Heme oxygenase 1 is required for mammalian iron reutilization
Open accessAbstract
The majority of iron for essential mammalian biological activities such as erythropoiesis is thought to be reutilized from cellular hemoproteins. Here, we generated mice lacking functional heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron, to assess its participation in iron homeostasis. Hmox1-deficient adult mice developed an anemia associated with abnormally low serum iron levels, yet accumulated hepatic and renal iron that contributed to macromolecular oxidative damage, tissue injury, and chronic inflammation. Our results indicate that Hmox1 has an important recycling role by facilitating the release of iron from hepatic and renal cells, and describe a mouse model of human iron metabolic disorders.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Recycling of iron from HB starts with erythrophagocytosis of senescent RBC and involves degradation in the lysosome, separation of heme and globin, and cleavage of heme by HO1 yielding iron, CO and biliverdin.
“The recycling of iron from HB starts with erythrophagocytosis of senescent RBC and involves the degradation of those cells in the lysosome, the separation of heme and globin and the cleavage of heme by HO1 which yields iron, CO and biliverdin (Poss and Tonegawa, 1997).”
From Iron in infection and immunity (2020) · cites this paper as Poss and Tonegawa, 1997
The introduction states that heme oxygenase catabolizes heme to biliverdin, carbon monoxide, and free iron, and the Discussion describes an Hmox1-dependent pathway for iron reutilization (pages not specified in our copy). The paper notes that hemolysis usually occurs in phagocytic cells, but does not describe senescent RBC erythrophagocytosis, lysosomal degradation, or separation of heme from globin as the sequence claimed. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHO-1 deficient mice show enhanced CD4+ T cell activation.
“Accordingly, HO-1 deficient mice show enhanced CD4+ T cell activation (Poss and Tonegawa, 1997).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Poss and Tonegawa, 1997
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101 · see citing works
[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 · see citing works
Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800 · see citing works
A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664 · see citing works
THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases
Maines, M. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.517 · Cited by 2,489 · see citing works
Carbon Monoxide: a Putative Neural Messenger
Verma, A. M., Hirsch, D. B., Glatt, C. E., Ronnett, G. V., & Snyder, S. H. (1993) · Science · doi:10.1126/science.7678352 · Cited by 1,563 · see citing works
Age-related changes in oxidized proteins.
Oliver, C. N., Ahn, B. W., Moerman, E. J., Goldstein, S., & Stadtman, E. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45598-6 · Cited by 1,306 · see citing works
Keyse, S. M., & Tyrrell, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.1.99 · Cited by 1,271 · see citing works
Teratocarcinomas and Embryonic Stem Cells: A Practical Approach
Robertson, E. J., & Beddington, R. (1988) · Development · doi:10.1242/dev.102.1.3 · Cited by 1,034 · see citing works
Progress in understanding the pathogenesis of the anemia of chronic disease [see comments]
Means, R. T., & Krantz, S. B. (1992) · Blood · doi:10.1182/blood.v80.7.1639.bloodjournal8071639 · Cited by 671 · see citing works
Cloning and expression of cDNA for rat heme oxygenase.
Shibahara, S., Müller, R., Taguchi, H., & Yoshida, T. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.7865 · Cited by 452 · see citing works
Zakhary, R., Gaine, S., DINERMAN, J. L., Ruat, M., Flavahan, N. A., & Snyder, S. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.2.795 · Cited by 401 · see citing works
Hepatology: A Textbook of Liver Disease
O'Grady, J. (1997) · Gut · doi:10.1136/gut.40.4.562 · Cited by 391 · see citing works
Protein oxidative damage is associated with life expectancy of houseflies.
Sohal, R. S., Agarwal, S., Dubey, A., & Orr, W. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7255 · Cited by 354 · see citing works
Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron.
Eisenstein, R. S., García-Mayol, D., Pettingell, W. H., & Munro, H. N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.3.688 · Cited by 308 · see citing works
Ewing, J. F., & Maines, M. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.12.5364 · Cited by 264 · see citing works
Nathanson, J. A., Scavone, C., Scanlon, C., & McKee, M. (1995) · Neuron · doi:10.1016/0896-6273(95)90222-8 · Cited by 182 · see citing works
Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
Poss, K. D., Thomas, M. J., Ebralidze, A. K., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90177-9 · Cited by 169 · see citing works
Self-citationKutty, R. K., Kutty, G., Wiggert, B. O., Chader, G. J., Darrow, R. M., & Organisciak, D. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1177 · Cited by 157 · see citing works
Cantoni, L., Rossi, C., Rizzardini, M., et al. (1991) · Biochemical Journal · doi:10.1042/bj2790891 · Cited by 155 · see citing works
Rizzardini, M., Terao, M., Falciani, F., et al. (1993) · Biochemical Journal · doi:10.1042/bj2900343 · Cited by 144 · see citing works
Kutty, R. K., Nagineni, C. N., Kutty, G., et al. (1994) · Journal of Cellular Physiology · doi:10.1002/jcp.1041590221 · Cited by 119 · see citing works
The Role of the Reticulo‐Endothelial Cell in Iron Metabolism*
Noyes, W. D., Bothwell, T. H., & Finch, C. A. (1960) · British Journal of Haematology · doi:10.1111/j.1365-2141.1960.tb06216.x · Cited by 110 · see citing works
Zufall, F., & Leinders‐Zufall, T. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02703.1997 · Cited by 96 · see citing works
Braggins, P. E., Trakshel, G. M., Kutty, R. K., & Maines, M. D. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80205-4 · Cited by 96 · see citing works
Storage iron kinetics. II. The uptake of hemoglobin iron by hepatic parenchymal cells.
Hershko, C., Cook, J. D., & Ca, F. (1972) · PubMed · Cited by 81 · see citing works
The anemia of chronic disease.
Lee, G. R. (1983) · PubMed · Cited by 70 · see citing works
Bissell, D. M., & Guzelian, P. S. (1980) · Journal of Clinical Investigation · doi:10.1172/jci109767 · Cited by 59 · see citing works
Arosa, F. A., Silva, A. J. D., Godinho, I., ter Steege, J. C. A., Porto, G., Rudd, C. E., & de Sousa, M. A. B. (1994) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1994.tb03396.x · Cited by 45 · see citing works
Flagged first, then by citations
Research works printed but not linked: 8
- [7]Zakhary, R., Gaine, S. P., Dinerman, J. L., Ruat, M., Flavahan, N. A. & Snyder, S. H. (1996) Proc. Natl. Acad. Sci. USA 93, 795-798.
- [9]Keyse, S. M. & Tyrrell, R. M. (1989) Proc. Natl. Acad. Sci. USA 86, 99-103.
- [10]Eisenstein, R. S., Garcia-Mayol, D., Pettingell, W. & Munro, H. N. (1991) Proc. Natl. Acad. Sci. USA 88, 688-692.
- [11]Ewing, J. F. & Maines, M. D. (1991) Proc. Natl. Acad. Sci. USA 88, 5364-5368.
- [12]Kutty, R. K., Kutty, G., Wiggert, B., Chader, G. J., Darrow, R. M. & Organisciak, D. T. (1995) Proc. Natl. Acad. Sci. USA 92, 1177-1181.
- [13]Shibahara, S., Muller, R., Taguchi, H. & Yoshida, T. (1985) Proc. Natl. Acad. Sci. USA 82, 7865-7869.
- [16]Hogan, B., Constantini, F. & Lacy, E. (1986) Manipulating the Mouse Embryo (Cold Spring Lab. Press, Plainview, NY).
- [18]Sohal, R. S., Agarwal, S., Dubey, A. & Orr, W. C. (1993) Proc. Natl. Acad. Sci. USA 90, 7255-7259.
Cited by
Sorted by citations
Points of control in inflammation
Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738 · see citing works
Mori, K., Lee, H. T., Rapoport, D., Drexler, I. R., Foster, K., Yang, J., Schmidt-Ott, K. M., Chen, X., Li, J. Y., Weiss, S., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23056 · Cited by 954 · see citing works
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701 · see citing works
Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
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 · see citing works
Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
Ryter, S. W., Otterbein, L. E., Morse, D., & Choi, A. M. K. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015957026924 · Cited by 497 · see citing works
Philippidis, P., Mason, J. C., Evans, B. J., Nadra, I., Taylor, K. M., Haskard, D. O., & Landis, R. C. (2004) · Circulation Research · doi:10.1161/01.res.0000109414.78907.f9 · Cited by 476 · see citing works
Differential regulation of iron homeostasis during human macrophage polarized activation
Recalcati, S., Locati, M., Marini, A., Santambrogio, P., Zaninotto, F., De Pizzol, M., Zammataro, L., Girelli, D., & Cairo, G. (2010) · European Journal of Immunology · doi:10.1002/eji.200939889 · Cited by 438 · see citing works
Heme-mediated SPI-C induction promotes monocyte differentiation into iron-recycling macrophages
Haldar, M., Kohyama, M., So, A. Y.-L., KC, W., Wu, X., Briseño, C. G., Satpathy, A. T., Kretzer, N. M., Arase, H., Rajasekaran, N. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.069 · Cited by 431 · see citing works
Heme oxygenase–1, oxidation, inflammation, and atherosclerosis
Araujo, J. A., Zhang, M., & Yin, F. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00119 · Cited by 443 · see citing works
Macrophages and Iron Metabolism
Soares, M. P., & Hamza, I. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.016 · Cited by 401 · see citing works
Iron in infection and immunity
Nairz, M., & Weiss, G. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100864 · Cited by 359 · see citing works
Hemolysis-induced lethality involves inflammasome activation by heme
Dutra, F. F., Alves, L. S., Rodrigues, D., Fernandez, P. L., de Oliveira, R. B., Golenbock, D. T., Zamboni, D. S., & Bozza, M. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405023111 · Cited by 353 · see citing works
Targeting iron metabolism in drug discovery and delivery
Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352 · see citing works
Iron metabolism in the anemia of chronic disease
Weiss, G. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.08.006 · Cited by 322 · see citing works
Iron trafficking and metabolism in macrophages: contribution to the polarized phenotype.
Cairo, G., Recalcati, S., Mantovani, A., & Locati, M. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.03.007 · Cited by 312 · see citing works
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
Polarization dictates iron handling by inflammatory and alternatively activated macrophages
Corna, G., Campana, L., Pignatti, E., Castiglioni, A., Tagliafico, E., Bosurgi, L., Campanella, A., Brunelli, S., Manfredi, A. A., Apostoli, P., et al. (2010) · Haematologica · doi:10.3324/haematol.2010.023879 · Cited by 304 · see citing works
An overview of molecular basis of iron metabolism regulation and the associated pathologies
Silva, B., & Faustino, P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.011 · Cited by 300 · see citing works
Macrophages and Systemic Iron Homeostasis
Ganz, T. (2012) · Journal of Innate Immunity · doi:10.1159/000336423 · Cited by 281 · see citing works
Iron homeostasis and toxicity in retinal degeneration
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 · see citing works
Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production
Fortes, G. B., Alves, L. S., de Oliveira, R., Dutra, F. F., Rodrigues, D., Fernandez, P. L., Souto-Padron, T., De Rosa, M. J., Kelliher, M., Golenbock, D., et al. (2012) · Blood · doi:10.1182/blood-2011-08-375303 · Cited by 246 · see citing works
Cardioprotective and Antiapoptotic Effects of Heme Oxygenase-1 in the Failing Heart
Wang, G., Hamid, T., Keith, R. J., Zhou, G., Partridge, C. R., Xiang, X., Kingery, J. R., Lewis, R. K., Li, Q., Rokosh, D. G., et al. (2010) · Circulation · doi:10.1161/circulationaha.109.905471 · Cited by 249 · see citing works
Iron and neurodegenerative disorders
Thompson, K. J., Shoham, S., & Connor, J. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00510-x · Cited by 235 · see citing works
Cunnington, A. J., de Souza, J. B., Walther, M., & Riley, E. M. (2012) · Nature Medicine · doi:10.1038/nm.2601 · Cited by 231 · see citing works
The Iron age of host–microbe interactions
Soares, M. P., & Weiss, G. (2015) · The EMBO Reports · doi:10.15252/embr.201540558 · Cited by 227 · see citing works
Macrophages and iron trafficking at the birth and death of red cells
Korolnek, T., & Hamza, I. (2015) · Blood · doi:10.1182/blood-2014-12-567776 · Cited by 196 · see citing works
Iron induces anti-tumor activity in tumor-associated macrophages
Costa da Silva, M., Breckwoldt, M. O., Vinchi, F., Correia, M. P., Stojanovic, A., Thielmann, C. M., Meister, M., Muley, T., Warth, A., Platten, M., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01479 · Cited by 164 · see citing works
The role of iron neurotoxicity in ischemic stroke
Selim, M. H., & Ratan, R. R. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.04.001 · Cited by 158 · see citing works
Interferon‐γ limits the availability of iron for intramacrophage <i>Salmonella typhimurium</i>
Nairz, M., Fritsche, G., Brunner, P., Talasz, H., Hantke, K., & Weiss, G. (2008) · European Journal of Immunology · doi:10.1002/eji.200738056 · Cited by 151 · see citing works
Coupling Heme and Iron Metabolism <i>via</i> Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151 · see citing works
Iron levels in polarized macrophages: regulation of immunity and autoimmunity
Recalcati, S., Locati, M., Gammella, E., Invernizzi, P., & Cairo, G. (2012) · Autoimmunity Reviews · doi:10.1016/j.autrev.2012.03.003 · Cited by 150 · see citing works
Delaby, C., Pilard, N., Puy, H., & Canonne-Hergaux, F. (2008) · Biochemical Journal · doi:10.1042/bj20071474 · Cited by 144 · see citing works
Porto, G. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4707 · Cited by 140 · see citing works
Haemin uptake and use as an iron source by Candida albicans: role of CaHMX1-encoded haem oxygenase
Santos, R., Buisson, N., Knight, S., Dancis, A., Camadro, J.-M., & Lesuisse, E. (2003) · Microbiology · doi:10.1099/mic.0.26108-0 · Cited by 139 · see citing works
Oxidized Hemoglobin Is an Endogenous Proinflammatory Agonist That Targets Vascular Endothelial Cells
Silva, G., Jeney, V., Chora, Â., Larsen, R., Balla, J., & Soares, M. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045344 · Cited by 137 · see citing works
Heme Oxygenase-1 Accelerates Cutaneous Wound Healing in Mice
Grochot-Przeczek, A., Lach, R., Mis, J., Skrzypek, K., Gozdecka, M., Sroczynska, P., Dubiel, M., Rutkowski, A., Kozakowska, M., Zagorska, A., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005803 · Cited by 131 · see citing works
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · see citing works
Zhu, W., Hunt, D. J., Richardson, A. R., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.2.439-447.2000 · Cited by 108 · see citing works
A physiological model to study iron recycling in macrophages
Delaby, C., Pilard, N., Hetet, G., Driss, F., Grandchamp, B., Beaumont, C., & Canonne-Hergaux, F. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.07.002 · Cited by 103 · see citing works
Immunoregulatory effects of HO-1: how does it work?
Soares, M. P., Marguti, I., Cunha, A., & Larsen, R. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.05.008 · Cited by 97 · see citing works
Emerging concepts on the anti-inflammatory actions of carbon monoxide-releasing molecules (CO-RMs)
Motterlini, R., Haas, B., & Foresti, R. (2012) · Medical Gas Research · doi:10.1186/2045-9912-2-28 · Cited by 86 · see citing works
Characterization of nuclear ferritin and mechanism of translocation
SURGULADZE, N., PATTON, S., COZZI, A., FRIED, M. G., & CONNOR, J. R. (2005) · Biochemical Journal · doi:10.1042/bj20041853 · Cited by 81 · see citing works
Like iron in the blood of the people: the requirement for heme trafficking in iron metabolism
Korolnek, T., & Hamza, I. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00126 · Cited by 73 · see citing works
Both Nramp1 and DMT1 are necessary for efficient macrophage iron recycling
Soe-Lin, S., Apte, S. S., Mikhael, M. R., Kayembe, L. K., Nie, G., & Ponka, P. (2010) · Experimental Hematology · doi:10.1016/j.exphem.2010.04.003 · Cited by 69 · see citing works
Cytoprotective Effects of Heme Oxygenase in Acute Renal Failure
Akagi, R., Takahashi, T., & Sassa, S. (2005) · Contributions to Nephrology · doi:10.1159/000086044 · Cited by 53 · see citing works
Fraser, S. T., Midwinter, R. G., Coupland, L. A., Kong, S., Berger, B. S., Yeo, J. H., Andrade, O. C., Cromer, D., Suarna, C., Lam, M., et al. (2015) · Haematologica · doi:10.3324/haematol.2014.116368 · Cited by 50 · see citing works
Heme oxygenase-1 promotes granuloma development and protects against dissemination of mycobacteria
Regev, D., Surolia, R., Karki, S., Zolak, J., Montes- Worboys, A., Oliva, O., Guroji, P., Saini, V., Steyn, A. J., Agarwal, A., et al. (2012) · Laboratory Investigation · doi:10.1038/labinvest.2012.125 · Cited by 44 · see citing works
Gill, A. J., Garza, R., Ambegaokar, S. S., Gelman, B. B., & Kolson, D. L. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1102-z · Cited by 37 · see citing works
Weissman, Z., Pinsky, M., Donegan, R. K., Reddi, A. R., & Kornitzer, D. (2020) · doi:10.1101/2020.07.26.221606 · Cited by 26 · see citing works
- Authors
- Poss, K. D., & Tonegawa, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1997-09-30
- Volume
- 94
- Issue
- 20
- Pages
- 10919-10924
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC23531
- OpenAlex
- W2067714284
- Cited by
- 1,016
- References
- 29
- Citations by year
- 2026: 11 · 2025: 26 · 2024: 23 · 2023: 29 · 2022: 28 · 2021: 37 · 2020: 40 · 2019: 31 · 2018: 31 · 2017: 24 · 2016: 23 · 2015: 32 · 2014: 43 · 2013: 32 · 2012: 52
- FWCI
- 11.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01-NS32925-03, R01NS032925)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- heme oxygenase-1, iron homeostasis, iron recycling, anemia, serum iron, hepatic iron deposition, oxidative damage, chronic inflammation, erythropoiesis, heme degradation
- MeSH terms
- Anemia, Animals, Female, Heme Oxygenase (Decyclizing), Homeostasis, Iron, Male, Mice, Inbred C57BL, Mutation, Oxidative Stress, Gene Targeting, Mice
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