PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22562044-2	2012	Despite its distinct substrate specificity from the classic nucleoside transporters ENT1 and 2, PMAT appears to share similar protein architecture with ENT1/2 and retains low affinity binding to classic ENT inhibitors such as nitrobenzylmercaptopurine riboside (NBMPR) and the coronary vasodilators dilazep and dipyridamole.	Dipyridamole	311-323	solute carrier family 29 member 4	Homo sapiens	96-100	
16873718-6	2006	ENT4-mediated nucleoside transport was adenosine selective, sodium independent and only weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine.	Dipyridamole	172-184	solute carrier family 29 member 4	Homo sapiens	0-4	
26979520-2	2016	The gastrointestinal uptake of metformin is mediated by the human equilibrative nucleoside transporter 4 (ENT4), which is inhibited by dipyridamole in preclinical studies.	Dipyridamole	135-147	solute carrier family 29 member 4	Homo sapiens	66-104	
26979520-2	2016	The gastrointestinal uptake of metformin is mediated by the human equilibrative nucleoside transporter 4 (ENT4), which is inhibited by dipyridamole in preclinical studies.	Dipyridamole	135-147	solute carrier family 29 member 4	Homo sapiens	106-110	
26979520-10	2016	CONCLUSIONS: Previous in vitro studies report that dipyridamole inhibits the ENT4 transporter that mediates gastrointestinal uptake of metformin.	Dipyridamole	51-63	solute carrier family 29 member 4	Homo sapiens	77-81	
24021350-4	2013	Of the dipyridamole analogs evaluated, about one fourth of the compounds inhibited hENT4 with higher potencies than dipyridamole.	Dipyridamole	7-19	solute carrier family 29 member 4	Homo sapiens	83-88