node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ALOX5 | GPX7 | ENSP00000363512 | ENSP00000354677 | Arachidonate 5-lipoxygenase; Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes; Belongs to the lipoxygenase family | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | 0.909 |
ERO1L | GPX7 | ENSP00000379042 | ENSP00000354677 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | 0.947 |
ERO1L | GSR | ENSP00000379042 | ENSP00000221130 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | 0.419 |
ERO1L | P4HB | ENSP00000379042 | ENSP00000327801 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.984 |
GPX7 | ALOX5 | ENSP00000354677 | ENSP00000363512 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Arachidonate 5-lipoxygenase; Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes; Belongs to the lipoxygenase family | 0.909 |
GPX7 | ERO1L | ENSP00000354677 | ENSP00000379042 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] | 0.947 |
GPX7 | GSR | ENSP00000354677 | ENSP00000221130 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | 0.983 |
GPX7 | GSS | ENSP00000354677 | ENSP00000216951 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Glutathione synthetase; Belongs to the eukaryotic GSH synthase family | 0.944 |
GPX7 | GSTA4 | ENSP00000354677 | ENSP00000360002 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Glutathione S-transferase A4; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE); Soluble glutathione S-transferases | 0.892 |
GPX7 | GSTM3 | ENSP00000354677 | ENSP00000256594 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Glutathione S-transferase Mu 3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers; Belongs to the GST superfamily. Mu family | 0.894 |
GPX7 | P4HB | ENSP00000354677 | ENSP00000327801 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.964 |
GPX7 | SOD1 | ENSP00000354677 | ENSP00000270142 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems | 0.976 |
GPX7 | SOD2 | ENSP00000354677 | ENSP00000446252 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Superoxide dismutase [Mn], mitochondrial; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems | 0.977 |
GPX7 | SOD3 | ENSP00000354677 | ENSP00000371554 | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | Extracellular superoxide dismutase [Cu-Zn]; Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen | 0.962 |
GSR | ERO1L | ENSP00000221130 | ENSP00000379042 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] | 0.419 |
GSR | GPX7 | ENSP00000221130 | ENSP00000354677 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family | 0.983 |
GSR | GSS | ENSP00000221130 | ENSP00000216951 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | Glutathione synthetase; Belongs to the eukaryotic GSH synthase family | 0.985 |
GSR | GSTA4 | ENSP00000221130 | ENSP00000360002 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | Glutathione S-transferase A4; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE); Soluble glutathione S-transferases | 0.864 |
GSR | GSTM3 | ENSP00000221130 | ENSP00000256594 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | Glutathione S-transferase Mu 3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers; Belongs to the GST superfamily. Mu family | 0.858 |
GSR | P4HB | ENSP00000221130 | ENSP00000327801 | Glutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.711 |