The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Ferritin: design and formation of an iron-storage molecule
Abstract
Although essential for most forms of life, too much iron is harmful. To cope with these antagonistic phenomena an iron-storage molecule, ferritin, has evolved. The structure of horse spleen apoferritin, which has recently been refined, consists of 24 symmetrically related subunits forming a near-spherical hollow shell. In ferritin the central cavity is occupied by an iron core of ‘ferrihydrite’, a geologically ephem eral mineral found in hot or cold springs and in mine workings, or produced in the laboratory by heating solutions of ferric salts. Ferritin itself forms most readily from apoferritin, in the presence of dioxygen, from FeII, not FeIII . Access to its interior is through small intersubunit channels, and the protein influences both the rate of FeII-oxidation and the form of oxide produced.
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Citations
Cites
The Oxides and Hydroxides of Iron and Their Structural Inter-Relationships
Bernal, J. D. (1959) · Clay Minerals · doi:10.1180/claymin.1959.004.21.02 · Cited by 585
Mineralogical constitution of colloidal “hydrous ferric oxides”
Towe, K. M., & Bradley, W. F. (1967) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(67)90266-4 · Cited by 443
Ferritin: structure, biosynthesis, and role in iron metabolism.
Munro, H. N., & Linder, M. C. (1978) · Physiological Reviews · doi:10.1152/physrev.1978.58.2.317 · Cited by 396
Regulation of synthesis and turnover of ferritin in rat liver
Drysdale, J. W., & Munro, H. N. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99877-7 · Cited by 326
Electron density map of apoferritin at 2.8-Å resolution
BANYARD, S. H., STAMMERS, D. K., & HARRISON, P. M. (1978) · Nature · doi:10.1038/271282a0 · Cited by 261
Self-citationThe formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake
Macara, I. G., Hoy, T. G., & Harrison, P. M. (1972) · Biochemical Journal · doi:10.1042/bj1260151 · Cited by 243
Self-citationTowe, K. M., & Lowenstam, H. A. (1967) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(67)80015-7 · Cited by 224
Ferric Oxyhydroxide Core of Ferritin
HARRISON, P. M., FISCHBACH, F. A., HOY, T. G., & HAGGIS, G. H. (1967) · Nature · doi:10.1038/2161188a0 · Cited by 205
Self-citationMechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogs
Jones, T., Spencer, R., & Walsh, C. (1978) · Biochemistry · doi:10.1021/bi00612a021 · Cited by 198
Surface structures of gibbsite goethite and phosphated goethite
RUSSELL, J. D., PARFITT, R. L., FRASER, A. R., & FARMER, V. C. (1974) · Nature · doi:10.1038/248220a0 · Cited by 197
Cited by
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Self-citationMolecular recognition in biomineralization
Mann, S. (1988) · Nature · doi:10.1038/332119a0 · Cited by 960
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
Self-citationCRICHTON, R. R., & CHARLOTEAUX‐WAUTERS, M. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11155.x · Cited by 686
Binding and uptake of H-ferritin are mediated by human transferrin receptor-1
Li, L., Fang, C. J., Ryan, J. C., Niemi, E. C., Lebrón, J. A., Björkman, P. J., Arase, H., Torti, F. M., Torti, S. V., Nakamura, M. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913192107 · Cited by 561
Metadata
- Authors
- Ford, G. C., Harrison, P. M., Rice, D. W., Smith, J. M. A., Treffry, A., White, J. L., & Yariv, J.
- Venue
- Philosophical Transactions of the Royal Society of London. B, Biological Sciences
- Publisher
- The Royal Society
- Published
- 1984-02-13
- Volume
- 304
- Issue
- 1121
- Pages
- 551-565
- ISSN
- 0080-4622 (ISSN-L)
- 2054-0280
- OpenAlex
- W2156605690
- Cited by
- 566
- References
- 40
- FWCI
- 14.52
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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