PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23353586-2	2013	The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE.	Aminosalicylic Acid	157-160	acetylcholinesterase (Cartwright blood group)	Homo sapiens	33-37	
23353586-2	2013	The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE.	Aminosalicylic Acid	157-160	acetylcholinesterase (Cartwright blood group)	Homo sapiens	165-169	
23353586-3	2013	In the present study, a workflow has been developed for the identification and prioritization of potential compounds that could interact not only with the catalytic site but also with the PAS of AChE.	Aminosalicylic Acid	188-191	acetylcholinesterase (Cartwright blood group)	Homo sapiens	195-199	
23353586-10	2013	The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE.	Aminosalicylic Acid	235-238	acetylcholinesterase (Cartwright blood group)	Homo sapiens	79-83	
23353586-10	2013	The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE.	Aminosalicylic Acid	235-238	acetylcholinesterase (Cartwright blood group)	Homo sapiens	242-246