PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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