PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23928335-12	2013	Furthermore, incubation of catechol estrogens with myeloperoxidase (MPO) in the presence of HCys resulted in the formation of respective estrogen-HCys conjugates.	catechol	27-35	myeloperoxidase	Homo sapiens	51-66	
23928335-12	2013	Furthermore, incubation of catechol estrogens with myeloperoxidase (MPO) in the presence of HCys resulted in the formation of respective estrogen-HCys conjugates.	catechol	27-35	myeloperoxidase	Homo sapiens	68-71	
23905650-8	2013	The 4-methylcoumarin derivatives bearing the catechol group suppressed the elastase and myeloperoxidase activity and reduced the 1,1-diphenyl-2-picrylhydrazyl free radical the most strongly.	catechol	45-53	myeloperoxidase	Homo sapiens	75-103	
1654782-4	1991	In order to gain insights into the mechanisms of this stimulation, we have compared the kinetics of human myeloperoxidase-dependent phenol, hydroquinone, and catechol metabolism.	catechol	158-166	myeloperoxidase	Homo sapiens	106-121	
1654782-5	1991	The specificity (Vmax/Km) of hydroquinone for myeloperoxidase was found to be 5-fold greater than that of catechol and 16-fold greater than that of phenol.	catechol	106-114	myeloperoxidase	Homo sapiens	46-61	
1654782-6	1991	These specificities for myeloperoxidase-dependent metabolism inversely correlated with the respective one-electron oxidation potentials of hydroquinone, catechol, and phenol and suggested that phenol- and catechol-induced stimulation of myeloperoxidase-dependent hydroquinone metabolism cannot simply be explained by interaction of hydroquinone with stimulant-derived radicals.	catechol	153-161	myeloperoxidase	Homo sapiens	24-39	
1654782-6	1991	These specificities for myeloperoxidase-dependent metabolism inversely correlated with the respective one-electron oxidation potentials of hydroquinone, catechol, and phenol and suggested that phenol- and catechol-induced stimulation of myeloperoxidase-dependent hydroquinone metabolism cannot simply be explained by interaction of hydroquinone with stimulant-derived radicals.	catechol	153-161	myeloperoxidase	Homo sapiens	237-252	
1654782-6	1991	These specificities for myeloperoxidase-dependent metabolism inversely correlated with the respective one-electron oxidation potentials of hydroquinone, catechol, and phenol and suggested that phenol- and catechol-induced stimulation of myeloperoxidase-dependent hydroquinone metabolism cannot simply be explained by interaction of hydroquinone with stimulant-derived radicals.	catechol	205-213	myeloperoxidase	Homo sapiens	24-39	
1654782-6	1991	These specificities for myeloperoxidase-dependent metabolism inversely correlated with the respective one-electron oxidation potentials of hydroquinone, catechol, and phenol and suggested that phenol- and catechol-induced stimulation of myeloperoxidase-dependent hydroquinone metabolism cannot simply be explained by interaction of hydroquinone with stimulant-derived radicals.	catechol	205-213	myeloperoxidase	Homo sapiens	237-252	
1654782-7	1991	Phenol (100 microM), catechol (20 microM), and imidazole (50 mM) did, however, all increase the specificity (Vmax/Km) of hydroquinone for myeloperoxidase, indicating that these three compounds may be stimulating hydroquinone metabolism by a common mechanism.	catechol	21-29	myeloperoxidase	Homo sapiens	138-153	
6300234-5	1983	These results indicate that aggregation was due to MPO-H2O2-mediated oxidation of catechol to orthoquinone, which was deemed to be directly responsible for cross-linking by non-enzymic biochemical reactions.	catechol	82-90	myeloperoxidase	Homo sapiens	51-54	
1648866-0	1991	Effect of phenol and catechol on the kinetics of human myeloperoxidase-dependent hydroquinone metabolism.	catechol	21-29	myeloperoxidase	Homo sapiens	55-70	
1651573-1	1991	The effects of two catechols (1,2-benzenediol and nordihydroguaiaretic acid) on the myeloperoxidase-Cl(-)-H2O2 antimicrobial/cytotoxic system of the human neutrophil were investigated.	catechol	30-45	myeloperoxidase	Homo sapiens	84-99	
24916123-6	2014	In the present study we show that oxidation of the catechol moiety of epicatechins to an omicron-quinone by MPO generates potent MIF inhibitors.	catechol	51-59	myeloperoxidase	Homo sapiens	108-111