PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15910880-5	2005	We here review current knowledge on the molecular basis of the interaction of classical K(ATP) channel openers (cromakalim, pinacidil, diazoxide) with SUR.	Pinacidil	124-133	ATP binding cassette subfamily C member 8	Homo sapiens	151-154	
18723823-4	2008	SUR1- but not SUR2-containing channels are highly sensitive to metabolic inhibition and diazoxide, whereas SUR2 channels are sensitive to pinacidil.	Pinacidil	138-147	ATP binding cassette subfamily C member 8	Homo sapiens	0-4	
18723823-9	2008	Consistent with this, heteromeric SUR1+SUR2A channels were sensitive to azide, diazoxide, and pinacidil, and their single-channel burst duration was 2-fold longer than that of the T1 channels.	Pinacidil	94-103	ATP binding cassette subfamily C member 8	Homo sapiens	34-38	
18723823-9	2008	Consistent with this, heteromeric SUR1+SUR2A channels were sensitive to azide, diazoxide, and pinacidil, and their single-channel burst duration was 2-fold longer than that of the T1 channels.	Pinacidil	94-103	ATP binding cassette subfamily C member 8	Homo sapiens	39-44	
15561900-7	2004	In competition experiments using [3H]glibenclamide as radioligand, SUR1(T1285L, M1289T) showed much higher affinity toward the cyanoguanidine openers pinacidil and P1075 than SUR1 wild type.	Pinacidil	150-159	ATP binding cassette subfamily C member 8	Homo sapiens	67-71	
12496311-7	2003	The F1388L-SUR1 channel has increased sensitivity to MgADP and metabolic inhibition, decreased sensitivity to glibenclamide, and responds to both diazoxide and pinacidil.	Pinacidil	160-169	ATP binding cassette subfamily C member 8	Homo sapiens	11-15