PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28791960-9 2017 Copper-dependent enzymes such as ceruloplasmin, superoxide dismutase SOD1 and SOD3, group of metallothionein and cytochrome c oxidase are present at all stages of gametogenesis as well as in the somatic cells of the testis and in the somatic cells of epididymis. Copper 0-6 superoxide dismutase 3 Homo sapiens 78-82 29168020-0 2018 Copper chaperone antioxidant-1, Atox-1, is involved in the induction of SOD3 in THP-1 cells. Copper 0-6 superoxide dismutase 3 Homo sapiens 72-76 29168020-1 2018 Superoxide dismutase (SOD) 3, a copper (Cu)-containing anti-oxidative enzyme, plays a key role in extracellular redox homeostasis. Copper 32-38 superoxide dismutase 3 Homo sapiens 0-28 29168020-1 2018 Superoxide dismutase (SOD) 3, a copper (Cu)-containing anti-oxidative enzyme, plays a key role in extracellular redox homeostasis. Copper 40-42 superoxide dismutase 3 Homo sapiens 0-28 29168020-2 2018 Cu chaperone antioxidant-1 (Atox-1) not only delivers Cu ions to SOD3 at the trans-Golgi network, it also functions as a transcription factor of SOD3; however, the role of Atox-1 in the regulation of SOD3 during the monocytic differentiation of THP-1 cells has not yet been elucidated. Copper 0-2 superoxide dismutase 3 Homo sapiens 65-69 29168020-2 2018 Cu chaperone antioxidant-1 (Atox-1) not only delivers Cu ions to SOD3 at the trans-Golgi network, it also functions as a transcription factor of SOD3; however, the role of Atox-1 in the regulation of SOD3 during the monocytic differentiation of THP-1 cells has not yet been elucidated. Copper 0-2 superoxide dismutase 3 Homo sapiens 145-149 29168020-2 2018 Cu chaperone antioxidant-1 (Atox-1) not only delivers Cu ions to SOD3 at the trans-Golgi network, it also functions as a transcription factor of SOD3; however, the role of Atox-1 in the regulation of SOD3 during the monocytic differentiation of THP-1 cells has not yet been elucidated. Copper 0-2 superoxide dismutase 3 Homo sapiens 145-149 8394057-8 1993 These spectral findings support the notion that the active sites of the SOD iso-enzymes are similar, but with a higher tetragonal symmetry of the copper ligands in EC-SOD. Copper 146-152 superoxide dismutase 3 Homo sapiens 72-75 8394057-8 1993 These spectral findings support the notion that the active sites of the SOD iso-enzymes are similar, but with a higher tetragonal symmetry of the copper ligands in EC-SOD. Copper 146-152 superoxide dismutase 3 Homo sapiens 164-170 31474628-2 2019 Superoxide dismutase 3 (SOD3) is a copper-containing secretory antioxidative enzyme that plays a critical role in redox homeostasis, particularly in extracellular spaces. Copper 35-41 superoxide dismutase 3 Homo sapiens 0-22 31474628-2 2019 Superoxide dismutase 3 (SOD3) is a copper-containing secretory antioxidative enzyme that plays a critical role in redox homeostasis, particularly in extracellular spaces. Copper 35-41 superoxide dismutase 3 Homo sapiens 24-28 28686842-1 2017 The entire enzyme catalytic mechanism including the electron and the proton transfers of the copper- and zinc-containing extracellular superoxide dismutase (SOD3) was investigated by using QM/MM method. Copper 93-99 superoxide dismutase 3 Homo sapiens 157-161 15761197-5 2005 Using recombinant human SOD3, we found that the specific activity of SOD3 directly correlates with its copper content (R2=0.99). Copper 103-109 superoxide dismutase 3 Homo sapiens 24-28 26356671-3 2015 Disulfiram (DSF), currently in clinical cancer trials is activated by copper chelation, being potentially capable of diminishing the copper dependent activation of MEK1/2 and SOD1/SOD3 and promoting reactive oxygen species (ROS) toxicity. Copper 70-76 superoxide dismutase 3 Homo sapiens 180-184 26356671-3 2015 Disulfiram (DSF), currently in clinical cancer trials is activated by copper chelation, being potentially capable of diminishing the copper dependent activation of MEK1/2 and SOD1/SOD3 and promoting reactive oxygen species (ROS) toxicity. Copper 133-139 superoxide dismutase 3 Homo sapiens 180-184 19289127-1 2009 Extracellular superoxide dismutase (SOD3) is a homotetrameric copper- and zinc-containing glycoprotein with affinity for heparin. Copper 62-68 superoxide dismutase 3 Homo sapiens 36-40 15855335-5 2005 Mean extracellular superoxide dismutase (EC-SOD) activity was elevated in diabetic subjects, and its activity correlated strongly with the interaction between [Cu]serum and HbA1c. Copper 160-162 superoxide dismutase 3 Homo sapiens 5-39 15855335-5 2005 Mean extracellular superoxide dismutase (EC-SOD) activity was elevated in diabetic subjects, and its activity correlated strongly with the interaction between [Cu]serum and HbA1c. Copper 160-162 superoxide dismutase 3 Homo sapiens 41-47 23329142-8 2013 When copper and zinc were incorporated into hEC-SOD before MBP tag cleavage, the enzymatic activity was higher than when the metal ions were bound to the purified protein after MBP tag cleavage. Copper 5-11 superoxide dismutase 3 Homo sapiens 44-51 24024135-6 2013 The major part of EC-SOD inhibited by the peroxidase reaction was not fragmented but found to encompass oxidations of histidine residues involved in the coordination of copper (His98 and His163). Copper 169-175 superoxide dismutase 3 Homo sapiens 18-24 15761197-5 2005 Using recombinant human SOD3, we found that the specific activity of SOD3 directly correlates with its copper content (R2=0.99). Copper 103-109 superoxide dismutase 3 Homo sapiens 69-73 15280800-3 2004 EC-SOD is a secretory, tetrameric glycoprotein containing copper and zinc, with a high affinity to certain glycosaminoglycans, such as heparin and heparan sulfate. Copper 58-64 superoxide dismutase 3 Homo sapiens 0-6 12126755-5 2002 SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. Copper 83-89 superoxide dismutase 3 Homo sapiens 0-4 12551935-2 2003 Copper chaperone for SOD1 (CCS) and extracellular Cu,Zn superoxide dismutase (SOD3) have some sequence identity with SOD1, particularly in the regions of metal binding, but play no significant role in mutant SOD1-induced disease. Copper 0-6 superoxide dismutase 3 Homo sapiens 78-82 12551935-2 2003 Copper chaperone for SOD1 (CCS) and extracellular Cu,Zn superoxide dismutase (SOD3) have some sequence identity with SOD1, particularly in the regions of metal binding, but play no significant role in mutant SOD1-induced disease. Copper 50-52 superoxide dismutase 3 Homo sapiens 78-82