PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21451505-0	2011	Effect of ABCC2 (MRP2) transport function on erythromycin metabolism.	Erythromycin	45-57	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	10-15	
21451505-0	2011	Effect of ABCC2 (MRP2) transport function on erythromycin metabolism.	Erythromycin	45-57	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	17-21	
21451505-2	2011	By means of a transporter screen, erythromycin was identified as a substrate for the transporter ABCC2 (MRP2) and its murine ortholog, Abcc2.	Erythromycin	34-46	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	97-102	
21451505-2	2011	By means of a transporter screen, erythromycin was identified as a substrate for the transporter ABCC2 (MRP2) and its murine ortholog, Abcc2.	Erythromycin	34-46	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	104-108	
21451505-2	2011	By means of a transporter screen, erythromycin was identified as a substrate for the transporter ABCC2 (MRP2) and its murine ortholog, Abcc2.	Erythromycin	34-46	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	135-140	
21451505-3	2011	Because these proteins are highly expressed on the biliary surface of hepatocytes, we hypothesized that impaired Abcc2 function may influence the rate of hepatobiliary excretion and thereby enhance erythromycin metabolism.	Erythromycin	198-210	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	113-118	
21451505-6	2011	These results suggest that impaired ABCC2 function can alter erythromycin metabolism, independent of changes in CYP3A4 activity.	Erythromycin	61-73	ATP-binding cassette, sub-family C (CFTR/MRP), member 2	Mus musculus	36-41