| Name | ferritin (protein family or complex) |
|---|---|
| Synonyms | Ferritin; Ferritins |
| Name | diquat |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9244385 | Rikans LE, Ardinska V, Hornbrook KR: Age-associated increase in ferritin content of male rat liver: implication for diquat-mediated oxidative injury. Arch Biochem Biophys. 1997 Aug 1;344(1):85-93. The present study was conducted to determine whether quantitative or qualitative changes in hepatic ferritin occur as a consequence of aging and whether diquat-mediated oxidation is intensified by elevated ferritin concentrations. |
306(3,5,5,6) | Details |
| 3368924 | Reif DW, Beales IL, Thomas CE, Aust SD: Effect of diquat on the distribution of iron in rat liver. . Toxicol Appl Pharmacol. 1988 May;93(3):506-10. These results suggest that diquat toxicity may be associated with the release of iron from ferritin in vivo and that iron release from ferritin may be a process common to other free radical mediated toxicities. |
49(0,1,4,4) | Details |
| 2753390 | Monteiro HP, Vile GF, Winterbourn CC: Release of iron from ferritin by semiquinone, anthracycline, bipyridyl, and nitroaromatic radicals. Free Radic Biol Med. 1989;6(6):587-91. Ferritin iron was released by a number of bipyridyl radicals including those derived from diquat and paraquat, the anthracycline radicals of adriamycin, daunorubicin and epirubicin, the semiquinones of anthraquinone-2-sulphonate, 1,5 and 2,6-dihydroxyanthraquinone, 1-hydroxyanthraquinone, purpurin, and plumbagin, and the nitroaromatic radicals of nitrofurantoin and metronidazole. |
34(0,1,1,4) | Details |
| 3020022 | Thomas CE, Aust SD: Reductive release of iron from ferritin by cation free radicals of paraquat and other bipyridyls. J Biol Chem. 1986 Oct 5;261(28):13064-70. Similarly, the cation free radicals of the closely related chemicals, diquat and benzyl viologen, also promoted iron release. |
6(0,0,0,6) | Details |
| 10810445 | Clothier B, Robinson S, Akhtar RA, Francis JE, Peters TJ, Raja K, Smith AG: Genetic variation of basal iron status, ferritin and iron regulatory protein in mice: potential for modulation of oxidative stress. Biochem Pharmacol. 2000 Jan 15;59(2):115-22. SWR mice were more susceptible than C57BL/10ScSn mice to the toxic action of diquat, which is thought to involve iron catalysis. |
5(0,0,0,5) | Details |
| 16670937 | Abe T, Kinda T, Takano Y, Chikazawa S, Higuchi M, Kawasaki N, Orino K, Watanabe K: Relationship between body iron stores and diquat toxicity in male Fischer-344 rats. Biometals. 2006 Dec;19(6):651-7. Epub 2006 May 3. |
0(0,0,0,0) | Details |