PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22529530-1	2012	Extracellular superoxide dismutase (SOD3), an enzyme mediating dismutation of superoxide into hydrogen peroxide, has been shown to reduce inflammation by inhibiting macrophage migration into injured tissues.	Hydrogen Peroxide	94-111	superoxide dismutase 3, extracellular	Mus musculus	0-34	
22529530-1	2012	Extracellular superoxide dismutase (SOD3), an enzyme mediating dismutation of superoxide into hydrogen peroxide, has been shown to reduce inflammation by inhibiting macrophage migration into injured tissues.	Hydrogen Peroxide	94-111	superoxide dismutase 3, extracellular	Mus musculus	36-40	
35142393-9	2022	Furthermore, exosomes overexpressing SOD3 significantly enhanced angiogenesis in ECs by increasing local H2 O2  levels in a heparin-binding domain-dependent manner as well as restored defective wound healing and angiogenesis in T2DM or SOD3-/- mice.	Hydrogen Peroxide	105-110	superoxide dismutase 3, extracellular	Mus musculus	37-41	
20422004-2	2010	Extracellular superoxide dismutase (ecSOD) is a major secreted extracellular enzyme that catalyzes the dismutation of superoxide to H(2)O(2), and anchors to EC surface through heparin-binding domain (HBD).	Hydrogen Peroxide	132-140	superoxide dismutase 3, extracellular	Mus musculus	0-34	
20422004-2	2010	Extracellular superoxide dismutase (ecSOD) is a major secreted extracellular enzyme that catalyzes the dismutation of superoxide to H(2)O(2), and anchors to EC surface through heparin-binding domain (HBD).	Hydrogen Peroxide	132-140	superoxide dismutase 3, extracellular	Mus musculus	36-41	
20422004-6	2010	Mice lacking ecSOD show reduction of H(2)O(2) in non-ischemic and ischemic limbs.	Hydrogen Peroxide	37-45	superoxide dismutase 3, extracellular	Mus musculus	13-18	
17170376-7	2007	Incubation of aortic segments with peroxynitrite or hydrogen peroxide attenuated ecSOD activity, but peroxynitrite did not induce tyrosine nitration of ecSOD, suggesting oxidative inactivation of the enzyme.	Hydrogen Peroxide	52-69	superoxide dismutase 3, extracellular	Mus musculus	81-86	
20422004-15	2010	In summary, extracellular H(2)O(2) generated by ecSOD localized at caveolae/lipid rafts via HBD promotes VEGFR2 signaling via oxidative inactivation of PTPs in these microdomains.	Hydrogen Peroxide	26-34	superoxide dismutase 3, extracellular	Mus musculus	48-53	
12231557-3	2002	METHODS AND RESULTS: In the presence of HCO3-, SOD3 reacted with H2O2 to produce a hydroxyl radical adduct of the spin trap 5-diethoxyphosphoryl-5methyl-1-pyrroline N-oxide (DEMPO).	Hydrogen Peroxide	65-69	superoxide dismutase 3, extracellular	Mus musculus	47-51	
12231557-4	2002	SOD1 and SOD3 were inactivated by H2O2 in a dose- and time-dependent fashion, and this was prevented by physiological levels of uric acid.	Hydrogen Peroxide	34-38	superoxide dismutase 3, extracellular	Mus musculus	9-13	
33919252-1	2021	Superoxide dismutase (SOD) family isoenzymes, SOD1, SOD2, and SOD3, synthesize hydrogen peroxide (H2O2), which regulates the signal transduction.	Hydrogen Peroxide	79-96	superoxide dismutase 3, extracellular	Mus musculus	62-66	
33919252-1	2021	Superoxide dismutase (SOD) family isoenzymes, SOD1, SOD2, and SOD3, synthesize hydrogen peroxide (H2O2), which regulates the signal transduction.	Hydrogen Peroxide	98-102	superoxide dismutase 3, extracellular	Mus musculus	62-66	
33919252-4	2021	Similar to the H2O2 response in the cells, the cellular response of SOD3 is dose-dependent; even a short supraphysiological concentration reduces the cell survival and activates the growth arrest and apoptotic signaling, whereas the physiological SOD3 levels support its growth and survival.	Hydrogen Peroxide	15-19	superoxide dismutase 3, extracellular	Mus musculus	68-72