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The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
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The oxidation of Fe(II) by serum was studied at pH 7.35 and at various oxygen concentrations which approach the physiological conditions of human serum. The nonenzymic oxidation of Fe(II) was estimated to be insufficient to account for a rate of Fe(III)-transferrin formation necessary to provide an adequate iron supply for hemoglobin and other biosyntheses if Fe(II) is a relevant source of serum iron. The results suggested that an appreciable catalytic activity was involved in Fe(II) oxidation in serum. The ferroxidase activity of various normal human sera correlates precisely with the p-phenylenediamine oxidase activity of these sera. This catalytic activity is inhibited by azide and cyanide, and is low in sera with reduced ceruloplasmin levels. Fe(II) oxidation is also associated with the ceruloplasmin fraction on diethylaminoethyl cellulose chromatography of serum. The oxidation of Fe(II) by ceruloplasmin is zero order with respect to oxygen (10 to 200 µm), whereas the nonenzymic oxidation is first order. A biological role for the ceruloplasmin of serum in promoting the rate of iron saturation of transferrin and in stimulating iron utilization and the designation of the enzyme as serum ferroxidase is proposed.
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“Transport is facilitated by multicopper ferroxidases including the abundant serum protein ceruloplasmin and its membrane-bound intestinal homolog hephaestin.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [81]
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Cites
Mack, H. C. (1960) · Clinical Obstetrics & Gynecology · doi:10.1097/00003081-196006000-00007 · Cited by 929
Holmberg, C. G., Laurell, C. ‐., & Gjertsen, P. (1948) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.02-0550 · Cited by 472
THE PLASMA-TO-CELL CYCLE OF TRANSFERRIN*
Jandl, J. H., & Katz, J. H. (1963) · Journal of Clinical Investigation · doi:10.1172/jci104718 · Cited by 440
The specific binding of iron(III) and copper(II) to transferrin and conalbumin
Aasa, R., Malmström, B. G., Saltman, P., & Vänngård, T. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)90599-7 · Cited by 366
TRANSFER OF IRON FROM SERUM IRON-BINDING PROTEIN TO HUMAN RETICULOCYTES*
Jandl, J. H., Inman, J. K., Simmons, R. L., & Allen, D. W. (1959) · Journal of Clinical Investigation · doi:10.1172/jci103786 · Cited by 353
THE QUANTITATIVE DETERMINATION OF IRON KINETICS AND HEMOGLOBIN SYNTHESIS IN HUMAN SUBJECTS*
Pollycove, M., & Mortimer, R. G. (1961) · Journal of Clinical Investigation · doi:10.1172/jci104310 · Cited by 231
Koechlin, B. A. (1952) · Journal of the American Chemical Society · doi:10.1021/ja01130a054 · Cited by 124
Moore, C. V., Arrowsmith, W. R., Welch, J., & Minnich, V. (1939) · Journal of Clinical Investigation · doi:10.1172/jci101069 · Cited by 105
The role of chelation in iron metabolism
Saltman, P. (1965) · Journal of Chemical Education · doi:10.1021/ed042p682 · Cited by 101
Studies on the Exchange of Iron between Transferrin and Reticulocytes
Morgan, E. H., & Laurell, C. ‐. (1963) · British Journal of Haematology · doi:10.1111/j.1365-2141.1963.tb05471.x · Cited by 88
Research works printed but not linked: 3
- Osaki, S., McDermott, J. A., Johnson, D. A., and Frieden, E., in J. Peisach, W. Blumberg, and P. Aisen (Editors), International Symposium on the Biochemistry of Copper, Academic Press, Inc., New York, in press.
- Trader, 1965, Federation Proc., 24, 222
- Broman, 1964, Acta Soc. Med. Upsalien., 69, 75
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[1] Role of free radicals and catalytic metal ions in human disease: An overview
Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M. F., Kieber‐Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,795
Ala, A., Walker, A. P., Ashkan, K., Dooley, J. S., & Schilsky, M. L. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60196-2 · Cited by 1,449
Role of metals in oxygen radical reactions
Aust, S. D., Morehouse, L. A., & Thomas, C. E. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90025-x · Cited by 1,150
The importance of free radicals and catalytic metal ions in human diseases.
Halliwell, B., & Gutteridge, J. M. C. (1985) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(85)90001-9 · Cited by 941
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Hellman, N. E., & Gitlin, J. D. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.012502.114457 · Cited by 954
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Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A. (1996) · Science · doi:10.1126/science.271.5255.1552 · Cited by 683
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Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670
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Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568
Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2539 · Cited by 558
Regulation of iron acquisition and storage: consequences for iron-linked disorders
De Domenico, I., McVey Ward, D., & Kaplan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2295 · Cited by 464
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Yoshida, K., Furihata, K., Takeda, S., Nakamura, A., Yamamoto, K., Morita, H., Hiyamuta, S., Ikeda, S.-I., Shimizu, N., & Yanagisawa, N. (1995) · Nature Genetics · doi:10.1038/ng0395-267 · Cited by 463
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Mylroie, A. A., Collins, H. H. L., Umbles, C., & Kyle, J. (1986) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(86)90286-3 · Cited by 383
Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury
Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06578.2002 · Cited by 379
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377
The role of ceruloplasmin in iron metabolism.
Roeser, H. P., Lee, G. R., Nacht, S., & Cartwright, G. E. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106460 · Cited by 365
Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis
Shiva, S., Wang, X., Ringwood, L. A., Xu, X., Yuditskaya, S., Annavajjhala, V., Miyajima, H., Hogg, N., Harris, Z. L., & Gladwin, M. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio813 · Cited by 359
Yanatori, I., & Kishi, F. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.020 · Cited by 371
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Solomons, N. W. (1979) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/32.4.856 · Cited by 343
Martin, F., Linden, T., Katschinski, D. M., Oehme, F., Flamme, I., Mukhopadhyay, C. K., Eckhardt, K., Tröger, J., Barth, S., Camenisch, G., et al. (2005) · Blood · doi:10.1182/blood-2004-10-3980 · Cited by 349
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Iron misregulation in the brain: a primary cause of neurodegenerative disorders
Ke, Y., & Qian, Z. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00353-3 · Cited by 341
Ferroptosis and cell death mechanisms in Parkinson's disease
Guiney, S. J., Adlard, P. A., Bush, A. I., Finkelstein, D. I., & Ayton, S. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.01.004 · Cited by 353
Mazumder, B., Sampath, P., Seshadri, V., Maitra, R. K., DiCorleto, P. E., & Fox, P. L. (2003) · Cell · doi:10.1016/s0092-8674(03)00773-6 · Cited by 344
CueO Is a Multi-copper Oxidase That Confers Copper Tolerance in Escherichia coli
Grass, G., & Rensing, C. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5474 · Cited by 331
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Mason, K. E. (1979) · Journal of Nutrition · doi:10.1093/jn/109.11.1979 · Cited by 328
Patel, B. N., & David, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20185 · Cited by 327
Iron Metabolism: A Comprehensive Review
Beard, J. L., Dawson, H. D., & Piñero, D. J. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1996.tb03794.x · Cited by 323
copper proteins systems containing the “Blue” copper center
Fee, J. A. (2007) · Springer eBooks · doi:10.1007/bfb0116549 · Cited by 309
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
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Eide, D. J. (1998) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.18.1.441 · Cited by 295
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Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274
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He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.004 · Cited by 260
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van Veen, W. L., Mulder, E. G., & Deinema, M. H. (1978) · Microbiological Reviews · doi:10.1128/mr.42.2.329-356.1978 · Cited by 254
The Regulation of Iron Absorption and Homeostasis.
Wallace, D. F. (2016) · PubMed · Cited by 268
1 Iron toxicity and oxygen radicals
Gutteridge, J. M. C., & Halliwell, B. B. (1989) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(89)80017-4 · Cited by 254
The 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
Old iron, young copper: from Mars to Venus
Crichton, R. R., & Pierre, J.-L. (2001) · Biometals · doi:10.1023/a:1016710810701 · Cited by 248
Morita, H., Ikeda, S., Yamamoto, K., Morita, S., Yoshida, K., Nomoto, S., Kato, M., & Yanagisawa, N. (1995) · Annals of Neurology · doi:10.1002/ana.410370515 · Cited by 245
Brain iron metabolism: Neurobiology and neurochemistry
Ke, Y., & Qian, Z. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.07.009 · Cited by 239
Increased regional brain concentrations of ceruloplasmin in neurodegenerative disorders
Loeffler, D. A., LeWitt, P. A., Juneau, P. L., Sima, A. A. F., Nguyen, H.-U., DeMaggio, A. J., Brickman, C. M., Brewer, G. J., Dick, R. D., Troyer, M. D., et al. (1996) · Brain Research · doi:10.1016/s0006-8993(96)00782-2 · Cited by 237
The Mobilization of Iron from the Perfused Mammalian Liver by a Serum Copper Enzyme, Ferroxidase I
Osaki, S., Johnson, D. A., & Frieden, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62284-7 · Cited by 236
Self-citationFREE-RADICAL OXIDATION AND ANTIOXIDANTS
Dormandy, T. L. (1978) · The Lancet · doi:10.1016/s0140-6736(78)91148-0 · Cited by 236
The long history of iron in the Universe and in health and disease
Sheftel, A. D., Mason, A. B., & Ponka, P. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.002 · Cited by 243
Qian, Z., & Wang, Q. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00012-5 · Cited by 230
Serum copper to zinc ratio: Relationship with aging and health status
Malavolta, M., Piacenza, F., Basso, A., Giacconi, R., Costarelli, L., & Mocchegiani, E. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.01.004 · Cited by 230
Iron and copper transport in yeast and its relevance to human disease
Askwith, C. C., & Kaplan, J. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01192-x · Cited by 220
Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 262
Rattner, A., & Nathans, J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0492-05.2005 · Cited by 218
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Kwok, J. C., & Richardson, D. R. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00213-x · Cited by 215
Iron Metabolism: Iron Deficiency and Iron Overload
Andrews, N. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.75 · Cited by 211
Caeruloplasmin: Physiological and Pathological Perspectives
Gutteridge, J. M. C., & Stocks, J. (1981) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368109105866 · Cited by 217
Structure to function relationships in ceruloplasmin: a 'moonlighting' protein
Bielli, P., & Calabrese, L. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8519-2 · Cited by 212
Underwood, E. J. (1977) · Elsevier eBooks · doi:10.1016/b978-0-12-709065-8.50007-9 · Cited by 210
Multi-Copper Oxidases and Human Iron Metabolism
Vashchenko, G., & MacGillivray, R. T. A. (2013) · Nutrients · doi:10.3390/nu5072289 · Cited by 223
Metal ions in macrophage antimicrobial pathways: emerging roles for zinc and copper
Stafford, S. L., Bokil, N. J., Achard, M. E. S., Kapétanovic, R., Schembri, M. A., McEwan, A. G., & Sweet, M. J. (2013) · Bioscience Reports · doi:10.1042/bsr20130014 · Cited by 217
Patel, B. N., Dunn, R. J., & David, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4305 · Cited by 202
Brain iron transport and neurodegeneration
Qian, Z., & Shen, X. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(00)01910-9 · Cited by 196
The copper-iron connection in biology: Structure of the metallo-oxidase Fet3p
Taylor, A. B., Stoj, C. S., Ziegler, L. M., Kosman, D. J., & Hart, P. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506227102 · Cited by 192
Passamonti, S., Terdoslavich, M., Franca, R., Vanzo, A., Tramer, F., Braidot, E., Petrussa, E., & Vianello, A. (2009) · Current Drug Metabolism · doi:10.2174/138920009788498950 · Cited by 190
Copper transport and its alterations in Menkes and Wilson diseases
DiDonato, M., & Sarkar, B. (1997) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(96)00064-6 · Cited by 189
Novel Chelators for Cancer Treatment: Where Are We Now?
Merlot, A. M., Kalinowski, D. S., & Richardson, D. R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4540 · Cited by 195
Zinc-induced copper deficiency
Hoffman, H. N., Phyliky, R. L., & Fleming, C. R. (1988) · Gastroenterology · doi:10.1016/0016-5085(88)90445-3 · Cited by 182
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Chua, A. C. G., Graham, R. M., Trinder, D., & Olynyk, J. K. (2007) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701428257 · Cited by 172
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Healy, J., & Tipton, K. F. (2007) · Journal of Neural Transmission · doi:10.1007/s00702-007-0687-7 · Cited by 166
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Samokyszyn, V. M., Miller, D. M., Reif, D. W., & Aust, S. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31218-8 · Cited by 166
Review article: the iron overload syndromes
Siddique, A., & Kowdley, K. V. (2012) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2012.05051.x · Cited by 162
Mobilization of liver iron by ferroxidase (ceruloplasmin).
Osaki, S., & Johnson, D. A. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63623-3 · Cited by 159
Ayton, S., & Lei, P. (2014) · BioMed Research International · doi:10.1155/2014/581256 · Cited by 163
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)
Osaki, S. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99669-9 · Cited by 160
Self-citationAceruloplasminemia: An Inherited Neurodegenerative Disease with Impairment of Iron Homeostasis
XU, X., PIN, S., GATHINJI, M., FUCHS, R., & HARRIS, Z. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.024 · Cited by 160
Unexpected role of ceruloplasmin in intestinal iron absorption
Cherukuri, S., Potla, R., Sarkar, J., Nurko, S., Harris, Z. L., & Fox, P. L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.003 · Cited by 163
Bremner, I. (1974) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500001359 · Cited by 159
Role of the syncytium in placenta-mediated complications of preeclampsia
Guller, S. (2009) · Thrombosis Research · doi:10.1016/j.thromres.2009.05.016 · Cited by 151
Ceruloplasmin in neurodegenerative diseases
Vassiliev, V. B., Harris, Z. L., & Zatta, P. F. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.003 · Cited by 151
Gutteridge, J. M. C., & Quinlan, G. J. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90052-f · Cited by 148
Parkinson's disease: Alterations in iron and redox biology as a key to unlock therapeutic strategies
Ma, L., Azad, M. G., Dharmasivam, M., Richardson, V., Quinn, R. J., Feng, Y., Pountney, D. L., Tonissen, K. F., Mellick, G. D., Yanatori, I., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101896 · Cited by 148
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Lohr, H. R., Kunchithapautham, K., Sharma, A. K., & Rohrer, B. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.01.014 · Cited by 147
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Frieden, E., & Hsieh, H. (1976) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122891.ch6 · Cited by 146
Self-citationAttieh, Z. K., Mukhopadhyay, C. K., Seshadri, V., Tripoulas, N. A., & Fox, P. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.1116 · Cited by 144
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Harris, E. D. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360390250649 · Cited by 156
Frazer, D. M., Vulpe, C. D., McKie, A. T., Wilkins, S. J., Trinder, D., Cleghorn, G. J., & Anderson, G. J. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.4.g931 · Cited by 137
Gitlin, J. D. (1998) · Pediatric Research · doi:10.1203/00006450-199809000-00001 · Cited by 140
Antioxidant properties of caeruloplasmin towards iron‐ and copper‐dependent oxygen radical formation
Gutteridge, J. M. C. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)81111-9 · Cited by 137
Anemia, Iron Storage and Ceruloplasmin in Copper Nutrition in the Growing Rat
Evans, J. L., & Abraham, P. A. (1973) · Journal of Nutrition · doi:10.1093/jn/103.2.196 · Cited by 137
Oxidative stress by inorganic nanoparticles
Tee, J. K., Ong, C. N., Bay, B., Ho, H. K., & Leong, D. T. (2015) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1374 · Cited by 139
Aceruloplasminemia, an inherited disorder of iron metabolism
Miyajima, H., Takahashi, Y., & Kono, S. (2003) · BioMetals · doi:10.1023/a:1020775101654 · Cited by 136
Swain, J., & Gutteridge, J. M. C. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00726-p · Cited by 136
Sampath, P., Mazumder, B., Seshadri, V., & Fox, P. L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1509-1519.2003 · Cited by 130
Impact of Copper Limitation on Expression and Function of Multicopper Oxidases (Ferroxidases)
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Sharp, P. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004386 · Cited by 125
Metadata
- Authors
- Osaki, S., Johnson, D. A., & Frieden, E.
- Affiliations
- Florida State University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1966-06
- Volume
- 241
- Issue
- 12
- Pages
- 2746-2751
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1508143080
- Cited by
- 679
- References
- 20
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 18 · 2020: 7 · 2019: 12 · 2018: 15 · 2017: 9 · 2016: 15 · 2015: 17 · 2014: 21 · 2013: 16 · 2012: 17
- FWCI
- 8.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- ceruloplasmin, ferroxidase activity, iron(II) oxidation, serum iron, oxygen dependence, iron metabolism
- MeSH terms
- Aniline Compounds, Humans, Iron, Oxidoreductases, Spectrophotometry, Transferrin, In Vitro Techniques
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