The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Identification of the ferroxidase centre in ferritin
Abstract
Ferroxidase activity in human H‐chain ferritin has been studied with the aid of site‐directed mutagenesis. A site discovered by X‐ray crystallography has now been identified as the ferroxidase centre. This centre is present only in H‐chains and is located within the four‐helix bundle of the chain fold.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“It was demonstrated that Saccharomyces cerevisiae cells lacking the YFH1 gene, the yeast homologue of the human frataxin gene, showed low levels of cytochrome and ferrochelatase (181).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [181]
Citations
Cites
FERRITIN: STRUCTURE, GENE REGULATION, AND CELLULAR FUNCTION IN ANIMALS, PLANTS, AND MICROORGANISMS
Theil, E. C. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.001445 · Cited by 1,337
Ferritin: design and formation of an iron-storage molecule
Ford, G. C., Harrison, P. M., Rice, D. W., Smith, J. M., Treffry, A., WHITE, J. L., & Yariv, J. (1984) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1984.0046 · Cited by 567
Self-citationOn ferritin heterogeneity. Further evidence for heteropolymers.
Arosio, P., Adelman, T. G., & Drysdale, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34741-5 · Cited by 457
Self-citationLevi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A., & Arosio, P. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81326-1 · Cited by 378
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 242
Self-citationBryce, C. F. A., & Crichton, R. R. (1973) · Biochemical Journal · doi:10.1042/bj1330301 · Cited by 112
Iron binding by horse spleen apoferritin. A vanadyl(IV) EPR spin probe study.
Chasteen, N. D., & Theil, E. C. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34433-8 · Cited by 111
Iron incorporation into apoferritin. The role of apoferritin as a ferroxidase.
Bakker, G., & Boyer, R. F. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69288-9 · Cited by 104
The formation of ferritin from apoferritin. Catalytic action of apoferritin
Macara, I. G., Hoy, T. G., & Harrison, P. M. (1973) · Biochemical Journal · doi:10.1042/bj1350343 · Cited by 73
Self-citationSpectroscopic studies on the binding of Iron, Terbium, and Zinc by Apoferritin
Treffry, A., & Harrison, P. M. (1984) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(84)85035-7 · Cited by 69
Self-citation
Research works printed but not linked: 6
- Treffry A., 1989, FEBS Lett.
- Levi S., 1989, Biochemistry
- Wagstaff M., 1978, Biochem. J., 199, 567
- Levi S., 1989, Biochem. J.
- Lawson D.M., 1989, Inorganic Biochemistry Discussion Group, Christmas meeting
- Bauminger E.R., 1989, Biochemistry
Cited by
Sorted by citations
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-citationStructural and Functional Aspects of Metal Sites in Biology
Holm, R. H., Kennepohl, P., & Solomon, E. I. (1996) · Chemical Reviews · doi:10.1021/cr9500390 · Cited by 2,573
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
Molecular recognition in biomineralization
Mann, S. (1988) · Nature · doi:10.1038/332119a0 · Cited by 961
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
“4) (Lawson et al., 1989; Baum- ing parts of two subunits near a twofold axis.”
BackgroundSelf-citationSolving 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-citationThe molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
Richardson, D. R., & Ponka, P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(96)00014-7 · Cited by 714
Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 695
Magnetoferritin: in Vitro Synthesis of a Novel Magnetic Protein
Meldrum, F. C., Heywood, B. R., & Mann, S. (1992) · Science · doi:10.1126/science.1636086 · Cited by 572
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526
“The same group demonstrated the ferroxidase activity of yeast frataxin (233) [similar to that of ferritin H, which oxidizes Fe 2 (cid:2) to Fe 3 (cid:2) (178)].”
High‐field magnetic resonance imaging of brain iron: birth of a biomarker?
Schenck, J. F., & Zimmerman, E. A. (2004) · NMR in Biomedicine · doi:10.1002/nbm.922 · Cited by 335
“It is believed that cytoplasmic iron is presented to ferritin in the Fe2þ state and that it is oxidized to Fe3þ at a ferroxidase center within the ferritin molecule before mineralization as Fe3þ in ferrihydrite.(89) Note that spe-”
BackgroundBayır, H., Dixon, S. J., Tyurina, Y. Y., Kellum, J. A., & Kagan, V. E. (2023) · Nature Reviews Nephrology · doi:10.1038/s41581-023-00689-x · Cited by 355
Structure, function, and evolution of ferritins
Andrews, S. C., Harrison, P. M., Yewdall, S. J., Arosio, P., Levi, S., Bottke, W., DARL, M. V., Briat, J., Laulhère, J. P., & Lobréaux, S. (1992) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(92)84062-r · Cited by 336
Self-citationHempstead, P. D., Yewdall, S. J., Fernie, A. R., Lawson, D. M., Artymiuk, P. J., Rice, D. W., Ford, G. C., & Harrison, P. M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0970 · Cited by 321
Self-citationUnity in the Biochemistry of the Iron-Storage Proteins Ferritin and Bacterioferritin
Honarmand Ebrahimi, K., Hagedoorn, P.-L., & Hagen, W. R. (2015) · Chemical Reviews · doi:10.1021/cr5004908 · Cited by 297
Limitations of Serum Ferritin in Diagnosing Iron Deficiency in Inflammatory Conditions
Dignass, A. U., Farrag, K., & Stein, J. M. (2018) · International Journal of Chronic Diseases · doi:10.1155/2018/9394060 · Cited by 309
“The H chains of ferritin have ferroxidase activity and convert Fe(II) to Fe(III) as the iron is internalized within the ferritin complex [27].”
BackgroundPietsch, E. C., Chan, J. Y., Torti, F. M., & Torti, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210664200 · Cited by 284
Lopes, K. O., Sparks, D. L., & Streit, W. J. (2008) · Glia · doi:10.1002/glia.20678 · Cited by 262
“VC 2008 Wiley-Liss, Inc. oxidation and detoxification of ferrous ion (Fe21) to its less reactive form ferric ion (Fe31) while the L-subunit possesses glutamate residues in its interior that facilitate Fe31 mineralization for long-term storage (Chasteen and Harrison, 1999; Lawson et al., 1989).”
BackgroundNanophase Cobalt Oxyhydroxide Mineral Synthesized within the Protein Cage of Ferritin
Douglas, T., & Stark, V. T. (2000) · Inorganic Chemistry · doi:10.1021/ic991269q · Cited by 281
Nichol, H., Law, J. H., & Winzerling, J. J. (2002) · Annual Review of Entomology · doi:10.1146/annurev.ento.47.091201.145237 · Cited by 282
Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin
Levi, S., Yewdall, S. J., Harrison, P. M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1992) · Biochemical Journal · doi:10.1042/bj2880591 · Cited by 268
Self-citationThe Role of Iron in Oxygen-Mediated Toxicities
Ryan, T. P., & Aust, S. D. (1992) · Critical Reviews in Toxicology · doi:10.3109/10408449209146308 · Cited by 249
The significance of ferritin in cancer: Anti-oxidation, inflammation and tumorigenesis
Alkhateeb, A. A., & Connor, J. R. (2013) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.07.002 · Cited by 250
Ferritin: The Protein Nanocage and Iron Biomineral in Health and in Disease
Theil, E. C. (2013) · Inorganic Chemistry · doi:10.1021/ic400484n · Cited by 247
Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235
“The H-chain of ferritin contains 12 lysine residues and it is not clear which of the residues is ubiquitinated, or whether all of the residues are potential ubiquitination sites.”
Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., & Chiancone, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3259 · Cited by 216
Chiancone, E., & Ceci, P. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.01.013 · Cited by 213
Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Jacob, H. S., Eaton, J. W., & Balla, G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1787 · Cited by 215
“The ferroxidase activity of human H-chain ferritin has been widely studied by Arosio’s group with the aid of site-directed mutagenesis (73).”
Biomimetic Synthesis and Characterization of Magnetic Proteins (Magnetoferritin)
Wong, K. K. W., Douglas, T., Gider, S., Awschalom, D. D., & Mann, S. (1998) · Chemistry of Materials · doi:10.1021/cm970421o · Cited by 197
Wolbachia Interferes with Ferritin Expression and Iron Metabolism in Insects
Kremer, N., Voronin, D., Charif, D., Mavingui, P., Mollereau, B., & Vavre, F. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000630 · Cited by 202
“maintains all the ferroxidase residues of the ferritin HCH which are necessary for iron oxidation and iron absorption”
BackgroundReconstitution of manganese oxide cores in horse spleen and recombinant ferritins
Meldrum, F. C., Douglas, T., Levi, S., Arosio, P., & Mann, S. (1995) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(94)00037-b · Cited by 187
Self-citationBrain Iron Metabolism Dysfunction in Parkinson’s Disease
Jiang, H. F., Wang, J., Rogers, J. T., & Xie, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9879-1 · Cited by 188
“L-Ferritin is required for the long-term storage of iron [73], whereas H-ferritin has ferroxidase activity [74].”
BackgroundUltrastructure of ferritin and apoferritin: A review
Massover, W. H. (1993) · Micron · doi:10.1016/0968-4328(93)90005-l · Cited by 174
Thompson, K., Menzies, S. L., Muckenthaler, M. U., Torti, F. M., Wood, T. L., Torti, S. V., Hentze, M. W., Beard, J., & Connor, J. R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10463 · Cited by 171
Koorts, A. M., & Viljoen, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701318583 · Cited by 164
“Under cellular conditions where low Fe2þ concentrations relative to the amount of apoferritin may be expected, the ferroxidase activity of H-subunits is probably essential to initiate the formation of iron nuclei and for iron mineralization to proceed at a significant rate (Lawson et al., 1989).”
BackgroundInfluentialMcCarthy, R. C., & Kosman, D. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1771-4 · Cited by 163
“Evidence suggests that FHC, which contains a ferroxidase center, oxidizes Fe for FLC which, in turn, mineralizes and stores Fe [152, 153].”
Influence of site-directed modifications on the formation of iron cores in ferritin
Wade, V. J., Levi, S., Arosio, P., Treffry, A., Harrison, P. M., & Mann, S. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90944-2 · Cited by 157
Self-citationMössbauer spectroscopic investigation of structure-function relations in ferritins
Bauminger, E. R., Harrison, P. M., Hechel, D., Nowik, I., & Treffry, A. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90440-b · Cited by 154
Self-citationAlkhateeb, A. A., Han, B., & Connor, J. R. (2013) · Breast Cancer Research and Treatment · doi:10.1007/s10549-012-2405-x · Cited by 155
“H-subunit has ferroxidase activity [4], whereas the L-subunit contributes to the stable storage of iron in the ferritin”
BackgroundFerritin-based drug delivery systems: Hybrid nanocarriers for vascular immunotargeting
Khoshnejad, M., Parhiz, H., Shuvaev, V. V., Dmochowski, I. J., & Muzykantov, V. R. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.02.042 · Cited by 152
“The heavy chain has catalytic ferroxidase activity that oxidizes Fe(II) to Fe(III) which is insoluble and nucleates at the core [15,16].”
Coupling Heme and Iron Metabolism via Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151
“The ferroxidase activity of FTH is provided by a core of evolutionary conserved amino acids, that is, Glu-27, Glu-62, and His-65 (80, 103).”
Microglial degeneration in the aging brain - bad news for neurons?
Streit, W. (2008) · Frontiers in Bioscience · doi:10.2741/2937 · Cited by 150
Ferritins: furnishing proteins with iron
Bradley, J. M., Brun, N. E. L., & Moore, G. R. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1336-0 · Cited by 150
Ferritins as natural and artificial nanozymes for theranostics
Jiang, B., Fang, L., Wu, K., Yan, X., & Fan, K. (2019) · Theranostics · doi:10.7150/thno.39827 · Cited by 144
“It is reported that ferritin H-subunit lost its ferroxidase-like activity after mutation of two amino acid residues, E62K and H65G (using amino acids of L-subunits to replace H-subunits on 62 and 65) [30].”
BackgroundSantambrogio, P., Levi, S., Arosio, P., Palagi, L., Vecchio, G., Lawson, D. M., Yewdall, S. J., Artymiuk, P. J., Harrison, P. M., & Jappelli, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49681-6 · Cited by 143
Self-citationIron metabolism-new perspectives in view
Crichton, R. R., & Ward, R. J. (1992) · Biochemistry · doi:10.1021/bi00161a001 · Cited by 138
A Novel Plant Ferritin Subunit from Soybean That Is Related to a Mechanism in Iron Release
Masuda, T., Goto, F., & Yoshihara, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011399200 · Cited by 140
deMaré, F., Kurtz, D. M. J., & Nordlund, P. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0696-539 · Cited by 138
Reaction Paths of Iron Oxidation and Hydrolysis in Horse Spleen and Recombinant Human Ferritins
Yang, X., Chen-Barrett, Y., Arosio, P., & Chasteen, N. D. (1998) · Biochemistry · doi:10.1021/bi973128a · Cited by 137
Self-citationIron, the substantia nigra and related neurological disorders
Snyder, A. M., & Connor, J. R. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.08.005 · Cited by 138
Masuda, T., Goto, F., Yoshihara, T., & Mikami, B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059790 · Cited by 135
Santambrogio, P., Levi, S., Cozzi, A., Corsi, B., & Arosio, P. (1996) · Biochemical Journal · doi:10.1042/bj3140139 · Cited by 133
Self-citationLi, R., Luo, C., Mines, M. A., Zhang, J., & Fan, G.-H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607266200 · Cited by 129
Treffry, A., Bauminger, E. R., Hechel, D., Hodson, N. W., Nowik, I., Yewdall, S. J., & Harrison, P. M. (1993) · Biochemical Journal · doi:10.1042/bj2960721 · Cited by 129
Self-citationIron oxidation chemistry in ferritin. Increasing Fe/O2 stoichiometry during core formation.
Xu, B., & Chasteen, N. D. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54877-8 · Cited by 125
Heme, heme oxygenase and ferritin in vascular endothelial cell injury
Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Eaton, J. W., & Balla, G. (2005) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500076 · Cited by 126
Iron Homeostasis in Healthy Kidney and its Role in Acute Kidney Injury
Scindia, Y. M., Leeds, J. T., & Swaminathan, S. (2018) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2018.10.006 · Cited by 120
Everett, J. L., Collingwood, J. F., Tjhin, V. T., Brooks, J., Lermyte, F., Plascencia‐Villa, G., Hands-Portman, I., Dobson, J., Perry, G. L., & Telling, N. D. (2018) · Nanoscale · doi:10.1039/c7nr06794a · Cited by 122
Gozzelino, R., Andrade, B. B., Larsen, R., Luz, N. F., Vanoaica, L., Seixas, E., Coutinho, A., Cardoso, S., Rebelo, S., Poli, M., et al. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 119
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)
Hu, Y., Zheng, W., & Sun, L. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.01.001 · Cited by 115
“In silico analyses identified in SoFer1 a ferritin ferroxidase center with the seven conserved residues (E24, Y31, E58, E59, H62, E104, and Q138) that are known to function as iron ligands in H/M ferritins [3,41].”
BackgroundFormation of protein-coated iron minerals
Lewin, A. C., Moore, G. R., & Brun, N. E. L. (2005) · Dalton Transactions · doi:10.1039/b506071k · Cited by 115
Iron core mineralisation in prokaryotic ferritins
Brun, N. E. L., Crow, A., Murphy, M. E. P., Mauk, A. G., & Moore, G. R. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.04.002 · Cited by 115
Probing Structure-Function Relations In Ferritin And Bacterioferritin
Harrison, P. M., Andrews, S. C., Artymiuk, P. J., Ford, G. C., Guest, J. R., Hirzmann, J., Lawson, D. M., Livingstone, J. C., Smith, J. M., Treffry, A., et al. (1991) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60046-x · Cited by 114
Self-citationRegulation, mechanisms and proposed function of ferritin translocation to cell nuclei
Thompson, K. J., Fried, M. G., Ye, Z., Boyer, P., & Connor, J. R. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.10.2165 · Cited by 110
Biomimetic magnetic nanoparticles
Klem, M. T., Young, M., & Douglas, T. (2005) · Materials Today · doi:10.1016/s1369-7021(05)71078-6 · Cited by 110
Molecular aspects of iron uptake and storage in ferritin
Proulx-Curry, P. M., & Chasteen, N. D. (1995) · Coordination Chemistry Reviews · doi:10.1016/0010-8545(95)01148-i · Cited by 108
Ferritin L and H Subunits Are Differentially Regulated on a Post-transcriptional Level
Sammarco, M. C., Ditch, S., Banerjee, A., & Grabczyk, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703456200 · Cited by 102
Hamburger, A. E., West, A. P., Hamburger, Z. A., Hamburger, P., & Björkman, P. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.03.074 · Cited by 102
Sun, S., Arosio, P., Levi, S., & Chasteen, N. D. (1993) · Biochemistry · doi:10.1021/bi00087a015 · Cited by 99
Self-citationStructure and composition of ferritin cores from pea seed (Pisum sativum)
Wade, V. J., Treffry, A., Laulhère, J. P., Bauminger, E. R., Cleton, M. I., Mann, S., Briat, J., & Harrison, P. M. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90201-2 · Cited by 98
Self-citationThe many faces of the octahedral ferritin protein
Watt, R. K. (2011) · BioMetals · doi:10.1007/s10534-011-9415-8 · Cited by 98
Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin
Lobréaux, S., Yewdall, S. J., Briat, J., & Harrison, P. M. (1992) · Biochemical Journal · doi:10.1042/bj2880931 · Cited by 95
Self-citationLiu, X., & Theil, E. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401146101 · Cited by 94
Larade, K., & Storey, K. B. (2004) · Journal of Experimental Biology · doi:10.1242/jeb.00872 · Cited by 93
“Ferritin heavy chain subunits, which contain a catalytic ferroxidase center not present on the light chain, are responsible for the oxidation of iron and allow iron uptake/release (Lawson et al., 1989).”
BackgroundIron release and uptake by plant ferritin: effects of pH, reduction and chelation
Laulhère, J. P., & Briat, J. (1993) · Biochemical Journal · doi:10.1042/bj2900693 · Cited by 93
Andrews, S. C., Brun, N. E. L., Barynin, V. V., THOMSON, A. J., Moore, G. R., Guest, J. R., & Harrison, P. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23268 · Cited by 92
“The ferroxidase activity of mammalian ferritins is due to an active site (the ferroxidase center) in the middle of the four-helix bundle of each H-chain subunit where a dinuclear iron species is thought to form (Lawson et al., 1989, 1991).”
BackgroundSelf-citationFerroxidase kinetics of horse spleen apoferritin.
Sun, S., & Chasteen, N. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74019-8 · Cited by 91
Unification of the ferritin family of proteins.
Grossman, M. J., Hinton, S. M., Minak-Bernero, V., Slaughter, C. A., & Stiefel, E. I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2419 · Cited by 91
Levi, S., Santambrogio, P., Corsi, B., Cozzi, A., & Arosio, P. (1996) · Biochemical Journal · doi:10.1042/bj3170467 · Cited by 90
Self-citationConditional deletion of ferritin H in mice induces loss of iron storage and liver damage #
Darshan, D., Vanoaica, L., Richman, L., Beermann, F., & Kühn, L. C. (2009) · Hepatology · doi:10.1002/hep.23058 · Cited by 86
“The Fth allele was generated by crossing mice carrying the Fth allele to transgenic mice with β-actinFlpE recombinase.(3) Mice with the Fth allele on mixed genetic background (C57 BL/6 x 129/Sv) were crossed with the Mx-Cre transgenic mice(4) to obtain Fth;Mx-Cre (mutant) and Fth;+ (control) mice.”
BackgroundMethodMechanism of catalysis of Fe(II) oxidation by ferritin H chains
Treffry, A., Hirzmann, J., Yewdall, S. J., & Harrison, P. M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80417-f · Cited by 88
Self-citationBauminger, E. R., Harrison, P. M., Hechel, D., Hodson, N. W., Nowik, I., Treffry, A., & Yewdall, S. J. (1993) · Biochemical Journal · doi:10.1042/bj2960709 · Cited by 87
Self-citationFletcher, L. M., Halliday, J. W., & Powell, L. W. (1999) · Journal of Gastroenterology and Hepatology · doi:10.1046/j.1440-1746.1999.01836.x · Cited by 85
Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell
Watt, R. K., Hilton, R. J., & Graff, D. M. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.03.001 · Cited by 86
Iron detoxifying activity of ferritin
Cozzi, A., Santambrogio, P., Levi, S., & Arosio, P. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80823-2 · Cited by 84
Self-citationBrun, N. E. L., Wilson, M. T., Andrews, S. C., Guest, J. R., Harrison, P. M., THOMSON, A. J., & Moore, G. R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80404-i · Cited by 85
Self-citationFrazier, B. A., Pfeifer, J. D., Russell, D. G., Falk, P., Olsén, A., Hammar, M., Westblom, T. U., & Normark, S. J. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.4.966-972.1993 · Cited by 85
“Two of these deletions were localized in regions corresponding to loops in the horse L chain (7) and human H chain (17, 18, 31) (whose crystal structures have been solved); a single-amino-acid deletion localized to helix D; and a 2-amino-acid deletion localized to the region corresponding to helix E.”
BackgroundNeuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation
Levi, S., Cozzi, A., & Arosio, P. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.08.021 · Cited by 84
Self-citationIdentification of the ferroxidase centre of Escherichia coli bacterioferritin
Brun, N. E. L., Andrews, S. C., Guest, J. R., Harrison, P. M., Moore, G. R., & THOMSON, A. J. (1995) · Biochemical Journal · doi:10.1042/bj3120385 · Cited by 83
Self-citationDalton perspectives. Biomineralization: the hard part of bioinorganic chemistry!
Mann, S. (1993) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/dt9930000001 · Cited by 81
Broxmeyer, H. E., Cooper, S. H., Levi, S., & Arosio, P. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.3.770 · Cited by 81
Self-citationFormation of iron(III)-tyrosinate is the fastest reaction observed in ferritin
Waldo, G. S., & Theil, E. C. (1993) · Biochemistry · doi:10.1021/bi00211a039 · Cited by 80
Role of H and L Subunits in Mouse Ferritin
Rucker, P. J., Torti, F. M., & Torti, S. V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.52.33352 · Cited by 78
Treffry, A., Zhao, Z., Quail, M. A., Guest, J. R., & Harrison, P. M. (1997) · Biochemistry · doi:10.1021/bi961830l · Cited by 75
Self-citationCloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)
Zheng, W., Hu, Y., Xiao, Z., & Sun, L. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.01.013 · Cited by 74
Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
Garner, B., Roberg, K. B., & Brunk, U. T. (1998) · Free Radical Research · doi:10.1080/10715769800300121 · Cited by 74
Interactions and Reactions of Ferritin with DNA
Surguladze, N., Thompson, K., Beard, J. L., Connor, J. R., & Fried, M. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313348200 · Cited by 73
Lipiński, P., Drapier, J., Oliveira, L., Retmańska, H., Sochanowicz, B., & Kruszewski, M. K. (2000) · Blood · doi:10.1182/blood.v95.9.2960.009k13_2960_2966 · Cited by 73
Macrophage activation syndrome: Serological markers and treatment with anti-thymocyte globulin
Coca, A., Bundy, K. W., Marston, B. A., Huggins, J., & Looney, R. J. (2009) · Clinical Immunology · doi:10.1016/j.clim.2009.02.005 · Cited by 69
Wuytswinkel, O. V., Savino, G., & Briat, J. (1995) · Biochemical Journal · doi:10.1042/bj3050253 · Cited by 69
Metadata
- Authors
- Lawson, D. M., Treffry, A., Artymiuk, P. J., Harrison, P. M., Yewdall, S. J., Luzzago, A., Cesareni, G., Levi, S., & Arosio, P.
- Affiliations
- University of Sheffield (GB)
- European Molecular Biology Laboratory (DE)
- University of Rome Tor Vergata (IT)
- University of Milan (IT)
- Corresponding author
- Artymiuk, Peter J.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1989-08-28
- Volume
- 254
- Issue
- 1-2
- Pages
- 207-210
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1987119816
- Cited by
- 312
- References
- 13
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 8 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 5 · 2019: 5 · 2018: 8 · 2017: 2 · 2016: 9 · 2015: 8 · 2014: 8 · 2013: 11 · 2012: 10
- FWCI
- 8.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion)
- Archivio Istituzionale della Ricerca - Università Vita-Salute San Raffaele (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- ferritin, iron oxidation, site-directed mutagenesis, four-helix bundle, protein structure, iron storage
- MeSH terms
- Animals, Binding Sites, Ferritins, Horses, Humans, Mutation, Oxidoreductases, Protein Conformation, Recombinant Proteins, X-Ray Diffraction, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review