PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
5512438-0	1970	[Photometric determination of myeloperoxidase with p-phenylenediamine].	4-phenylenediamine	51-69	myeloperoxidase	Homo sapiens	30-45	
170559-10	1975	Myeloperoxidase activity was tested with paraphenylenediamine and was found to be normal on two occasions.	4-phenylenediamine	41-61	myeloperoxidase	Homo sapiens	0-15	
23843990-3	2013	This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo.	4-phenylenediamine	174-192	myeloperoxidase	Homo sapiens	138-141	
23843990-3	2013	This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo.	4-phenylenediamine	174-192	myeloperoxidase	Homo sapiens	206-209	
19031316-3	2008	The contact between CP and MPO probably entails conformational changes close to the p-phenylenediamine binding site in CP, which explains the observed activation by MPO of the substrate"s oxidation.	4-phenylenediamine	84-102	myeloperoxidase	Homo sapiens	27-30	
19031316-3	2008	The contact between CP and MPO probably entails conformational changes close to the p-phenylenediamine binding site in CP, which explains the observed activation by MPO of the substrate"s oxidation.	4-phenylenediamine	84-102	myeloperoxidase	Homo sapiens	165-168