PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30918256-2	2019	Myoglobin binds O2, facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species.	Superoxides	16-18	myoglobin	Homo sapiens	0-9	
30918256-5	2019	Biochemical characterization reveals that the mutant myoglobin has altered O2 binding, exhibits a faster heme dissociation rate and has a lower reduction potential compared to wild-type myoglobin.	Superoxides	75-77	myoglobin	Homo sapiens	53-62	
30918256-6	2019	Preliminary studies show that mutant myoglobin may result in elevated superoxide levels at the cellular level.	Superoxides	70-80	myoglobin	Homo sapiens	37-46	
15325298-1	2004	This study shows that hydroethidine (HE) used for the qualitative detection of superoxide anion can also be oxidized by heme proteins such as the mitochondrial cytochromes, hemoglobin, and myoglobin, forming spectrally nonhomogenous mixtures of HE-derived products of various oxidation states.	Superoxides	79-95	myoglobin	Homo sapiens	189-198	
3939140-3	1985	To understand fully the interaction between reactive oxygen metabolites, myoglobin and lipid, we investigate the possibility that myoglobin may use xanthine oxidase-generated superoxide and/or hydrogen peroxide to catalyze peroxidation of a polyunsaturated fatty acid.	Superoxides	175-185	myoglobin	Homo sapiens	130-139	
10401602-2	1999	Myoglobin has not been viewed as a participant but is present in relatively high concentrations in heart muscle and, even under normal conditions, undergoes reactions that generate met (Fe3+) species and also superoxide, hydrogen peroxide, and other oxidants, albeit slowly.	Superoxides	209-219	myoglobin	Homo sapiens	0-9