The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry
Abstract
Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields diferric oxo/hydroxo complexes at ferroxidase sites in maxi-ferritin subunits (24 subunits, 480 kDa; plants, animals, microorganisms). Oxidation occurs at the cavity surface of mini-ferritins/Dps proteins (12 subunits, 240 kDa; bacteria). Oxidation products are concentrated as minerals in the nanocavity for iron-protein cofactor synthesis (maxi-ferritins) or DNA protection (mini-ferritins). The protein cage and nanocavity characterize all ferritins, although amino acid sequences diverge, especially in bacteria. Catalytic oxidation/di-iron coupling in the protein cage (maxi-ferritins, 480 kDa; plants, bacteria and animal cell-specific isoforms) or on the cavity surface (mini-ferritins/Dps proteins, 280 kDa; bacteria) initiates mineralization. Gated pores (eight or four), symmetrically arranged, control iron flow. The multiple ferritin functions combine pore, channel, and catalytic functions in compact protein structures required for life and disease response.
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Cites
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702
Regulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173
Mineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M. A., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., et al. (1991) · Nature · doi:10.1038/349541a0 · Cited by 777
I RON S TATUS AND N EURAL F UNCTIONING
Beard, J. L., & Connor, J. R. (2003) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.020102.075739 · Cited by 669
Curtis, A. R. J., Fey, C., Morris, C. M., Bindoff, L. A., Ince, P. G., Chinnery, P. F., Coulthard, A., Jackson, M. J., Jackson, A. P., McHale, D. P., et al. (2001) · Nature Genetics · doi:10.1038/ng571 · Cited by 537
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Biasiotto, G., & Arosio, P. (2004) · Blood · doi:10.1182/blood-2003-06-1842 · Cited by 132
Langlois d'Estaintot, B., Santambrogio, P., Granier, T., Gallois, B., Chevalier, J. M., Précigoux, G., Levi, S., & Arosio, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.036 · Cited by 113
Cited by
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659
Kell, D. B., & Pretorius, E. (2014) · Metallomics · doi:10.1039/c3mt00347g · Cited by 667
Jasniewski, A. J., & Que, L. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00457 · Cited by 474
Ferritin: A Versatile Building Block for Bionanotechnology
Jutz, G., van Rijn, P., Santos Miranda, B., & Böker, A. (2015) · Chemical Reviews · doi:10.1021/cr400011b · Cited by 408
Natural supramolecular protein assemblies
Pieters, B. J. G. E., van Eldijk, M. B., Nolte, R. J. M., & Mecinović, J. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00157a · Cited by 369
Metadata
- Authors
- Liu, X., & Theil, E. C.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-01-29
- Volume
- 38
- Issue
- 3
- Pages
- 167-175
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2106699885
- Cited by
- 514
- References
- 9
- FWCI
- 14.83
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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