PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15777089-6	2005	On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions.	carbonate anion radical	101-124	superoxide dismutase 1	Homo sapiens	85-89	
22569304-5	2012	Our results demonstrate that peroxymonocarbonate oxidizes SOD1-Cu(I) to SOD1-Cu(II) and is in turn reduced to the carbonate anion radical.	carbonate anion radical	114-137	superoxide dismutase 1	Homo sapiens	58-62	
22569304-5	2012	Our results demonstrate that peroxymonocarbonate oxidizes SOD1-Cu(I) to SOD1-Cu(II) and is in turn reduced to the carbonate anion radical.	carbonate anion radical	114-137	superoxide dismutase 1	Homo sapiens	72-76	
15544920-2	2004	The carbonate anion radical (CO(3)(-))-induced oxidation of Trp-32 to kynurenine-type oxidation products was proposed to cause the aggregation of hSOD1.	carbonate anion radical	4-27	superoxide dismutase 1	Homo sapiens	146-151