| Name | ferritin (protein family or complex) |
|---|---|
| Synonyms | Ferritin; Ferritins |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19699718 | Kaur D, Rajagopalan S, Andersen JK: Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease. Brain Res. 2009 Nov 10;1297:17-22. Epub 2009 Aug 21. This has been speculated to be due to subsequent reductions in the labile iron pool (LIP) needed for the synthesis of iron-sulfur-containing enzymes. |
6(0,0,0,6) | Details |
| 19781920 | Fukuta M, Yamashita I: Adsorption behavior of ferritin and buffer components, buffer agents and salts, onto silane-coupled substrate. Colloids Surf B Biointerfaces. 2010 Jan 1;75(1):323-9. Epub 2009 Sep 11. |
2(0,0,0,2) | Details |
| 19453295 | Metzendorf C, Wu W, Lind MI: Overexpression of Drosophila mitoferrin in l (2) mbn cells results in dysregulation of Fer1HCH expression. Biochem J. 2009 Jul 15;421(3):463-71. Compared with control cell lines, mbn-dmfrn cells had higher Fer1HCH (ferritin 1 heavy chain homologue) transcript and protein levels. |
1(0,0,0,1) | Details |
| 19997898 | Richardson DR, Huang ML, Whitnall M, Becker EM, Ponka P, Rahmanto YS: The ins and outs of mitochondrial iron-loading: the metabolic defect in Friedreich's ataxia. J Mol Med. 2010 Apr;88(4):323-9. Epub 2009 Dec 9. There is also marked downregulation of ferritin that is required for iron storage and decreased expression of the iron exporter, ferroportin 1, leading to decreased cellular iron efflux. This stimulation of iron uptake probably attempts to rescue the deficit in mitochondrial iron metabolism that is due to downregulation of mitochondrial iron utilization, namely, heme and iron-sulfur cluster (ISC) synthesis and also iron storage (mitochondrial ferritin). |
1(0,0,0,1) | Details |
| 19805308 | Huang ML, Becker EM, Whitnall M, Rahmanto YS, Ponka P, Richardson DR: Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16381-6. Epub 2009 Sep 4. Using cardiac tissues, we demonstrate that frataxin deficiency leads to down-regulation of key molecules involved in 3 mitochondrial utilization pathways: iron-sulfur cluster (ISC) synthesis (iron-sulfur cluster scaffold protein1/2 and the desulferase Nfs1), mitochondrial iron storage (mitochondrial ferritin), and heme synthesis dehydratase, coproporphyrinogen oxidase, hydroxymethylbilane synthase, uroporphyrinogen III synthase, and ferrochelatase). This effect is compounded by increased iron availability for mitochondrial uptake through (i) transferrin receptor1 up-regulation, increasing iron uptake from transferrin; (ii) decreased ferroportin1 expression, limiting iron export; (iii) increased expression of the heme catabolism enzyme heme oxygenase1 and down-regulation of ferritin-H and -L, both likely leading to increased "free iron" for mitochondrial uptake; and (iv) increased expression of the mammalian exocyst protein Sec15l1 and the mitochondrial iron importer mitoferrin-2 (Mfrn2), which facilitate cellular iron uptake and mitochondrial iron influx, respectively. |
1(0,0,0,1) | Details |
| 19283345 | Pandolfo M, Pastore A: The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J Neurol. 2009 Mar;256 Suppl 1:9-17. Frataxins are small essential proteins whose deficiency causes a range of metabolic disturbances, which include oxidative stress, deficit of iron- clusters, and defects in heme synthesis, sulfur amino acid and energy metabolism, stress response, and mitochondrial function. It has been suggested that frataxin function is that of a ferritin-like protein, an iron chaperone of the iron cluster machinery and heme metabolism and/or a controller of cellular oxidative stress. |
1(0,0,0,1) | Details |
| 20355572 | Kim JW, Posey AE, Watt GD, Choi SH, Lillehei PT: Gold nanoshell assembly on a ferritin protein employed as a bio-template. J Nanosci Nanotechnol. 2010 Mar;10(3):1771-7. The process was facilitated by the energetically favorable gold-sulfur bonds formed at the residues lining these channels. |
3(0,0,0,3) | Details |