitor, verapamil (200 microM, applied apically).	Fluorescein	20-31	ATP binding cassette subfamily C member 2	Rattus norvegicus	151-154	
15139520-8	2004	CONCLUSIONS: D-glucose at the mucosal side activates fluorescein secretion across rat jejunum by an apical MRP, most probably by isoform 2 (MRP2), which could have an impact on the intestinal absorption of MRP substrates.	Fluorescein	53-64	ATP binding cassette subfamily C member 2	Rattus norvegicus	107-110	
15139520-8	2004	CONCLUSIONS: D-glucose at the mucosal side activates fluorescein secretion across rat jejunum by an apical MRP, most probably by isoform 2 (MRP2), which could have an impact on the intestinal absorption of MRP substrates.	Fluorescein	53-64	ATP binding cassette subfamily C member 2	Rattus norvegicus	140-144	
15139520-8	2004	CONCLUSIONS: D-glucose at the mucosal side activates fluorescein secretion across rat jejunum by an apical MRP, most probably by isoform 2 (MRP2), which could have an impact on the intestinal absorption of MRP substrates.	Fluorescein	53-64	ATP binding cassette subfamily C member 2	Rattus norvegicus	140-143	
12495220-5	2002	In cultures, the correct secretion of fluorescein (mrp2-mediated) into bile canaliculi was observed.	Fluorescein	38-49	ATP binding cassette subfamily C member 2	Rattus norvegicus	51-55	
11758761-6	2001	RESULTS: In vitro experiments showed that probenecid, indomethacin, LY-329146, and all MRP inhibitors significantly increased (two- to threefold) the accumulation of fluorescein in BBMEC, whereas LY-335979, a P-gp inhibitor, had no effect on the accumulation of fluorescein.	Fluorescein	166-177	ATP binding cassette subfamily C member 2	Rattus norvegicus	87-90	
11758761-6	2001	RESULTS: In vitro experiments showed that probenecid, indomethacin, LY-329146, and all MRP inhibitors significantly increased (two- to threefold) the accumulation of fluorescein in BBMEC, whereas LY-335979, a P-gp inhibitor, had no effect on the accumulation of fluorescein.	Fluorescein	262-273	ATP binding cassette subfamily C member 2	Rattus norvegicus	87-90	
11758761-9	2001	CONCLUSIONS: These results demonstrate that MRPs or MRP-like transport system(s) may play an important role in fluorescein distribution across both BBB and BCSFB.	Fluorescein	111-122	ATP binding cassette subfamily C member 2	Rattus norvegicus	44-47	
10820430-9	2000	Moreover, indomethacin, probenecid, and sulfinpyrazone increased the uptake of fluorescein (a substrate of MRP but not of P-gp).	Fluorescein	79-90	ATP binding cassette subfamily C member 2	Rattus norvegicus	107-110