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Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells
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Transfectant HeLa cells were generated that expressed human ferritin H-chain wild type and an H-chain mutant with inactivated ferroxidase activity under the control of the tetracycline-responsive promoter (Tet-off). The clones accumulated exogenous ferritins up to levels 14-16-fold over background, half of which were as H-chain homopolymers. This had no evident effect in the mutant ferritin clone, whereas it induced an iron-deficient phenotype in the H-ferritin wild type clone, manifested by approximately 5-fold increase of IRPs activity, approximately 2.5-fold increase of transferrin receptor, approximately 1.8-fold increase in iron-transferrin iron uptake, and approximately 50% reduction of labile iron pool. Overexpression of the H-ferritin, but not of the mutant ferritin, strongly reduced cell growth and increased resistance to H(2)O(2) toxicity, effects that were reverted by prolonged incubation in iron-supplemented medium. The results show that in HeLa cells H-ferritin regulates the metabolic iron pool with a mechanism dependent on the functionality of the ferroxidase centers, and this affects, in opposite directions, cellular growth and resistance to oxidative damage. This, and the finding that also in vivo H-chain homopolymers are much less efficient than the H/L heteropolymers in taking up iron, indicate that functional activity of H-ferritin in HeLa cells is that predicted from the in vitro data.
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“Accumulating evidence shows that ferritin acts as an antioxidant protein (59, 60, 78, 159, 227, 243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
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“ferritin H disruption by siRNA sensitized the cells to H2O2-induced oxidative stress (60)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
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“overexpression or knockdown of ferritin expression in mammalian cells has proven the cytoprotective role of ferritin under prooxidative conditions (59, 60, 78, 159, 227, 243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [60]
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Citations
Cites
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943
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-citationUse of an Aqueous Soluble Tetrazolium/Formazan Assay for Cell Growth Assays in Culture
Cory, A. H., Owen, T. C., Barltrop, J. A., & Cory, J. G. (1991) · Cancer Communications · doi:10.3727/095535491820873191 · Cited by 1,520
Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292
Jordan, M., Schallhorn, A., & Wurm, F. M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.4.596 · Cited by 862
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-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-citationBeaumont, C., Leneuve, P., Devaux, I., Scoazec, J.-Y., Berthier, M., Loiseau, M.-N., Grandchamp, B., & Bonneau, D. (1995) · Nature Genetics · doi:10.1038/ng1295-444 · Cited by 293
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-citationIron-sulfur clusters as biosensors of oxidants and iron.
Rouault, T. A., & Klausner, R. D. (1996) · PubMed · Cited by 238
Research works printed but not linked: 1
- Yang, 1999, Biochem. J., 338, 615, 10.1042/bj3380615 · DOI · Paper page
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Items 101–200 of 241
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Iron metabolism in the eye: A review
Goralska, M., Ferrell, J., Harned, J., Lall, M. M., Nagar, S., Fleisher, L. N., & McGahan, M. C. (2008) · Experimental Eye Research · doi:10.1016/j.exer.2008.10.026 · Cited by 49
Czaja, A. J. (2019) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.15173 · Cited by 47
Kakhlon, O., Gruenbaum, Y., & Cabantchik, Z. I. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630431 · Cited by 44
Immunoregulation in human malaria: the challenge of understanding asymptomatic infection
de Mendonça, V. R. R., & Barral‐Netto, M. (2015) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/0074-02760150241 · Cited by 45
Lockyer, A. E., Spinks, J. N., Noble, L. R., Rollinson, D., & Jones, C. S. (2006) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2006.09.009 · Cited by 43
Iwasaki, K., Hailemariam, K., & Tsuji, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701477200 · Cited by 41
Cao, S., Ma, D., Ji, S., Zhou, M., & Zhu, S. (2024) · Molecules · doi:10.3390/molecules29174221 · Cited by 41
Balaratnam, S., West, N. R., & Basu, S. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky728 · Cited by 42
Magnetoferritin: Process, Prospects, and Their Biomedical Applications
Xue, L., Deng, D., & Sun, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102426 · Cited by 41
Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo
Wilkinson, J. C., Di, X., Schönig, K., Buss, J. L., Kock, N. D., Cline, J. M., Saunders, T. L., Bujard, H., Torti, S. V., & Torti, F. M. (2006) · Biochemical Journal · doi:10.1042/bj20060063 · Cited by 41
Pharmacological induction of ferritin prevents osteoblastic transformation of smooth muscle cells
Becs, G., Zarjou, A., Agarwal, A., Kovács, K. É., Becs, Á., Nyitrai, M., Balogh, E., Bányai, E., Eaton, J. W., Arosio, P., et al. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12682 · Cited by 40
Self-citationSodium nitroprusside suppresses male fertility in vitro
Rahman, M. S., Kwon, W., Lee, J. ‐., Kim, J., Yoon, S.-C., Park, Y. ‐., You, Y., Hwang, S., & Pang, M. (2014) · Andrology · doi:10.1111/j.2047-2927.2014.00273.x · Cited by 40
McCullough, K., & Bolisetty, S. (2020) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2020.01.007 · Cited by 40
Ali, A., Shafarin, J., Jabal, R. A., Al-Jabi, N., Hamad, M., Muhammad, J. S., Unnikannan, H., & Hamad, M. A. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13303 · Cited by 40
Li, G., ZHAO, Q., & ZHENG, W. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.10.003 · Cited by 39
Bitoun, J. P., Wu, G., & Ding, H. (2008) · BioMetals · doi:10.1007/s10534-008-9154-7 · Cited by 39
Intracellular and Extracellular Labile Iron Pools
Cabantchik, Z. I., Kakhlon, O., Epsztejn, S., Zanninelli, G., & Breuer, W. V. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0593-8_4 · Cited by 39
Cozzi, A., Santambrogio, P., Corsi, B., Campanella, A., Arosio, P., & Levi, S. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.05.004 · Cited by 38
Self-citationVercellotti, G. M., Khan, F. B., Nguyen, J., Chen, C., Bruzzone, C. M., Bechtel, H., Brown, G., Nath, K. A., Steer, C. J., Hebbel, R. P., et al. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00079 · Cited by 38
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Mattè, A., Falco, L. D., Federti, E., Cozzi, A., Iolascon, A., Levi, S., Mohandas, N., Zamò, A., Bruno, M., Lebœuf, C., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7051 · Cited by 38
Self-citationp53-Mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y
Faniello, M. C., Sanzo, M. D., Quaresima, B., Baudi, F., Caro, V. D., Cuda, G., Morrone, G., Sal, G. D., Spinelli, G., Venuta, S., et al. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.02.010 · Cited by 38
Li, G. J., Choi, B., Wang, X., Liu, J., Waalkes, M. P., & Zheng, W. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.02.003 · Cited by 38
Ren, C., Chen, T., Jiang, X., Wang, Y., & Hu, C. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.03.022 · Cited by 37
Receptor‐Mediated Cellular Uptake of Nanoparticles: A Switchable Delivery System
Zhang, L., Fischer, W., Pippel, E., Hause, G., Brandsch, M., & Knez, M. (2011) · Small · doi:10.1002/smll.201100238 · Cited by 34
Barnés, C. M., Theil, E. C., & Raymond, K. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032089399 · Cited by 34
Neuronal ferritin heavy chain and drug abuse affect HIV-associated cognitive dysfunction
Pitcher, J., Abt, A., Myers, J., Han, R., Snyder, M. A., Graziano, A., Festa, L. K., Kutzler, M. A., Garcia, F., Gao, W., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci70090 · Cited by 35
Federti, E., Mattè, A., Ghigo, A., Andolfo, I., Cimino, J., Siciliano, A., Lebœuf, C., Janin, A., Manna, F., Choi, S. Y., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.004 · Cited by 30
Self-citationP66Shc mediated ferritin degradation—A novel mechanism of ROS formation
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Naumova, A. V., Balu, N., Yarnykh, V. L., Reinecke, H., Murry, C. E., & Yuan, C. (2014) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248414525999 · Cited by 33
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Ono, K., Fuma, K., Tabata, K., & Sawada, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.055 · Cited by 32
Li, H., Xia, X., Tan, X., Zang, J., Wang, Z., El-Seedi, H. R., & Du, M. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1911925 · Cited by 31
Goralska, M., Holley, B. L., & McGahan, M. C. (2001) · PubMed · Cited by 32
Choi, S. H., Cho, H. R., Kim, H. S., Kim, Y. H., Kang, K. W., Kim, H., & Moon, W. K. (2011) · NMR in Biomedicine · doi:10.1002/nbm.1788 · Cited by 31
Ferrostatin-1 attenuates hypoxic-ischemic brain damage in neonatal rats by inhibiting ferroptosis
Zhang, M., Liu, Z., Zhou, W., Shen, M., Mao, N., Xu, H., Wang, Y., Xu, Z., Li, M., Jiang, H., et al. (2023) · Translational Pediatrics · doi:10.21037/tp-23-189 · Cited by 31
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Lee, S., Lee, S., & Biswal, S. (2012) · Theranostics · doi:10.7150/thno.3634 · Cited by 31
Ingrassia, R., Gerardi, G., Biasiotto, G., & Arosio, P. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj101 · Cited by 31
Self-citationGoralska, M., Holley, B. L., & McGahan, M. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305827200 · Cited by 31
Cremonesi, L., Foglieni, B., Fermo, I., Cozzi, A., Paroni, R. C., Ruggeri, G., Belloli, S., Levi, S., Fargion, S. R., Ferrari, M., et al. (2003) · PubMed · Cited by 31
Self-citationFerritinophagy induced ferroptosis in the management of cancer
Liu, Y.-C., Gong, Y.-T., Sun, Q., Wang, B., Yan, Y., Chen, Y.-X., Zhang, L., Zhang, W., & Luan, X. (2023) · Cellular Oncology · doi:10.1007/s13402-023-00858-x · Cited by 30
H ferritin silencing induces protein misfolding in K562 cells: A Raman analysis
Zolea, F., Biamonte, F., Candeloro, P., Sanzo, M. D., Cozzi, A., Vito, A. D., Quaresima, B., Lobello, N., Trecroci, F., Fabrizio, E. M. D., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.161 · Cited by 30
Self-citationCarmona, F., Poli, M., Bertuzzi, M., Gianoncelli, A., Gangemi, F., & Arosio, P. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.12.011 · Cited by 30
Self-citationBou‐Abdallah, F., Carney, E. S., Chasteen, N. D., Arosio, P., Viescas, A. J., & Papaefthymiou, G. C. (2007) · Biophysical Chemistry · doi:10.1016/j.bpc.2007.08.003 · Cited by 30
Self-citationPicard, É., Ranchon‐Cole, I., Jonet, L., Beaumont, C., Béhar‐Cohen, F., Courtois, Y., & Jeanny, J. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5705 · Cited by 33
Nash, B., Tarn, K., Irollo, E., Luchetta, J., Festa, L. K., Halcrow, P. W., Datta, G., Geiger, J. D., & Meucci, O. (2019) · eNeuro · doi:10.1523/eneuro.0237-19.2019 · Cited by 30
Kaikkonen, M. U., Lesch, H. P., Pikkarainen, J. T., Räty, J. K., Vuorio, T., Huhtala, T., Taavitsainen, M., Laitinen, T., Tuunanen, P. I., Gröhn, O. H. J., et al. (2009) · Gene Therapy · doi:10.1038/gt.2009.47 · Cited by 29
Efficiency of Ferritin as an MRI Reporter Gene in NPC Cells Is Enhanced by Iron Supplementation
Feng, Y., Liu, Q., Zhu, J., Xie, F., & Li, L. (2012) · BioMed Research International · doi:10.1155/2012/434878 · Cited by 29
Keogh, M. J., Morris, C. M., & Chinnery, P. F. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00006-5 · Cited by 28
Lu, Z., Nie, G., Li, Y., Soe-Lin, S., Tao, Y., Cao, Y., Zhang, Z., Liu, N., Ponka, P., & Zhao, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2306 · Cited by 28
He, X., Cai, J., Liu, B., Zhong, Y., & Qin, Y. (2015) · Stem Cell Research & Therapy · doi:10.1186/s13287-015-0205-z · Cited by 27
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Walker, B., Tiong, J., & Jefferies, W. A. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)11020-x · Cited by 27
Mao, Q., Xie, Z., Wang, X., Chen, W., Ren, M., Shang, M., Lei, H., Tian, Y., Li, S., Liang, P., et al. (2014) · Parasitology Research · doi:10.1007/s00436-014-4230-0 · Cited by 27
The LIM-homeodomain transcription factor LMX1B regulates expression of NF-kappa B target genes
Rascle, A., Neumann, T., Raschta, A., Neumann, A., Heining, E., Kastner, J., & Witzgall, R. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.012 · Cited by 27
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Ikegami, Y., Inukai, K., Imai, K., Sakamoto, Y., Katagiri, H., Kurihara, S., Awata, T., & Katayama, S. (2008) · Diabetes · doi:10.2337/db07-0690 · Cited by 26
Hałoń, M., Kaczor, J. J., Ziółkowski, W., Flis, D. J., Borkowska, A., Popowska, U., Nyka, W. M., Woźniak, M., & Antosiewicz, J. (2014) · Free Radical Research · doi:10.3109/10715762.2014.955484 · Cited by 26
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Holtkamp, N., Afanasieva, A., Elstner, A., van Landeghem, F. K. H., Könneker, M., Kuhn, S. A., Kettenmann, H., & von Deimling, A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.253 · Cited by 25
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Chen, J., Ma, D., Bao, J., Zhang, Y., & Deng, G. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/7410865 · Cited by 22
Wallander, M. L., Zumbrennen‐Bullough, K. B., Rodansky, E. S., Romney, S. J., & Leibold, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803005200 · Cited by 22
He, S., Peng, K., Hong, Y., Wang, J., Sheng, J., & Gu, Q. (2013) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.12.021 · Cited by 22
Eid, R., Boucher, É. L., Gharib, N., Khoury, C. M., Arab, N. T. T., Murray, A., Young, P. G., Mandato, C. A., & Greenwood, M. T. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.02.010 · Cited by 22
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Shahraki, S., Delarami, H. S., Razmara, Z., & Heidari, A. (2023) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2023.123569 · Cited by 21
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Zolea, F., Biamonte, F., Battaglia, A. M., Faniello, M. C., Cuda, G., & Costanzo, F. S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163078 · Cited by 20
RetractedBoero, M., Pagliaro, P., Tullio, F., Pellegrino, R. M., Palmieri, A., Ferbo, L., Saglio, G. N., Gobbi, M. D., Penna, C. R. R., & Roetto, A. (2015) · BioFactors · doi:10.1002/biof.1237 · Cited by 20
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Self-citationKoike, T., Takenaka, M., Suzuki, N., Ueda, Y., Mori, M., Hirayama, T., Nagasawa, H., & Morishige, K. (2022) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.21-82 · Cited by 18
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Daba, A., Koromilas, A. E., & Pantopoulos, K. (2012) · RNA · doi:10.1261/rna.029322.111 · Cited by 17
Seidel, U., Lüersen, K., Huebbe, P., & Rimbach, G. H. (2020) · Antioxidants · doi:10.3390/antiox9111071 · Cited by 17
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Wilkinson, J. C., Pietsch, E. C., Torti, S. V., & Torti, F. M. (2003) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(02)00037-7 · Cited by 17
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Maria, A., & Viljoe, M. (2011) · InTech eBooks · doi:10.5772/20586 · Cited by 16
Mulvey, C. M., Tudzarova, S., Crawford, M., Williams, G. H., Stoeber, K., & Godovac‐Zimmermann, J. (2013) · Journal of Proteome Research · doi:10.1021/pr3010919 · Cited by 16
Harned, J., Ferrell, J., Lall, M. M., Fleisher, L. N., Nagar, S., Goralska, M., & McGahan, M. C. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-3861 · Cited by 16
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Self-citationKruszewski, M. K., Iwaneñko, T., Bartłomiejczyk, T., Woliński, J., Starzyński, R. R., Gralak, M. A., Zabielski, R., & Lipiński, P. (2008) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2008.08.020 · Cited by 15
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Naumova, A. V., & Velde, G. V. (2017) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1482 · Cited by 15
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Hasegawa, S., Morokoshi, Y., Kanda, H., Tsukamoto, S., Zheng, J., Tsuji, A. B., Furukawa, T., Kakinuma, S., Shimada, Y., & Saga, T. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs251 · Cited by 15
Sun, S., Zhu, J. X., Ge, X., & Zhang, W. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.08.029 · Cited by 13
Mackenzie, E. L., & Tsuji, Y. (2008) · Biochemical Journal · doi:10.1042/bj20071544 · Cited by 13
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Metadata
- Authors
- Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P.
- Affiliations
- IRCCS Ospedale San Raffaele (IT)
- University of Brescia (IT)
- Corresponding author
- Arosio, Paolo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25122-25129
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2030928461
- Cited by
- 242
- References
- 36
- Citations by year
- 2025: 4 · 2024: 5 · 2023: 8 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 7 · 2018: 3 · 2017: 8 · 2016: 7 · 2015: 8 · 2014: 14 · 2013: 9 · 2012: 10
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Keywords
- ferroxidase activity, iron metabolism, iron regulatory proteins, transferrin receptor, iron absorption, labile iron pool, oxidative stress resistance, cell growth, HeLa cells, tetracycline-responsive promoter
- MeSH terms
- Anti-Bacterial Agents, Apoferritins, Cell Division, Ceruloplasmin, Doxycycline, Enzyme-Linked Immunosorbent Assay, Ferritins, HeLa Cells, Humans, Hydrogen Peroxide, Iron, Mutation, Plasmids, Precipitin Tests, Promoter Regions, Genetic, Tetracycline, Time Factors, Transfection, Immunoblotting, Mutagenesis, DNA, Complementary, Oxidative Stress
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