PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	74-84	myeloperoxidase	Homo sapiens	22-37	
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	74-84	myeloperoxidase	Homo sapiens	39-42	
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	74-84	myeloperoxidase	Homo sapiens	212-215	
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	115-126	myeloperoxidase	Homo sapiens	22-37	
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	115-126	myeloperoxidase	Homo sapiens	39-42	
29293312-2	2018	The phagocytic enzyme myeloperoxidase (MPO) is coated with two functional polyphenol derivatives (platinum prodrug polyphenols and PEG polyphenols) and ferric ion by metal phenolic coordination, which can shield MPO from degradation by other compounds in the blood.	Polyphenols	115-126	myeloperoxidase	Homo sapiens	212-215	
23221717-4	2012	Polyphenols, including catechins, curcumin, resveratrol, silibinin, and sulfurous compound alpha-lipoic acid, were found to inhibit both HOCl- and human MPO-induced Cl-Guo formation dose-dependently.	Polyphenols	0-11	myeloperoxidase	Homo sapiens	153-156	
24514562-4	2014	A correlation was observed between the polyphenol content and the MPO inhibition.	Polyphenols	39-49	myeloperoxidase	Homo sapiens	66-69	
24176923-9	2014	The results are in accordance with previous stopped-flow kinetic studies which showed a high reactivity of the polyphenol with MPO compound II.	Polyphenols	111-121	myeloperoxidase	Homo sapiens	127-130	
23072830-7	2013	Finally, all specimens containing polyphenols efficiently inhibited the MPO activity.	Polyphenols	34-45	myeloperoxidase	Homo sapiens	72-75	
18512968-2	2008	Because little is known about the protective role of natural antioxidants, such as polyphenols, for the myeloperoxidase-derived DNA damage, we screened the inhibitory effects of various phenolic antioxidants on the chlorination of the 2"-deoxycytidine residue by HOCl in vitro and found that green tea catechins, especially (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), significantly inhibited the chlorination.	Polyphenols	83-94	myeloperoxidase	Homo sapiens	104-119	
19053991-7	2009	The polyphenols were not cytotoxic and blocked N-formyl-methyl-leucyl-phenylalanine-induced myeloperoxidase release and activity in human neutrophils.	Polyphenols	4-15	myeloperoxidase	Homo sapiens	92-107