| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Jian-Hong Zhu, Xin Gen Le. Double null of selenium-glutathione peroxidase-1 and copper, zinc-superoxide dismutase enhances resistance of mouse primary hepatocytes to acetaminophen toxicity. Experimental biology and medicine (Maywood, N.J.). vol 231. issue 5. 2006-06-09. PMID:16636302. |
this study was conducted to determine the impact of knockout of selenium (se)-dependent glutathione peroxidase-1 (gpx1-/-) or double knockout of gpx1 and copper, zinc (cu,zn)-super-oxide dismutase (sod1) on cell death induced by acetaminophen (apap) and its major toxic metabolite n-acetyl-p-benzoquinoneimine (napqi). |
2006-06-09 |
2023-08-12 |
mouse |
| Shinsuke Kato, Yusuke Saeki, Masashi Aoki, Makiko Nagai, Aya Ishigaki, Yasuto Itoyama, Masako Kato, Kohtaro Asayama, Akira Awaya, Asao Hirano, Eisaku Oham. Histological evidence of redox system breakdown caused by superoxide dismutase 1 (SOD1) aggregation is common to SOD1-mutated motor neurons in humans and animal models. Acta neuropathologica. vol 107. issue 2. 2004-04-05. PMID:14648077. |
to clarify the biological significance of the interaction of the redox system (prx2/gpx1) with sod1 in sod1-mutated motor neurons in vivo, we produced an affinity-purified rabbit antibody against prx2 and investigated the immunohistochemical localization of prx2 and gpx1 in neuronal lewy body-like hyaline inclusions (lbhis) in the spinal cords of familial amyotrophic lateral sclerosis (fals) patients with a two-base pair deletion at codon 126 and an ala-->val substitution at codon 4 in the sod1 gene, as well as in transgenic rats expressing human sod1 with h46r and g93a mutations. |
2004-04-05 |
2023-08-12 |
human |
| J B de Haan, F Cristiano, R Iannello, C Bladier, M J Kelner, I Kol. Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Human molecular genetics. vol 5. issue 2. 1996-12-05. PMID:8824885. |
in this study we investigate the effects of a perturbation in the ratio of cu/zn-superoxide dismutase activity (sod1 dismutases .o2-to h2o2) to glutathione peroxidase activity (gpx1 catalyses h2o2 conversion to h2o) on cell growth and development. |
1996-12-05 |
2023-08-12 |
Not clear |
| J B de Haan, F Cristiano, R Iannello, C Bladier, M J Kelner, I Kol. Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Human molecular genetics. vol 5. issue 2. 1996-12-05. PMID:8824885. |
furthermore, fibroblasts established from individuals with down syndrome have an increase in the ratio of sod1 to gpx1 activity compared with corresponding controls and senesce earlier. |
1996-12-05 |
2023-08-12 |
Not clear |
| J B de Haan, F Cristiano, R Iannello, C Bladier, M J Kelner, I Kol. Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Human molecular genetics. vol 5. issue 2. 1996-12-05. PMID:8824885. |
we also show that cip1 mrna levels are elevated in down syndrome cells, sod1 transfectants with an altered sod1 to gpx1 activity ratio and those treated with h2o2, thus suggesting that the slow proliferation may be mediated by cip1. |
1996-12-05 |
2023-08-12 |
Not clear |
| J B de Haan, F Cristiano, R C Iannello, I Kol. Cu/Zn-superoxide dismutase and glutathione peroxidase during aging. Biochemistry and molecular biology international. vol 35. issue 6. 1996-01-11. PMID:7492966. |
we also examine the sod1 to gpx1 ratio in down syndrome tissue and show that all organs have an altered ratio. |
1996-01-11 |
2023-08-12 |
mouse |