PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27826418-4	2016	We tested the activity of full length recombinant human heme oxygenase-2 (FL-hHO-2) and its analog in which cys265 and cys282 were both replaced by alanine to determine the effect on activation by menadione (MD) and inhibition by QC-2350.	Vitamin K 3	197-206	heme oxygenase 2	Homo sapiens	56-72	
22039914-0	2011	Selective activation of heme oxygenase-2 by menadione.	Vitamin K 3	44-53	heme oxygenase 2	Homo sapiens	24-40	
24533775-1	2014	BACKGROUND: Previously, we reported that menadione activated rat, native heme oxygenase-2 (HO-2) and human recombinant heme oxygenase-2 selectively; it did not activate spleen, microsomal heme oxygenase-1.	Vitamin K 3	41-50	heme oxygenase 2	Homo sapiens	119-135	
24533775-8	2014	Menadione activated full-length recombinant human heme oxygenase-2 (FL-hHO-2) as effectively as rat brain enzyme, but it did not activate rat spleen heme oxygenase.	Vitamin K 3	0-9	heme oxygenase 2	Homo sapiens	50-66	
22039914-5	2011	This communication describes our observations of the up to 30-fold increase in the in-vitro activation of HO-2 by menadione.	Vitamin K 3	114-123	heme oxygenase 2	Homo sapiens	106-110	
31550661-7	2019	Furthermore, the development of HO-2 activators, such as menadione analogues, helped to understand the critical moieties required for HO-2 activation.	Vitamin K 3	57-66	heme oxygenase 2	Homo sapiens	32-36	
31550661-7	2019	Furthermore, the development of HO-2 activators, such as menadione analogues, helped to understand the critical moieties required for HO-2 activation.	Vitamin K 3	57-66	heme oxygenase 2	Homo sapiens	134-138	
28480030-2	2017	Previously, we observed that brain microsomes containing HO-2 produced many-fold more CO in the presence of menadione and its congeners; herein we explored these observations further.	Vitamin K 3	108-117	heme oxygenase 2	Homo sapiens	57-61