ArticleInorganica chimica acta2008
GATED PORES IN THE FERRITIN PROTEIN NANOCAGE.
Article in Inorganica chimica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 79 citations in OpenAlex.
- Structural Flexibility and Disassembly Kinetics of Single Ferritin Molecules Using Optical Nanotweezers.ACS nano · 2024Article
- Optical Monitoring ofNano letters · 2023Article
- Hyperthermostable recombinant human heteropolymer ferritin derived from a novel plasmid design.Protein science : a publication of the Protein Society · 2023Article
- Alteration of Iron Concentration in Alzheimer's Disease as a Possible Diagnostic Biomarker Unveiling Ferroptosis.International journal of molecular sciences · 2021Review
- Cryo-EM structures and functional characterization of homo- and heteropolymers of human ferritin variants.Scientific reports · 2020Article
- Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine.Nanomaterials (Basel, Switzerland) · 2020Review
- Bright Ferritin-a Reporter Gene Platform for On-Demand, Longitudinal Cell Tracking on MRI.iScience · 2020Article
- Mutant L-chain ferritins that cause neuroferritinopathy alter ferritin functionality and iron permeability.Metallomics : integrated biometal science · 2019Article
- Large protein organelles form a new iron sequestration system with high storage capacity.eLife · 2019Article
- Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Effect of chaotropes on the kinetics of iron release from ferritin by flavin nucleotides.Biochimica et biophysica acta. General subjects · 2017Article
- Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities.Antioxidants & redox signaling · 2014Review
- Iron acquisition in Bacillus cereus: the roles of IlsA and bacillibactin in exogenous ferritin iron mobilization.PLoS pathogens · 2014Article
- The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties.The Journal of biological chemistry · 2013Article
- Mobilization of stored iron in mammals: a review.Nutrients · 2013Review
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- Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry.Current opinion in chemical biology · 2011Review
- Maxi- and mini-ferritins: minerals and protein nanocages.Progress in molecular and subcellular biology · 2011Article
- Serum ferritin: Past, present and future.Biochimica et biophysica acta · 2010Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Synopsis and pictogram: Gated pores in the ferritin family of protein nanocages, illustrated in the pictogram, control transfer of ferrous iron into and out of the cages by regulating contact between hydrated ferric oxide mineral inside the protein cage, and reductants such as FMNH(2) on the outside. The structural and functional homology between the gated ion channel proteins in inaccessible membranes and gated ferritin pores in the stable, water soluble nanoprotein, make studies of ferritin pores models for gated pores in many ion channel proteins.Properties of ferritin gated pores, which control rates of FMNH(2) reduction of ferric iron in hydrated oxide minerals inside the protein nanocage, are discussed in terms of the conserved pore gate residues (arginine 72-apspartate 122 and leucine 110-leucine 134), of pore sensitivity to heat at temperatures 30 °C below that of the nanocage itself, and of pore sensitivity to physiological changes in urea (1-10 mM). Conditions which alter ferritin pore structure/function in solution, coupled with the high evolutionary conservation of the pore gates, suggest the presence of molecular regulators in vivo that recognize the pore gates and hold them either closed or open, depending on biological iron need. The apparent homology between ferrous ion transport through gated pores in the ferritin nanocage and ion transport through gated pores in ion channel proteins embedded in cell membranes, make studies of water soluble ferritin and the pore gating folding/unfolding a useful model for other gated pores.
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Registered trials
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