We are analyzing https://link.springer.com/article/10.1007/s00018-005-5285-y.

Title:
Cellular regulation and molecular interactions of the ferritins | Cellular and Molecular Life Sciences
Description:
Controlling iron/oxygen chemistry in biology depends on multiple genes, regulatory messenger RNA (mRNA) structures, signaling pathways and protein catalysts. Ferritin, a protein nanocage around an iron/oxy mineral, centralizes the control. Complementary DNA (antioxidant responsive element/Maf recognition element) and mRNA (iron responsive element) responses regulate ferritin synthesis rates. Multiple iron-protein interactions control iron and oxygen substrate movement through the protein cage, from dynamic gated pores to catalytic sites related to di-iron oxygenase cofactor sites. Maxi-ferritins concentrate iron for the bio-synthesis of iron/heme proteins, trapping oxygen; bacterial mini-ferritins, DNA protection during starvation proteins, reverse the substrate roles, destroying oxidants, trapping iron and protecting DNA. Ferritin is nature’s unique and conserved approach to controlled, safe use of iron and oxygen, with protein synthesis in animals adjusted by dual, genetic DNA and mRNA sequences that selectively respond to iron or oxidant signals and link ferritin to proteins of iron, oxygen and antioxidant metabolism.
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Topics {✒️}

controlling iron/oxygen chemistry regulatory messenger rna maxi-ferritins concentrate iron month download article/chapter iron responsive element iron/heme proteins cellular regulation privacy choices/manage cookies cellular iron homeostasis catalytic sites related iron/oxy mineral full article pdf author correspondence european economic area ferritins review published scope submit manuscript dynamic gated pores bacterial mini-ferritins conditions privacy policy oxygen substrate movement related subjects regulation accepting optional cookies protein synthesis main content log journal finder publish complementary dna dna protection protecting dna genetic dna protein catalysts protein nanocage protein cage article cellular molecular interactions starvation proteins check access furnishing proteins instant access trapping iron multiple genes link ferritin antioxidant metabolism nutritional sciences life sci privacy policy personal data information books a article number 591

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         description:Controlling iron/oxygen chemistry in biology depends on multiple genes, regulatory messenger RNA (mRNA) structures, signaling pathways and protein catalysts. Ferritin, a protein nanocage around an iron/oxy mineral, centralizes the control. Complementary DNA (antioxidant responsive element/Maf recognition element) and mRNA (iron responsive element) responses regulate ferritin synthesis rates. Multiple iron-protein interactions control iron and oxygen substrate movement through the protein cage, from dynamic gated pores to catalytic sites related to di-iron oxygenase cofactor sites. Maxi-ferritins concentrate iron for the bio-synthesis of iron/heme proteins, trapping oxygen; bacterial mini-ferritins, DNA protection during starvation proteins, reverse the substrate roles, destroying oxidants, trapping iron and protecting DNA. Ferritin is nature’s unique and conserved approach to controlled, safe use of iron and oxygen, with protein synthesis in animals adjusted by dual, genetic DNA and mRNA sequences that selectively respond to iron or oxidant signals and link ferritin to proteins of iron, oxygen and antioxidant metabolism.
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