Cited by 187Erythropoietin and Anemia TreatmentIron Metabolism and DisordersHemoglobin structure and function

The DOI matches its Crossref record; 143 of the 145 references it cites were found in a registry or an index.

Hypoxia-Inducible Factors Link Iron Homeostasis and Erythropoiesis

Open access

Shah, Yatrik M., Xie, Liwei·2014·Gastroenterology

DOI 10.1053/j.gastro.2013.12.031PMC PMC3943938

Open this paper in CoChat — free account Open PDF

Abstract

Iron is required for efficient oxygen transport, and hypoxia signaling links erythropoiesis with iron homeostasis. Hypoxia induces a highly conserved signaling pathway in cells under conditions of low levels of O2. One component of this pathway, hypoxia-inducible factor (HIF), is a transcription factor that is highly active in hypoxic cells. The first HIF target gene characterized was EPO, which encodes erythropoietin-a glycoprotein hormone that controls erythropoiesis. In the past decade, there have been fundamental advances in our understanding of how hypoxia regulates iron levels to support erythropoiesis and maintain systemic iron homeostasis. We review the cell type-specific effects of hypoxia and HIFs in adaptive response to changes in oxygen and iron availability as well as potential uses of HIF modulators for patients with iron-related 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

Crossref · 10.1053/j.gastro.2013.12.031

Cites

143 of 143 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212
Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
Forsythe, J. A., Jiang, B.-H., Iyer, N. V., Agani, F., Leung, S. W., Koos, R. D., & Semenza, G. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4604 · Cited by 3,981
C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650
A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
A conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168
A New Mouse Liver-specific Gene, Encoding a Protein Homologous to Human Antimicrobial Peptide Hepcidin, Is Overexpressed during Iron Overload
Pigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., Brissot, P., & Loréal, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008923200 · Cited by 1,697
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422
The impact of O2 availability on human cancer
Bertout, J. A., Patel, S. A., & Simon, M. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2540 · Cited by 1,365
Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis
Perutz, M. F., Rossmann, M. G., Cullis, A. F., Muirhead, H., Will, G., & North, A. C. T. (1960) · Nature · doi:10.1038/185416a0 · Cited by 1,351
Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells.
Tian, H., McKnight, S. L., & Russell, D. W. (1997) · Genes & Development · doi:10.1101/gad.11.1.72 · Cited by 1,351
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324
Hepcidin and iron homeostasis
Ganz, T., & Nemeth, E. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.014 · Cited by 1,282
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267
Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 ( USF2 ) knockout mice
Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233
The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159
An iron-regulated ferric reductase associated with the absorption of dietary iron
McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101
Purification of human erythropoietin.
Miyake, T., Kung, C. K.-H., & Goldwasser, E. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63387-9 · Cited by 895
Distribution of hematopoietic stem cells in the bone marrow according to regional hypoxia
Parmar, K., Mauch, P., Vergilio, J.-A., Sackstein, R., & Down, J. D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701152104 · Cited by 867
Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia.
Wang, G. L., & Semenza, G. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80571-7 · Cited by 863
Role of the kidney in erythropoiesis
JACOBSON, L. O., GOLDWASSER, E., FRIED, W., & PLZAK, L. (1957) · Nature · doi:10.1038/179633a0 · Cited by 862
High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854
Identification of an Intestinal Folate Transporter and the Molecular Basis for Hereditary Folate Malabsorption
Qiu, A., Jansen, M., Sakaris, A., Min, S. H., Chattopadhyay, S., Tsai, E., Sandoval, C., Zhao, R., Akabas, M. H., & Goldman, I. D. (2006) · Cell · doi:10.1016/j.cell.2006.09.041 · Cited by 847
An essential role for p300/CBP in the cellular response to hypoxia
Arany, Z., Huang, L. E., Eckner, R., Bhattacharya, S., Jiang, C., Goldberg, M. A., Bunn, H. F., & Livingston, D. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12969 · Cited by 790
Regulation of erythropoiesis by hypoxia-inducible factors
Haase, V. H. (2013) · Blood Reviews · doi:10.1016/j.blre.2012.12.003 · Cited by 787
Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT
Maltepe, E., Schmidt, J. V., Baunoch, D., Bradfield, C. A., & Simon, M. C. (1997) · Nature · doi:10.1038/386403a0 · Cited by 781
Desferrioxamine induces erythropoietin gene expression and hypoxia- inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction
Wang, G., & Semenza, G. (1993) · Blood · doi:10.1182/blood.v82.12.3610.3610 · Cited by 766
Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
Makino, Y., Cao, R., Svensson, K., Bertilsson, G., Asman, M., Tanaka, H., Cao, Y., Berkenstam, A., & Poellinger, L. (2001) · Nature · doi:10.1038/35107085 · Cited by 705
Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701
Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA)
Finberg, K. E., Heeney, M. M., Campagna, D. R., Aydınok, Y., Pearson, H. A., Hartman, K. R., Mayo, M. M., Samuel, S. M., Strouse, J. J., Markianos, K., et al. (2008) · Nature Genetics · doi:10.1038/ng.130 · Cited by 675
The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
Tian, H., Hammer, R. E., Matsumoto, A. M., Russell, D. W., & McKnight, S. L. (1998) · Genes & Development · doi:10.1101/gad.12.21.3320 · Cited by 647
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601
Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
Rankin, E. B., Biju, M. P., Liu, Q., Unger, T. L., Rha, J., Johnson, R. S., Simon, M. C., Keith, B., & Haase, V. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30117 · Cited by 596
The serine protease TMPRSS6 is required to sense iron deficiency
Du, X., She, E., Gelbart, T., Truksa, J., Lee, P., Xia, Y., Khovananth, K., Mudd, S., Mann, N., Moresco, E. M. Y., et al. (2008) · Science · doi:10.1126/science.1157121 · Cited by 578
The Serine Protease Matriptase-2 (TMPRSS6) Inhibits Hepcidin Activation by Cleaving Membrane Hemojuvelin
Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., & Camaschella, C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.012 · Cited by 555
Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia
Ang, S. O., Chen, H., Hirota, K., Gordeuk, V. R., Jelinek, J., Guan, Y., Liu, E., Sergueeva, A. I., Miasnikova, G. Y., Mole, D., et al. (2002) · Nature Genetics · doi:10.1038/ng1019 · Cited by 510
Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509
HIF-2α, but not HIF-1α, promotes iron absorption in mice
Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502
Hypoxemia in patients with COPD: cause, effects, and disease progression
McNicholas, W. T., Kent, & Mitchell (2011) · International Journal of COPD · doi:10.2147/copd.s10611 · Cited by 479
The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation
De Domenico, I., Ward, D. M., Langelier, C., Vaughn, M. B., Nemeth, E., Sundquist, W. I., Ganz, T., Musci, G., & Kaplan, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0060 · Cited by 434
Intestinal Hypoxia-Inducible Transcription Factors Are Essential for Iron Absorption following Iron Deficiency
Shah, Y. M., Matsubara, T., Ito, S., Yim, S.-H., & Gonzalez, F. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.012 · Cited by 431
Self-citation
Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
Schofield, C. J., & Zhang, Z. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00036-6 · Cited by 408
Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis.
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408
Cellular oxygen sensing by mitochondria: old questions, new insight
Chandel, N. S., & Schumacker, P. T. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.5.1880 · Cited by 389
Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice
Gnarra, J. R., Ward, J. M., Porter, F. D., WAGNER, J. R., Devor, D. E., Grinberg, A., Emmert‐Buck, M. R., Westphal, H., Klausner, R. D., & Linehan, W. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9102 · Cited by 366
Iron Sequestration and Anemia of Inflammation
Ganz, T., & Nemeth, E. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.001 · Cited by 361
Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells
Tanno, T., Porayette, P., Sripichai, O., Noh, S.-J., Byrnes, C., Bhupatiraju, A., Lee, Y. T., Goodnough, J. B., Harandi, O., Ganz, T., et al. (2009) · Blood · doi:10.1182/blood-2008-12-195503 · Cited by 352
Hemoglobin Variants: Biochemical Properties and Clinical Correlates
Thom, C. S., Dickson, C. F., Gell, D. A., & Weiss, M. J. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011858 · Cited by 336
A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis
Percy, M. J., Zhao, Q., Flores, A., Harrison, C., Lappin, T. R. J., Maxwell, P. H., McMullin, M. F., & Lee, F. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508423103 · Cited by 330
Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis
Liu, Q., Davidoff, O., Niss, K., & Haase, V. H. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63924 · Cited by 328
An oxygen-regulated switch in the protein synthesis machinery
Uniacke, J., Holterman, C. E., Lachance, G., Franovic, A., Jacob, M. D., Fabian, M. R., Payette, J., Holcik, M., Pause, A., & Lee, S. (2012) · Nature · doi:10.1038/nature11055 · Cited by 319
The Human Nramp2 Gene: Characterization of the Gene Structure, Alternative Splicing, Promoter Region and Polymorphisms
Lee, P. L., Gelbart, T., West, C., Halloran, C., & Beutler, E. (1998) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.1998.0186 · Cited by 318
Allosteric inhibition of hypoxia inducible factor-2 with small molecules
Scheuermann, T. H., Li, Q., Ma, H.-W., Key, J., Zhang, L., Chen, R., Garcia, J. A., Naidoo, J., Longgood, J., Frantz, D. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1185 · Cited by 315
A Gain-of-Function Mutation in the HIF2A Gene in Familial Erythrocytosis
Percy, M. J., Furlow, P. W., Lucas, G. S., Li, X., Lappin, T. R. J., McMullin, M. F., & Lee, F. S. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa073123 · Cited by 314
Hepatic HIF-2 regulates erythropoietic responses to hypoxia in renal anemia
Kapitsinou, P. P., Liu, Q., Unger, T. L., Rha, J., Davidoff, O., Keith, B., Epstein, J. A., Moores, S. L., Erickson-Miller, C. L., & Haase, V. H. (2010) · Blood · doi:10.1182/blood-2010-02-270322 · Cited by 307
Artificial ligand binding within the HIF2α PAS-B domain of the HIF2 transcription factor
Scheuermann, T. H., Tomchick, D. R., Machius, M., Guo, Y., Bruick, R. K., & Gardner, K. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808092106 · Cited by 301
Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287
The HIF Signaling Pathway in Osteoblasts Directly Modulates Erythropoiesis through the Production of EPO
Rankin, E. B., Wu, C., Khatri, R., Wilson, T. L. S., Andersen, R., Araldi, E., Rankin, A. L., Yuan, J., Kuo, C. J., Schipani, E., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.051 · Cited by 286
A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281
Macrophages and Systemic Iron Homeostasis
Ganz, T. (2012) · Journal of Innate Immunity · doi:10.1159/000336423 · Cited by 281
Hypoxic but not anoxic stabilization of HIF-1α requires mitochondrial reactive oxygen species
Schroedl, C., McClintock, D. S., Budinger, G. R. S., & Chandel, N. S. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00014.2002 · Cited by 266
Hypoxia-Inducible Factor-2α Mediates the Adaptive Increase of Intestinal Ferroportin During Iron Deficiency in Mice
Taylor, M., Qu, A., Anderson, E. R., Matsubara, T., Martin, A., Gonzalez, F. J., & Shah, Y. M. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.007 · Cited by 265
Self-citation
Iron Homeostasis in the Liver
Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 262
Self-citation
Targeted disruption of the hepcidin 1 gene results in severe hemochromatosis
Lesbordes-Brion, J.-C., Viatte, L., Bennoun, M., Lou, D.-Q., Ramey, G., Houbron, C., Hamard, G., Kahn, A., & Vaulont, S. (2006) · Blood · doi:10.1182/blood-2006-02-003376 · Cited by 257
Cell-type-specific and hypoxia-inducible expression of the human erythropoietin gene in transgenic mice.
Semenza, G. L., Koury, S. T., Nejfelt, M. K., Gearhart, J. D., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8725 · Cited by 248
Positioning of bone marrow hematopoietic and stromal cells relative to blood flow in vivo: serially reconstituting hematopoietic stem cells reside in distinct nonperfused niches
Winkler, I. G., Barbier, V., Wadley, R. B., Zannettino, A. C. W., Williams, S., & Lévesque, J.-P. (2010) · Blood · doi:10.1182/blood-2009-07-233437 · Cited by 246
Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPα
Pinto, J. P., Ribeiro, S., Pontes, H., Thowfeequ, S., Tosh, D., Carvalho, F. D., & Porto, G. (2008) · Blood · doi:10.1182/blood-2007-08-106195 · Cited by 239
HIF-2α regulates murine hematopoietic development in an erythropoietin-dependent manner
Scortegagna, M., Ding, K., Zhang, Q., Oktay, Y., Bennett, M. J., Bennett, M., Shelton, J. M., Richardson, J. A., Moe, O. W., & Garcia, J. A. (2004) · Blood · doi:10.1182/blood-2004-05-1695 · Cited by 237
Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
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
Erythropoietin.
Bunn, H. F. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011619 · Cited by 234
Reducing TMPRSS6 ameliorates hemochromatosis and β-thalassemia in mice
Guo, S., Casu, C., Gardenghi, S., Booten, S. L., Aghajan, M., Peralta, R. Q., Watt, A., Freier, S., Monia, B. P., & Rivella, S. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66969 · Cited by 233
Hepcidin as a therapeutic tool to limit iron overload and improve anemia in β-thalassemic mice
Gardenghi, S., Ramos, P., Marongiu, M. F., Melchiori, L., Breda, L., Guy, E., Muirhead, K., Rao, N., Roy, C. N., Andrews, N. C., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41717 · Cited by 220
In vitro hematopoietic and endothelial potential of flk-1 −/− embryonic stem cells and embryos
Schuh, A. C., Faloon, P. W., Hu, Q., Bhimani, M., & Choi, K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2159 · Cited by 216
The IRP1-HIF-2α Axis Coordinates Iron and Oxygen Sensing with Erythropoiesis and Iron Absorption
Anderson, S. A., Nizzi, C. P., Chang, Y.-I., Deck, K. M., Schmidt, P. J., Galy, B., Damnernsawad, A., Broman, A. T., Kendziorski, C., Hentze, M. W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.007 · Cited by 211
The HIF family member EPAS1/HIF-2α is required for normal hematopoiesis in mice
Scortegagna, M., Morris, M. A., Oktay, Y., Bennett, M., & Garcia, J. A. (2003) · Blood · doi:10.1182/blood-2003-02-0448 · Cited by 208
Enhancer element at the 3'-flanking region controls transcriptional response to hypoxia in the human erythropoietin gene
Beck, I., Ramirez, S., Weinmann, R. S., & Caro, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98438-3 · Cited by 206
Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing
Zimmer, M., Ebert, B. L., Neil, C., Brenner, K., Papaioannou, I., Melas, A., Tolliday, N., Lamb, J., Pantopoulos, K., Golub, T., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.004 · Cited by 191
Multilineage embryonic hematopoiesis requires hypoxic ARNT activity
Adelman, D. M., Maltepe, E., & Simon, M. C. (1999) · Genes & Development · doi:10.1101/gad.13.19.2478 · Cited by 185
Hepatic hypoxia-inducible factor-2 down-regulates hepcidin expression in mice through an erythropoietin-mediated increase in erythropoiesis
Mastrogiannaki, M., Matak, P., Mathieu, J. R. R., Delga, S., Mayeux, P., Vaulont, S., & Peyssonnaux, C. (2011) · Haematologica · doi:10.3324/haematol.2011.056119 · Cited by 171
Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis
Finberg, K. E., Whittlesey, R. L., Fleming, M. D., & Andrews, N. C. (2010) · Blood · doi:10.1182/blood-2009-05-224808 · Cited by 167
Reactivation of hepatic EPO synthesis in mice after PHD loss
Minamishima, Y. A., & Kaelin, W. G. (2010) · Science · doi:10.1126/science.1192811 · Cited by 163
Modulation of hepcidin production during hypoxia-induced erythropoiesis in humans in vivo: data from the HIGHCARE project
Piperno, A., Galimberti, S., Mariani, R., Pelucchi, S., Ravasi, G., Lombardi, C., Bilo, G., Revera, M., Giuliano, A., Faini, A., et al. (2011) · Blood · doi:10.1182/blood-2010-08-299859 · Cited by 151
The VHL tumor suppressor and HIF: insights from genetic studies in mice
Kapitsinou, P. P., & Haase, V. H. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402313 · Cited by 151
Hypoxia-Inducible Factor-2α Activation Promotes Colorectal Cancer Progression by Dysregulating Iron Homeostasis
Xue, X., Taylor, M. J., Anderson, E. R., Hao, C., Qu, A., Greenson, J. K., Zimmermann, E. M., Gonzalez, F. J., & Shah, Y. M. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3836 · Cited by 147
Self-citation
Growth differentiation factor 15 in erythroid health and disease
Tanno, T., Noel, P., & Miller, J. L. (2010) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328337b52f · Cited by 139
IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2α mRNA translation
Wilkinson, N., & Pantopoulos, K. (2013) · Blood · doi:10.1182/blood-2013-03-492454 · Cited by 136
Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins
Sánchez, M., Galy, B., Schwanhaeusser, B., Blake, J., Bähr-Ivacevic, T., Beneš, V., Selbach, M., Muckenthaler, M. U., & Hentze, M. W. (2011) · Blood · doi:10.1182/blood-2011-04-343541 · Cited by 132
Molecular basis of hypoxia-induced erythropoietin expression
Wang, G. L., & Semenza, G. L. (1996) · Current Opinion in Hematology · doi:10.1097/00062752-199603020-00009 · Cited by 131
Novel exon 12 mutations in the HIF2A gene associated with erythrocytosis
Percy, M. J., Beer, P. A., Campbell, G., Dekker, A. W., Green, A. R., Oscier, D., Rainey, M. G., van Wijk, R., Wood, M., Lappin, T. R. J., et al. (2008) · Blood · doi:10.1182/blood-2008-02-137703 · Cited by 127
Prolyl 4‐hydroxylases, master regulators of the hypoxia response
Myllyharju, J. (2013) · Acta Physiologica · doi:10.1111/apha.12096 · Cited by 123
Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
Smith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123
Human erythropoietin gene expression in transgenic mice: multiple transcription initiation sites and cis-acting regulatory elements.
Semenza, G. L., Dureza, R. C., Traystman, M. D., Gearhart, J. D., & Antonarakis, S. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.3.930 · Cited by 119
Iron deficiency anaemia
Liu, K., & Kaffes, A. J. (2011) · European Journal of Gastroenterology & Hepatology · doi:10.1097/meg.0b013e32834f3140 · Cited by 118
Erythrocytosis Secondary to Increased Oxygen Affinity of a Mutant Hemoglobin, Hemoglobin Kempsey
Reed, C., Hampson, R., Gordon, S., Jones, R. T., Novy, M. J., Brimhall, B., Edwards, M. J., & Koler, R. D. (1968) · Blood · doi:10.1182/blood.v31.5.623.623 · Cited by 116
The classification and diagnosis of erythrocytosis
McMullin, M. F. (2008) · International Journal of Laboratory Hematology · doi:10.1111/j.1751-553x.2008.01102.x · Cited by 115
Recent advances in mammalian haem transport
Latunde-Dada, G. O., Simpson, R. J., & McKie, A. T. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.005 · Cited by 113
Mechanisms of iron mediated regulation of the duodenal iron transporters divalent metal transporter 1 and ferroportin 1
Zoller, H., Theurl, I., Koch, R., Kaser, A., & Weiss, G. (2002) · Blood Cells, Molecules, and Diseases · doi:10.1006/bcmd.2002.0587 · Cited by 106
The glial cell response is an essential component of hypoxia-induced erythropoiesis in mice
Weidemann, A., Kerdiles, Y. M., Knaup, K. X., Rafie, C. A., Boutin, A. T., Stockmann, C., Takeda, N., Scadeng, M., Shih, A. Y., Haase, V. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39378 · Cited by 105
Intestinal HIF2α promotes tissue-iron accumulation in disorders of iron overload with anemia
Anderson, E. R., Taylor, M. J., Xue, X., Ramakrishnan, S. K., Martin, A. S., Xie, L., Bredell, B. X., Gardenghi, S., Rivella, S., & Shah, Y. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314197110 · Cited by 101
Self-citation
H+-Coupled Divalent Metal-Ion Transporter-1
Shawki, A., Knight, P. B., Maliken, B. D., Niespodzany, E. J., & Mackenzie, B. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394316-3.00005-3 · Cited by 100
Hif-2α is not essential for cell-autonomous hematopoietic stem cell maintenance
Guitart, A. V., Subramani, C., Armesilla-Diaz, A., Smith, G., Sepúlveda, C., Gezer, D., Vukovic, M., Dunn, K. M., Pollard, P. J., Holyoake, T. L., et al. (2013) · Blood · doi:10.1182/blood-2013-02-484923 · Cited by 94
Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors
Volke, M., Gale, D. P., Maegdefrau, U., Schley, G., Klanke, B., Bosserhoff, A.-K., Maxwell, P. H., Eckardt, K.-U., & Warnecke, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007875 · Cited by 93
CHRONIC HYPOXAEMIA AND DECOMPENSATED ERYTHROCYTOSIS IN CYANOTIC CONGENITAL HEART DISEASE
Rosove, M., Perloff, J. K., Hocking, W. G., CHILD, J. S., Canobbio, M. M., & Skorton, D. (1986) · The Lancet · doi:10.1016/s0140-6736(86)90005-x · Cited by 90
Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: small molecule-based therapeutics for anemia
Yan, L. Y., Colandrea, V. J., & Hale, J. J. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.510836 · Cited by 87
Mechanism of Cooperative Oxygen Binding to Hemoglobin
Ogata, R. T., & McConnell, H. M. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.2.335 · Cited by 82
Chronic hepcidin induction causes hyposideremia and alters the pattern of cellular iron accumulation in hemochromatotic mice
Viatte, L. (2005) · Blood · doi:10.1182/blood-2005-10-4071 · Cited by 81
Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles
Myllyharju, J., & Koivunen, P. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0328 · Cited by 80
The Treatment of Secondary Hemochromatosis
Gattermann, N. (2009) · Deutsches Ärzteblatt international · doi:10.3238/arztebl.2009.0499 · Cited by 78
Haem carrier protein 1 (HCP1): Expression and functional studies in cultured cells
Latunde-Dada, G. O., Takeuchi, K., Simpson, R. J., & McKie, A. T. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.048 · Cited by 77
Structure of hemoglobin.
Perutz, M. F. (1960) · PubMed · Cited by 74
Regulation of systemic iron homeostasis
Finberg, K. E. (2013) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32835f5a47 · Cited by 72
Structure and function of transferrin.
Aisen, P., & BROWN, E. B. (1975) · PubMed · Cited by 71
2-Oxoglutarate-dependent oxygenases control hepcidin gene expression
Braliou, G. G., Falzacappa, M. V. V., Chachami, G., Casanovas, G., Muckenthaler, M. U., & Simos, G. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2007.12.021 · Cited by 68
Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression
Leung, P. S. (2005) · Gut · doi:10.1136/gut.2004.062083 · Cited by 64
Cerebral atrophy in drug addicts.
von Zerssen, D., Fliege, K., & Wolf, M. (1970) · PubMed · Cited by 59
Intestinal Hypoxia-inducible Factor-2α (HIF-2α) Is Critical for Efficient Erythropoiesis
Anderson, E. R., Xue, X., & Shah, Y. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.238667 · Cited by 58
Self-citation
Deletion of HIF-2α in the enterocytes decreases the severity of tissue iron loading in hepcidin knockout mice
Mastrogiannaki, M., Matak, P., Delga, S., Deschemin, J.-C., Vaulont, S., & Peyssonnaux, C. (2012) · Blood · doi:10.1182/blood-2011-09-380337 · Cited by 57
Diagnosis and treatment of hereditary hemochromatosis: an update
Kanwar, P., & Kowdley, K. V. (2013) · Expert Review of Gastroenterology & Hepatology · doi:10.1586/17474124.2013.816114 · Cited by 57
Hypoxia inhibits hepcidin expression in HuH7 hepatoma cells via decreased SMAD4 signaling
Chaston, T. B., Matak, P., Pourvali, K., Srai, S. K., McKie, A. T., & Sharp, P. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00121.2010 · Cited by 55
Generation of conditional alleles of the murine iron regulatory protein (IRP)‐1 and ‐2 genes
Galy, B., Ferring–Appel, D., & Hentze, M. W. (2005) · genesis · doi:10.1002/gene.20169 · Cited by 54
Chuvash polycythemia VHLR200W mutation is associated with down-regulation of hepcidin expression
Gordeuk, V. R., Miasnikova, G. Y., Sergueeva, A. I., Niu, X., Nouraie, M., Okhotin, D. J., Polyakova, L. A., Ammosova, T., Nekhai, S., Ganz, T., et al. (2011) · Blood · doi:10.1182/blood-2011-03-345512 · Cited by 51
Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF–Prolyl 4-Hydroxylases for Treatment of Ischemic Diseases
Selvaraju, V., Parinandi, N. L., Adluri, R. S., Goldman, J. W., Hussain, N., Sánchez, J. A., & Maulik, N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5186 · Cited by 44
The Hypoxia-Inducible Factor–C/EBPα Axis Controls Ethanol-Mediated Hepcidin Repression
Anderson, E. R., Taylor, M. J., Xue, X., Martin, A. S., Moons, D. S., Omary, M. B., & Shah, Y. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00723-12 · Cited by 43
Self-citation
Subunit dissociation of certain abnormal human hemoglobins
Bunn, H. F. (1969) · Journal of Clinical Investigation · doi:10.1172/jci105961 · Cited by 31
Hypoxia Inducible Factor-2a Is Translationally Repressed in Response to Dietary Iron Deficiency in Sprague-Dawley Rats
Davis, M. R., Shawron, K., Rendina-Ruedy, E., Peterson, S., Lucas, E. A., Smith, B. J., & Clarke, S. L. (2011) · Journal of Nutrition · doi:10.3945/jn.111.144105 · Cited by 30
Plasma hepcidin of Ethiopian highlanders with steady-state hypoxia
Lundgrin, E. L., Janocha, A. J., Koch, C. D., Gebremedhin, A., Rienzo, A. D., Alkorta‐Aranburu, G., Brittenham, G. M., ERZURUM, S. C., & Beall, C. M. (2013) · Blood · doi:10.1182/blood-2013-03-491068 · Cited by 30
Increased susceptibility to iron deficiency of Tmprss6-haploinsufficient mice
Nai, A., Pagani, A., Silvestri, L., & Camaschella, C. (2010) · Blood · doi:10.1182/blood-2010-04-278655 · Cited by 27
Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.
Perutz, M. F., Fermi, G., & Shih, T. ‐. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.15.4781 · Cited by 27
Cloning and Characterization of TMPRSS6, a Novel Type 2 Transmembrane Serine Protease
Park, T. J., Lee, Y. J., Kim, H. J., Park, H. G., & Park, W. J. (2005) · Molecules and Cells · doi:10.1016/s1016-8478(23)13160-8 · Cited by 15
[2] Detection of oxygen-sensing properties of mitochondria
Chandel, N. S. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)52004-8 · Cited by 4

Sorted by citations

Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 960
Iron homeostasis during pregnancy
Fisher, A. L., & Nemeth, E. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155812 · Cited by 432
Oxygen battle in the gut: Hypoxia and hypoxia-inducible factors in metabolic and inflammatory responses in the intestine
Singhal, R., & Shah, Y. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011188 · Cited by 401
Self-citation
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
The physiological functions of iron regulatory proteins in iron homeostasis - an update
Zhang, D., Ghosh, M. C., & Rouault, T. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00124 · Cited by 310

See all 187

Authors: Shah, Y. M., & Xie, L.
Affiliations: University of Michigan (US)
Corresponding author: Shah, Yatrik M.
ORCID: Shah, Yatrik M.
Xie, Liwei
Venue: Gastroenterology
Publisher: Elsevier BV
Published: 2014-03
Volume: 146
Issue: 3
Pages: 630-642
ISSN: 0016-5085 (ISSN-L)
DOI: 10.1053/j.gastro.2013.12.031
PMC: PMC3943938
OpenAlex: W2168760727
Cited by: 187
References: 145
Citations by year: 2026: 18 · 2025: 14 · 2024: 23 · 2023: 19 · 2022: 22 · 2021: 22 · 2020: 15 · 2019: 12 · 2018: 11 · 2017: 9 · 2016: 7 · 2015: 11 · 2014: 4
FWCI: 1.58
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Gastroenterology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: University of Michigan
National Institutes of Health
University of Michigan Comprehensive Cancer Center
National Cancer Institute (CA148828, R01CA148828)
National Institute of Diabetes and Digestive and Kidney Diseases (DK-095201, R01DK095201)
Topics: Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords: hypoxia-inducible factor, iron homeostasis, erythropoiesis, erythropoietin, hypoxia signaling, oxygen availability
MeSH terms: Endothelial PAS Domain-Containing Protein 1, Hypoxia, Erythropoiesis, Erythropoietin, Homeostasis, Humans, Iron, Liver, Oxygen, Signal Transduction, Basic Helix-Loop-Helix Proteins, Hypoxia-Inducible Factor 1

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

Hypoxia-Inducible Factors Link Iron Homeostasis and Erythropoiesis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks