| + |
NOX4 | up-regulates quantity 
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264724 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOX5 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264725 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCB3 | up-regulates quantity 
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255014 |
|
|
|
|
| pmid |
sentence |
| 23994464 |
The PI3Kγ pathway (but not PLCβ2/3) is required for chemotaxis of the cells while both pathways are required for GPCR-induced superoxide release |
|
| Publications: |
1 |
| + |
C5AR1 | up-regulates quantity by expression
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263469 |
|
|
|
|
| pmid |
sentence |
| 1847994 |
The C5a receptor mediates the pro-inflammatory and chemotactic actions of the complement anaphylatoxin C5a. In addition to stimulating chemotaxis, granule enzyme release and superoxide anion production, this receptor stimulates upregulation of expression and activity of the adhesion molecule MAC-1, and of CR1, and a decrease in cell-surface glycoprotein 100MEL-14 on neutrophils. |
|
| Publications: |
1 |
| Pathways: | Complement Signaling |
| + |
superoxide | up-regulates
|
ROS |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272277 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35681445 |
The ROS, including superoxide anion, hydrogen peroxide, and nitric oxide, play both beneficial and detrimental roles depending upon their levels and cellular microenvironment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
superoxide | up-regulates
|
Oxidative_stress |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272276 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD3 | down-regulates quantity 
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272271 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
superoxide | up-regulates activity
precursor of
|
SOD3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272274 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUOX1 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264726 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MPO-ANCA | up-regulates
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270589 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15972951 |
Anti-MPO IgG (250 μg/ml) induces significant superoxide anion production in TNF-α-primed peritoneal exudate cells from WT C57BL/6 mice (black bars) as compared to normal mouse IgG (250 μg/ml) or buffer alone. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Blood Serum |
| + |
superoxide | up-regulates activity
precursor of
|
SOD1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272288 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOX3 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264722 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD2 | down-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272281 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CYBB | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264723 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUOX2 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264727 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
C5AR2 | up-regulates quantity by expression
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263470 |
|
|
|
|
| pmid |
sentence |
| 1847994 |
The C5a receptor mediates the pro-inflammatory and chemotactic actions of the complement anaphylatoxin C5a. In addition to stimulating chemotaxis, granule enzyme release and superoxide anion production, this receptor stimulates upregulation of expression and activity of the adhesion molecule MAC-1, and of CR1, and a decrease in cell-surface glycoprotein 100MEL-14 on neutrophils. |
|
| Publications: |
1 |
| + |
SOD1 | down-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOX1 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCB2 | up-regulates quantity
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255013 |
|
|
|
|
| pmid |
sentence |
| 23994464 |
The PI3Kγ pathway (but not PLCβ2/3) is required for chemotaxis of the cells while both pathways are required for GPCR-induced superoxide release |
|
| Publications: |
1 |
| + |
PI3K | up-regulates quantity
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255011 |
|
|
|
|
| pmid |
sentence |
| 23994464 |
The PI3Kγ pathway (but not PLCβ2/3) is required for chemotaxis of the cells while both pathways are required for GPCR-induced superoxide release |
|
| Publications: |
1 |
| + |
superoxide | up-regulates activity
precursor of
|
SOD2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272284 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
superoxide