The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells
Abstract
IRON IS INDISPENSABLE for life, serving as metal cofactor for many enzymes, either nonheme or hemoproteins. In the latter, iron is inserted like a gem in the center of the heme prosthetic group. Hemoproteins are involved in a broad spectrum of crucial biologic functions including oxygen binding (
Overview
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
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[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
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
Regulating the fate of mRNA: the control of cellular iron metabolism
Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210
Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation
Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709
Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.
Aziz, N., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8478 · Cited by 368
Regulation of synthesis and turnover of ferritin in rat liver
Drysdale, J. W., & Munro, H. N. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99877-7 · Cited by 326
Craven, C. M., Alexander, J., Eldridge, M., Kushner, J. P., Bernstein, S., & Kaplan, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3457 · Cited by 259
Hentze, M. W., Rouault, T. A., Caughman, S. W., Dancis, A., Harford, J. B., & Klausner, R. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6730 · Cited by 249
Taketani, S., Kohno, H., Furukawa, T., & Tokunaga, R. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124790 · Cited by 123
Regulation of 5-aminolevulinate synthase mRNA in different rat tissues.
Srivastava, G., Borthwick, I. A., Maguire, D. J., Elferink, C. J., Bawden, M. J., Mercer, J. F., & May, B. K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60700-8 · Cited by 107
Cited by
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
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
Papanikolaou, G., & Pantopoulos, K. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.06.021 · Cited by 1,070
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775
The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer
Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721
Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536
Self-citationKell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518
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
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400
Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399
The IRP/IRE system in vivo: insights from mouse models
Wilkinson, N., & Pantopoulos, K. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00176 · Cited by 366
Identification of a hypoxia response element in the transferrin receptor gene
Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380
Transferrin Receptor Induction by Hypoxia
Tacchini, L., Bianchi, L., Bernelli-Zazzera, A., & Cairo, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24142 · Cited by 379
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352
Anaemia in kidney disease: harnessing hypoxia responses for therapy
Koury, M. J., & Haase, V. H. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.82 · Cited by 313
The biochemistry of heme biosynthesis
Heinemann, I. U., Jahn, M., & Jahn, D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.02.015 · Cited by 311
Camaschella, C., Campanella, A., De Falco, L., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., & Iolascon, A. (2007) · Blood · doi:10.1182/blood-2007-02-072520 · Cited by 306
Tsiftsoglou, A. S., Tsamadou, A. I., & Papadopoulou, L. C. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.10.017 · Cited by 281
The Yeast Frataxin Homologue Mediates Mitochondrial Iron Efflux
Radisky, D. C., Babcock, M. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4497 · Cited by 277
Design of clinically useful iron(III)‐selective chelators
Liu, Z. D., & Hider, R. C. (2002) · Medicinal Research Reviews · doi:10.1002/med.1027 · Cited by 266
Oxidative Stress and the Homeodynamics of Iron Metabolism
Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247
Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235
Iron use for haeme synthesis is under control of the yeast frataxin homologue (Yfh1)
Lesuisse, E. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg096 · Cited by 226
The iron metabolism of neoplastic cells: Alterations that facilitate proliferation?
Kwok, J. C., & Richardson, D. R. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00213-x · Cited by 215
Guo, W., Bachman, E., Li, M., Roy, C. N., Blusztajn, J., Wong, S., Chan, S. Y., Serra, C., Jasuja, R., Travison, T. G., et al. (2013) · Aging Cell · doi:10.1111/acel.12052 · Cited by 192
HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
Bianchi, L., Tacchini, L., & Cairo, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.21.4223 · Cited by 189
PONKA, P. (1999) · The American Journal of the Medical Sciences · doi:10.1097/00000441-199910000-00004 · Cited by 182
Self-citationMitochondrial Ferritin: A New Player in Iron Metabolism
Drysdale, J., Arosio, P., Invernizzi, R., Cazzola, M., Volz, A., Corsi, B., Biasiotto, G., & Levi, S. (2002) · Blood Cells, Molecules, and Diseases · doi:10.1006/bcmd.2002.0577 · Cited by 180
Canonne-Hergaux, F., Zhang, A.-S., Ponka, P., & Gros, P. (2001) · Blood · doi:10.1182/blood.v98.13.3823 · Cited by 169
Self-citationCampanella, A. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh232 · Cited by 109
Heme and FLVCR-related transporter families SLC48 and SLC49
Khan, A. A., & Quigley, J. G. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.07.013 · Cited by 105
Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease
Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103
Iron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74
Friedreich's Ataxia, No Changes in Mitochondrial Labile Iron in Human Lymphoblasts and Fibroblasts
Sturm, B., Bistrich, U., Schranzhofer, M., Sarsero, J. P., Rauen, U., Scheiber-Mojdehkar, B., de Groot, H., Ioannou, P., & Petrat, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408717200 · Cited by 73
Frataxin: its role in iron metabolism and the pathogenesis of Friedreich's ataxia
Becker, E., & Richardson, D. R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00067-4 · Cited by 71
Nitric oxide blocks cellular heme insertion into a broad range of heme proteins
Waheed, S. M., Ghosh, A., Chakravarti, R., Biswas, A., Haque, M. M., Panda, K., & Stuehr, D. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.038 · Cited by 62
Silencing of ALA dehydratase affects ALA-photodynamic therapy efficacy in K562 erythroleukemic cells
Feuerstein, T., Schauder, A., & Malik, Z. (2009) · Photochemical & Photobiological Sciences · doi:10.1039/b9pp00007k · Cited by 19
Ghosh, A., & Stuehr, D. J. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6690 · Cited by 19
Dietary and Sentinel Factors Leading to Hemochromatosis
Oh, C.-K., & Moon, Y. (2019) · Nutrients · doi:10.3390/nu11051047 · Cited by 12
Metadata
- Authors
- Ponka, P.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1997-01-01
- Volume
- 89
- Issue
- 1
- Pages
- 1-25
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W77625167
- Cited by
- 552
- References
- 12
- FWCI
- 12.96
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.