PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8385794-7	1993	The MPO-dependent autoactivation of latent metalloenzymes by PMN, with consequent A1PI inactivation, was inhibited by the nonsteroidal anti-inflammatory drug nimesulide (NMS).	nimesulide	158-168	myeloperoxidase	Homo sapiens	4-7	
7506191-0	1993	Nimesulide as a downregulator of the activity of the neutrophil myeloperoxidase pathway.	nimesulide	0-10	myeloperoxidase	Homo sapiens	64-79	
8385794-7	1993	The MPO-dependent autoactivation of latent metalloenzymes by PMN, with consequent A1PI inactivation, was inhibited by the nonsteroidal anti-inflammatory drug nimesulide (NMS).	nimesulide	170-173	myeloperoxidase	Homo sapiens	4-7	
20939553-0	2010	Neutrophil- and myeloperoxidase-mediated metabolism of reduced nimesulide: evidence for bioactivation.	nimesulide	63-73	myeloperoxidase	Homo sapiens	16-31	
2170285-1	1990	The anti-inflammatory drug nimesulide was found to effectively reduce the availability of hypochlorous acid, the most potent chlorinated oxidant generated by the myeloperoxidase system of activated neutrophils.	nimesulide	27-37	myeloperoxidase	Homo sapiens	162-177	
20939553-8	2010	We demonstrate here that the reduced nimesulide, M1, undergoes a facile oxidation with activated neutrophils or with MPO in the presence of H(2)O(2) or HOCl to produce a variety of reactive as well as stable metabolites.	nimesulide	37-47	myeloperoxidase	Homo sapiens	117-120	
20939553-10	2010	Other metabolites, for example, M6, M8, and M9, were unique to the myeloperoxidase, because of their mode of formation from activation of the amino group of reduced nimesulide.	nimesulide	165-175	myeloperoxidase	Homo sapiens	67-82	
20939553-13	2010	In summary, our results demonstrate that a known nimesulide metabolite could be bioactivated by MPO through a pathway distinct from HLM-mediated pathways and that the generation of reactive species by the MPO-mediated bioactivation pathway at the site of inflammation may contribute to the toxicity associated with nimesulide.	nimesulide	49-59	myeloperoxidase	Homo sapiens	96-99	
20939553-13	2010	In summary, our results demonstrate that a known nimesulide metabolite could be bioactivated by MPO through a pathway distinct from HLM-mediated pathways and that the generation of reactive species by the MPO-mediated bioactivation pathway at the site of inflammation may contribute to the toxicity associated with nimesulide.	nimesulide	49-59	myeloperoxidase	Homo sapiens	205-208	
20939553-13	2010	In summary, our results demonstrate that a known nimesulide metabolite could be bioactivated by MPO through a pathway distinct from HLM-mediated pathways and that the generation of reactive species by the MPO-mediated bioactivation pathway at the site of inflammation may contribute to the toxicity associated with nimesulide.	nimesulide	315-325	myeloperoxidase	Homo sapiens	96-99	
20939553-13	2010	In summary, our results demonstrate that a known nimesulide metabolite could be bioactivated by MPO through a pathway distinct from HLM-mediated pathways and that the generation of reactive species by the MPO-mediated bioactivation pathway at the site of inflammation may contribute to the toxicity associated with nimesulide.	nimesulide	315-325	myeloperoxidase	Homo sapiens	205-208	
17610876-1	2007	The present in vitro study was designed to assess the inhibition of the myeloperoxidase (MPO)/H(2)O(2)/Cl(-) system by several non steroidal anti-inflammatory drugs (NSAIDs) of the oxicam family and of nimesulide and to compare their effect with flufenamic acid in order to investigate their influence on the chlorinating activity of MPO as a protective mechanism during chronic inflammatory syndromes.	nimesulide	202-212	myeloperoxidase	Homo sapiens	72-87	
17610876-1	2007	The present in vitro study was designed to assess the inhibition of the myeloperoxidase (MPO)/H(2)O(2)/Cl(-) system by several non steroidal anti-inflammatory drugs (NSAIDs) of the oxicam family and of nimesulide and to compare their effect with flufenamic acid in order to investigate their influence on the chlorinating activity of MPO as a protective mechanism during chronic inflammatory syndromes.	nimesulide	202-212	myeloperoxidase	Homo sapiens	89-92