PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23594119-1	2013	We have previously shown that human extracellular superoxide dismutase (EC-SOD) exists as two variants with differences in their disulfide bridge patterns: one form is the active enzyme (aEC-SOD), and the other is inactive (iEC-SOD).	Disulfides	129-138	superoxide dismutase 3	Homo sapiens	36-70	
23594119-1	2013	We have previously shown that human extracellular superoxide dismutase (EC-SOD) exists as two variants with differences in their disulfide bridge patterns: one form is the active enzyme (aEC-SOD), and the other is inactive (iEC-SOD).	Disulfides	129-138	superoxide dismutase 3	Homo sapiens	72-78	
18385137-2	2008	Two different folding variants of EC-SOD exist based on the disulfide bridge connectivity, resulting in enzymatically active (aEC-SOD) and inactive (iEC-SOD) subunits.	Disulfides	60-69	superoxide dismutase 3	Homo sapiens	34-40	
23329142-0	2013	Cu/Zn incorporation during purification of soluble human EC-SOD from E. coli stabilizes proper disulfide bond formation.	Disulfides	95-104	superoxide dismutase 3	Homo sapiens	57-63	
23329142-9	2013	Therefore, the enzymatic activity of hEC-SOD is associated with metal incorporation and protein folding via disulfide bond.	Disulfides	108-117	superoxide dismutase 3	Homo sapiens	37-44	
22062630-4	2012	We have determined the redox potential of this disulfide bridge and show that both EC-SOD dimers and EC-SOD monomers are present within the intracellular space.	Disulfides	47-56	superoxide dismutase 3	Homo sapiens	83-89	
22062630-4	2012	We have determined the redox potential of this disulfide bridge and show that both EC-SOD dimers and EC-SOD monomers are present within the intracellular space.	Disulfides	47-56	superoxide dismutase 3	Homo sapiens	101-107	
18385137-9	2008	This study shows that generation of the EC-SOD folding variants is an intracellular event that depends on a free cysteine residue not involved in disulfide bonding.	Disulfides	146-155	superoxide dismutase 3	Homo sapiens	40-46	
17937792-2	2007	We have previously shown that the EC-SOD subunit exists in two distinct folding variants based on differences in the disulfide bridge pattern (Petersen SV, Oury TD, Valnickova Z, Thogersen IB, Hojrup P, Crapo JD, Enghild JJ.	Disulfides	117-126	superoxide dismutase 3	Homo sapiens	34-40	
17937792-6	2007	The EC-SOD subunits are associated into covalently linked dimers through an inter-subunit disulfide bridge creating the theoretical possibility of 3 dimers (aa, ai or ii) with different antioxidant potentials.	Disulfides	90-99	superoxide dismutase 3	Homo sapiens	4-10	
17937792-7	2007	We have analyzed the quaternary structure of the endogenous EC-SOD disulfide-linked dimer to investigate if these dimers in fact exist.	Disulfides	67-76	superoxide dismutase 3	Homo sapiens	60-66	
14615576-3	2003	Cu/Zn-SOD is a homodimer containing four cysteine residues within each subunit, and EC-SOD is a tetramer composed of two disulfide-bonded dimers in which each subunit contains six cysteines.	Disulfides	121-130	superoxide dismutase 3	Homo sapiens	84-90	
14615576-7	2003	The results show that human EC-SOD exists in two forms, each with a unique disulfide bridge pattern.	Disulfides	75-84	superoxide dismutase 3	Homo sapiens	28-34	
14615576-8	2003	One form (active EC-SOD) is enzymatically active and contains a disulfide bridge pattern similar to Cu/Zn-SOD.	Disulfides	64-73	superoxide dismutase 3	Homo sapiens	17-23	
14615576-9	2003	The other form (inactive EC-SOD) has a different disulfide bridge pattern and is enzymatically inactive.	Disulfides	49-58	superoxide dismutase 3	Homo sapiens	25-31	
14567441-0	2003	An inter-subunit disulfide bond affects affinity of human lung extracellular superoxide dismutase to heparin.	Disulfides	17-26	superoxide dismutase 3	Homo sapiens	63-97	
14567441-4	2003	Western blot analysis of the heparin affinity chromatography product indicated that the presence of the inter-subunit disulfide bond affects the affinity of EC-SOD for heparin.	Disulfides	118-127	superoxide dismutase 3	Homo sapiens	157-163	
14567441-6	2003	The present study suggests that, not only the processing of the C-terminal region but inter-subunit disulfide bonds also play a role in determining the tissue distribution of EC-SOD.	Disulfides	100-109	superoxide dismutase 3	Homo sapiens	175-181	
15862712-0	2005	Extracellular superoxide dismutase: structural and functional considerations of a protein shaped by two different disulfide bridge patterns.	Disulfides	114-123	superoxide dismutase 3	Homo sapiens	0-34	
15518578-2	2004	Human EC-SOD contains an additional cysteine residue and folds into two forms with distinct disulfide bridge patterns.	Disulfides	92-101	superoxide dismutase 3	Homo sapiens	6-12