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词条 Mitochondrial ferritin
释义

  1. Structure

  2. References

  3. Further reading

{{Infobox_gene}}Mitochondrial ferritin is a ferroxidase enzyme that in humans is encoded by the FTMT gene.[1]

It is classified as a metal-binding protein which is located within the mitochondria. After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin shells.

Structure

Its structure was determined at 1.70 Å through the use of X-ray diffraction and contains 182 residues. It is 67% helical. The Ramachandran plot shows that the structure of mitochondrial ferritin is mainly alpha helical with a low prevalence of beta sheets.

References

1. ^{{cite journal |vauthors=Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J | title = A human mitochondrial ferritin encoded by an intronless gene | journal = J. Biol. Chem. | volume = 276 | issue = 27 | pages = 24437–40 |date=July 2001 | pmid = 11323407 | doi = 10.1074/jbc.C100141200 | url = | issn = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Langlois d'Estaintot B, Santambrogio P, Granier T, etal |title=Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala. |journal=J. Mol. Biol. |volume=340 |issue= 2 |pages= 277–93 |year= 2004 |pmid= 15201052 |doi= 10.1016/j.jmb.2004.04.036 }}
  • {{cite journal |vauthors=Zanella I, Derosas M, Corrado M, etal |title=The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. |journal=Biochim. Biophys. Acta |volume=1782 |issue= 2 |pages= 90–8 |year= 2008 |pmid= 18160053 |doi= 10.1016/j.bbadis.2007.11.006 }}
  • {{cite journal |vauthors=Wilkinson J, Di X, Schönig K, etal |title=Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo. |journal=Biochem. J. |volume=395 |issue= 3 |pages= 501–7 |year= 2006 |pmid= 16448386 |pmc=1462685 |doi= 10.1042/BJ20060063 }}
  • {{cite journal |vauthors=Iwasaki K, Mackenzie EL, Hailemariam K, etal |title=Hemin-mediated regulation of an antioxidant-responsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells. |journal=Mol. Cell. Biol. |volume=26 |issue= 7 |pages= 2845–56 |year= 2006 |pmid= 16537925 |pmc=1430308 |doi= 10.1128/MCB.26.7.2845-2856.2006 }}
  • {{cite journal |vauthors=Hasan MR, Tosha T, Theil EC |title=Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation. |journal=J. Biol. Chem. |volume=283 |issue= 46 |pages= 31394–400 |year= 2008 |pmid= 18805796 |pmc=2581568 |doi= 10.1074/jbc.M806025200 }}
  • {{cite journal |vauthors=Cazzola M, Invernizzi R, Bergamaschi G, etal |title=Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. |journal=Blood |volume=101 |issue= 5 |pages= 1996–2000 |year= 2003 |pmid= 12406866 |doi= 10.1182/blood-2002-07-2006 }}
  • {{cite journal |vauthors=Faniello MC, Fregola A, Nisticò A, etal |title=Detection and functional analysis of an SNP in the promoter of the human ferritin H gene that modulates the gene expression. |journal=Gene |volume=377 |issue= |pages= 1–5 |year= 2006 |pmid= 16797877 |doi= 10.1016/j.gene.2006.02.034 }}
  • {{cite journal |vauthors=Iwasaki K, Hailemariam K, Tsuji Y |title=PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element. |journal=J. Biol. Chem. |volume=282 |issue= 31 |pages= 22335–43 |year= 2007 |pmid= 17565989 |pmc=2409283 |doi= 10.1074/jbc.M701477200 }}
  • {{cite journal |vauthors=MacKenzie EL, Tsuji Y |title=Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization. |journal=Biochem. J. |volume=411 |issue= 1 |pages= 107–13 |year= 2008 |pmid= 18076382 |pmc=2702759 |doi= 10.1042/BJ20071544 }}
  • {{cite journal |vauthors=Drysdale J, Arosio P, Invernizzi R, etal |title=Mitochondrial ferritin: a new player in iron metabolism. |journal=Blood Cells Mol. Dis. |volume=29 |issue= 3 |pages= 376–83 |year= 2002|pmid= 12547228 |doi=10.1006/bcmd.2002.0577 }}
  • {{cite journal |vauthors=Fisher J, Devraj K, Ingram J, etal |title=Ferritin: a novel mechanism for delivery of iron to the brain and other organs. |journal=Am. J. Physiol., Cell Physiol. |volume=293 |issue= 2 |pages= C641–9 |year= 2007 |pmid= 17459943 |doi= 10.1152/ajpcell.00599.2006 }}
  • {{cite journal |vauthors=Campanella A, Rovelli E, Santambrogio P, etal |title=Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia. |journal=Hum. Mol. Genet. |volume=18 |issue= 1 |pages= 1–11 |year= 2009 |pmid= 18815198 |doi= 10.1093/hmg/ddn308 |pmc=3298861}}
  • {{cite journal |vauthors=Bou-Abdallah F, Biasiotto G, Arosio P, Chasteen ND |title=The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core. |journal=Biochemistry |volume=43 |issue= 14 |pages= 4332–7 |year= 2004 |pmid= 15065877 |doi= 10.1021/bi0498813 }}
  • {{cite journal |vauthors=Binning RC, Bacelo DE |title=Computational modeling of the dizinc-ferroxidase complex of human H ferritin: direct comparison of the density functional theory calculated and experimental structures. |journal=J. Biol. Inorg. Chem. |volume=14 |issue= 8 |pages= 1199–208 |year= 2009 |pmid= 19585161 |doi= 10.1007/s00775-009-0563-z }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |pmc=528928 |doi= 10.1101/gr.2596504 }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932 |pmc=139241 |doi= 10.1073/pnas.242603899 }}
  • {{cite journal |vauthors=MacKenzie EL, Ray PD, Tsuji Y |title=Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress. |journal=Free Radic. Biol. Med. |volume=44 |issue= 9 |pages= 1762–71 |year= 2008 |pmid= 18325346 |pmc=2682214 |doi= 10.1016/j.freeradbiomed.2008.01.031 }}
  • {{cite journal |vauthors=Bou-Abdallah F, Santambrogio P, Levi S, etal |title=Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with Human H-chain ferritin. |journal=J. Mol. Biol. |volume=347 |issue= 3 |pages= 543–54 |year= 2005 |pmid= 15755449 |doi= 10.1016/j.jmb.2005.01.007 }}
  • {{cite journal |vauthors=Faniello MC, Di Sanzo M, Quaresima B, etal |title=p53-mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y. |journal=Int. J. Biochem. Cell Biol. |volume=40 |issue= 10 |pages= 2110–9 |year= 2008 |pmid= 18372207 |doi= 10.1016/j.biocel.2008.02.010 }}
  • {{cite journal |vauthors=Snyder AM, Wang X, Patton SM, etal |title=Mitochondrial ferritin in the substantia nigra in restless legs syndrome. |journal=J. Neuropathol. Exp. Neurol. |volume=68 |issue= 11 |pages= 1193–9 |year= 2009 |pmid= 19816198 |pmc=3024883 |doi= 10.1097/NEN.0b013e3181bdc44f }}
{{refend}}{{Other oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{DEFAULTSORT:Mitochondrial Ferritin}}{{gene-5-stub}}

3 : EC 1.16.3|Storage proteins|Mitochondria
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