PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25921265-3	2015	The results of the former gave us pivotal information on the further optimization of the P4 moiety in plasmin inhibitors and those of the latter revealed that appropriate moieties extending from the benzimidazole scaffold engaged with S4 pocket in the active site of plasmin.	benzimidazole	199-212	plasminogen	Homo sapiens	102-109	
25921265-3	2015	The results of the former gave us pivotal information on the further optimization of the P4 moiety in plasmin inhibitors and those of the latter revealed that appropriate moieties extending from the benzimidazole scaffold engaged with S4 pocket in the active site of plasmin.	benzimidazole	199-212	plasminogen	Homo sapiens	267-274	
27009905-0	2016	Plasmin inhibitors with hydrophobic amino acid-based linker between hydantoin moiety and benzimidazole scaffold enhance inhibitory activity.	benzimidazole	89-102	plasminogen	Homo sapiens	0-7	
27009905-1	2016	In this letter we report the design and synthesis of a series of plasmin inhibitors, which share the amino acid-based linker with limited free rotation between the hydantoin moiety and the benzimidazole scaffold.	benzimidazole	189-202	plasminogen	Homo sapiens	65-72