Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617

Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation

Ganz, T. (2003) · Blood · doi:10.1182/blood-2003-03-0672 · Cited by 1,544

HIF-1 and mechanisms of hypoxia sensing

Semenza, G. L. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00194-0 · Cited by 1,301

Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression

Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026

Mutations in HFE2 cause iron overload in chromosome 1q–linked juvenile hemochromatosis

Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L. E., Franchini, P. L., Dubé, M.-P., Andres, L., MacFarlane, J., Sakellaropoulos, N., Politou, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1274 · Cited by 974

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

ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins

Puntervoll, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg545 · Cited by 597

Prediction of proprotein convertase cleavage sites

Duckert, P., Brunak, S., & Blom, N. (2004) · Protein Engineering Design and Selection · doi:10.1093/protein/gzh013 · Cited by 583

Myoglobin function reassessed

Wittenberg, J. B., & Wittenberg, B. A. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00243 · Cited by 550

Molecular biology, genetics and biochemistry of the repulsive guidance molecule family

Severyn, C. J., Shinde, U. P., & Rotwein, P. S. (2009) · Biochemical Journal · doi:10.1042/bj20090978 · Cited by 68

Hepcidin and sports anemia

Kong, W.-N., Gao, G., & Chang, Y.-Z. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-19 · Cited by 71

Neogenin Interacts with Matriptase-2 to Facilitate Hemojuvelin Cleavage

Enns, C. A., Ahmed, R., & Zhang, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363937 · Cited by 68

Suppression of the hepcidin‐encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase‐2/TMPRSS6

Truksa, J., Gelbart, T., Peng, H., Beutler, E., Beutler, B., & Lee, P. L. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07873.x · Cited by 66

Novel TMPRSS6 mutations associated with iron-refractory iron deficiency anemia (IRIDA)

Falco, L. D., Totaro, F., Nai, A., Pagani, A., Girelli, D., Silvestri, L., Piscopo, C., Campostrini, N., Dufour, C., Almanjomi, F., et al. (2010) · Human Mutation · doi:10.1002/humu.21243 · Cited by 67

Molecular basis of iron-loading disorders

Darshan, D., Frazer, D. M., & Anderson, G. J. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399410001687 · Cited by 63

Postmortem T 2 * - Weighted MRI Imaging of Cortical Iron Reflects Severity of Alzheimer’s Disease

Bulk, M., Kenkhuis, B., van der Graaf, L. M., Goeman, J. J., Natté, R., & van der Weerd, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180317 · Cited by 63

Therapeutic Advances in Regulating the Hepcidin/Ferroportin Axis

Hawula, Z. J., Wallace, D. F., Subramaniam, V. N., & Rishi, G. (2019) · Pharmaceuticals · doi:10.3390/ph12040170 · Cited by 62

Regulation of Iron Homeostasis and Related Diseases

Li, Y., Huang, X., Wang, J., Huang, R., & Wan, D. (2020) · Mediators of Inflammation · doi:10.1155/2020/6062094 · Cited by 66

Hypoxia-inducible factor-prolyl hydroxylase inhibitors for renal anemia in chronic kidney disease: Advantages and disadvantages

Mima, A. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174583 · Cited by 63

Matriptase-2- and Proprotein Convertase-cleaved Forms of Hemojuvelin Have Different Roles in the Down-regulation of Hepcidin Expression

Maxson, J. E., Chen, J., Enns, C. A., & Zhang, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.183160 · Cited by 60

Mitochondrial ferritin in neurodegenerative diseases

Yang, H., Yang, M., Guan, H., Liu, Z., Zhao, S., Takeuchi, S., Yanagisawa, D., & Tooyama, I. (2013) · Neuroscience Research · doi:10.1016/j.neures.2013.07.005 · Cited by 59

Genetics of the First Seven Proprotein Convertase Enzymes in Health and Disease

Turpeinen, H., Ortutay, Z., & Pesu, M. (2013) · Current Genomics · doi:10.2174/1389202911314050010 · Cited by 62

Modulation of hepcidin to treat iron deregulation: potential clinical applications

Blanchette, N. L., Manz, D. H., Torti, F. M., & Torti, S. V. (2015) · Expert Review of Hematology · doi:10.1586/17474086.2016.1124757 · Cited by 59

Osteocytic FGF23 and Its Kidney Function

Agoro, R., Ni, P., Noonan, M. L., & White, K. E. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00592 · Cited by 59

Skeletal muscle hemojuvelin is dispensable for systemic iron homeostasis

Chen, W., Huang, F. W., Renshaw, T. B. D., & Andrews, N. C. (2011) · Blood · doi:10.1182/blood-2010-12-327957 · Cited by 60

Hepcidin: A Critical Regulator of Iron Metabolism during Hypoxia

Hintze, K. J., & McClung, J. P. (2011) · Advances in Hematology · doi:10.1155/2011/510304 · Cited by 61

Mechanistic insights and emerging therapeutic stratagems for Alzheimer’s disease

Rajendran, K., & Krishnan, U. M. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102309 · Cited by 59

Thalassaemia Intermedia: an Update

Taher, A. T., Musallam, K. M., & Cappellini, M. D. (2009) · Mediterranean Journal of Hematology and Infectious Diseases · doi:10.4084/mjhid.2009.004 · Cited by 59

Iron metabolism and management: focus on chronic kidney disease

Agarwal, A. K. (2021) · Kidney International Supplements · doi:10.1016/j.kisu.2020.12.003 · Cited by 57

Conditional disruption of mouse HFE2 gene: Maintenance of systemic iron homeostasis requires hepatic but not skeletal muscle hemojuvelin

Gkouvatsos, K., Wagner, J., Papanikolaou, G. V., Sebastiani, G., & Pantopoulos, K. (2011) · Hepatology · doi:10.1002/hep.24547 · Cited by 55

Repulsive Guidance Molecule (RGM) Family Proteins Exhibit Differential Binding Kinetics for Bone Morphogenetic Proteins (BMPs)

Wu, Q., Sun, C. C., Lin, H. Y.-F., & Babitt, J. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046307 · Cited by 55

Small-protein Enrichment Assay Enables the Rapid, Unbiased Analysis of Over 100 Low Abundance Factors from Human Plasma

Harney, D., Hutchison, A. T., Su, Z., Hatchwell, L., Heilbronn, L. K., HOCKING, S. L., James, D. E., & Larance, M. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001562 · Cited by 53

Proprotein convertases: Key players in inflammation-related malignancies and metastasis

Siegfried, G., Descarpentrie, J., Évrard, S., & Khatib, A. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.12.027 · Cited by 57

Regulation of cell surface transferrin receptor-2 by iron-dependent cleavage and release of a soluble form

Pagani, A., Vieillevoye, M., Nai, A., Rausa, M., Ladli, M., Lacombe, C., Mayeux, P., Verdier, F., Camaschella, C., & Silvestri, L. (2015) · Haematologica · doi:10.3324/haematol.2014.118521 · 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

Evaluation of genome-wide loci of iron metabolism in hereditary hemochromatosis identifies PCSK7 as a host risk factor of liver cirrhosis

Stickel, F., Buch, S., Zoller, H., Hultcrantz, R., Gallati, S., Österreicher, C. H., Finkenstedt, A., Stadlmayr, A., Aigner, E. S., Sahinbegovic, E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu076 · Cited by 53

Role of hepcidin‐ferroportin axis in the pathophysiology, diagnosis, and treatment of anemia of chronic inflammation

Langer, A. L., & Ginzburg, Y. Z. (2017) · Hemodialysis International · doi:10.1111/hdi.12543 · Cited by 57

Modulation of iron metabolism in aging and in Alzheimer's disease: relevance of the choroid plexus

Mesquita, S. D., Ferreira, A. C., Sousa, J. C., Santos, N. C., Correia‐Neves, M., Sousa, N., Palha, J. A., & Marques, F. (2012) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2012.00025 · Cited by 52

Endocrine and Bone Complications inβ-Thalassemia Intermedia: Current Understanding and Treatment

Inati, A. C., Noureldine, M. H. A., Mansour, A. G., & Abbas, H. A. (2015) · BioMed Research International · doi:10.1155/2015/813098 · Cited by 52

Factors influencing disease phenotype and penetrance in HFE haemochromatosis

Rochette, J., Gac, G. L., Lassoued, K., Férec, C., & Robson, K. (2010) · Human Genetics · doi:10.1007/s00439-010-0852-1 · Cited by 52

Control of Systemic Iron Homeostasis by the Hemojuvelin-Hepcidin Axis

Zhang, A. (2010) · Advances in Nutrition · doi:10.3945/an.110.1009 · Cited by 51

The EPO-FGF23 Signaling Pathway in Erythroid Progenitor Cells: Opening a New Area of Research

van Vuren, A. J., Gaillard, S., Eisenga, M. F., van Wijk, R., & van Beers, E. J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00304 · Cited by 47

Selective binding of RGMc/hemojuvelin, a key protein in systemic iron metabolism, to BMP-2 and neogenin

Kuns-Hashimoto, R., Kuninger, D., Nili, M., & Rotwein, P. S. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00563.2007 · Cited by 47

Role of Matriptase-2 (TMPRSS6) in Iron Metabolism

Lee, P. L. (2009) · Acta Haematologica · doi:10.1159/000243792 · Cited by 47

Pro-hepcidin is unable to degrade the iron exporter ferroportin unless maturated by a furin-dependent process

Gagliardo, B., Kubat, N. J., Faye, A., Jaouen, M., Durel, B., Deschemin, J., Canonne‐Hergaux, F., Sari, M., & Vaulont, S. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.09.018 · Cited by 45

Treatment of erythropoietin deficiency in mice with systemically administered siRNA

Querbes, W., Bogorad, R. L., Moslehi, J., Wong, J., Chan, A. Y., Bulgakova, E., Kuchimanchi, S., Akinc, A., Fitzgerald, K., Koteliansky, V., et al. (2012) · Blood · doi:10.1182/blood-2012-04-423715 · Cited by 45

Non-HFE hemochromatosis: Pathophysiological and diagnostic aspects

Bardou‐Jacquet, E., Ali, Z. B., Beaumont-Epinette, M.-P., Loréal, O., Jouanolle, A., & Brissot, P. (2013) · Clinics and Research in Hepatology and Gastroenterology · doi:10.1016/j.clinre.2013.11.003 · Cited by 47

Iron Deficiency in Pulmonary Arterial Hypertension: A Deep Dive into the Mechanisms

Quatredeniers, M., Mendes‐Ferreira, P., Santos‐Ribeiro, D., Nakhleh, M. K., Ghigna, M., Cohen‐Kaminsky, S., & Perros, F. (2021) · Cells · doi:10.3390/cells10020477 · Cited by 45

Stimulated erythropoiesis with secondary iron loading leads to a decrease in hepcidin despite an increase in bone morphogenetic protein 6 expression

Frazer, D. M., Wilkins, S. J., Darshan, D., Badrick, A. C., McLaren, G. D., & Anderson, G. J. (2012) · British Journal of Haematology · doi:10.1111/j.1365-2141.2012.09104.x · Cited by 43

Iron deficiency and supplementation in heart failure

Lakhal‐Littleton, S., & Cleland, J. G. F. (2024) · Nature Reviews Cardiology · doi:10.1038/s41569-024-00988-1 · Cited by 44

Hepcidin suppression and defective iron recycling account for dysregulation of iron homeostasis in heme oxygenase‐1 deficiency

Kartikasari, A. E. R., Wagener, F. A. D. T. G., Yachie, A., Wiegerinck, E. T. G., Kemna, E., & Winkels, D. W. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00494.x · Cited by 41

Hepcidin is a Potential Regulator of Iron Status in Chronic Kidney Disease

Tsuchiya, K., & Nitta, K. (2012) · Therapeutic Apheresis and Dialysis · doi:10.1111/1744-9987.12001 · Cited by 42

Hemojuvelin: A New Link Between Obesity and Iron Homeostasis

Luciani, N., Brasse‐Lagnel, C., Poli, M., Anty, R., Lesueur, C., Cormont, M., Laquerrière, A., Folope, V., MARCHAND‐BRUSTEL, Y. L., Gugenheim, J., et al. (2011) · Obesity · doi:10.1038/oby.2011.12 · Cited by 43

Hepcidin is correlated to soluble hemojuvelin but not to increased GDF15 during pregnancy

Finkenstedt, A., Widschwendter, A., Brasse‐Lagnel, C., Theurl, I., Hubalek, M., Dieplinger, H., Tselepis, C., Ward, D. G., Vogel, W., & Zoller, H. (2012) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2012.02.001 · Cited by 40

Pro-protein convertases control the maturation and processing of the iron-regulatory protein, RGMc/hemojuvelin

Kuninger, D., Kuns-Hashimoto, R., Nili, M., & Rotwein, P. S. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-9 · Cited by 41

Unraveling Mechanisms Regulating Systemic Iron Homeostasis

Finberg, K. E. (2011) · Hematology · doi:10.1182/asheducation-2011.1.532 · Cited by 41

Insight onto the Pathophysiology and Clinical Complications of Thalassemia Intermedia

Cappellini, M. D., Musallam, K. M., & Taher, A. T. (2009) · Hemoglobin · doi:10.3109/03630260903351528 · Cited by 38

Neogenin Facilitates the Induction of Hepcidin Expression by Hemojuvelin in the Liver

Zhao, N., Maxson, J. E., Zhang, R. H., Wahedi, M., Enns, C. A., & Zhang, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721191 · Cited by 37

Discovery and Development of TMPRSS6 Inhibitors Modulating Hepcidin Levels in Human Hepatocytes

Béliveau, F., Tarkar, A., Dion, S. P., Désilets, A., Ghinet, M. G., Boudreault, P., St-Georges, C., Marsault, É., Paone, D. V., Collins, J. L., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.09.004 · Cited by 37

Iron effects versus metabolic alterations in hereditary hemochromatosis driven bone loss

Baschant, U., Altamura, S., Steele-Perkins, P., Muckenthaler, M. U., Spasić, M. V., Hofbauer, L. C., Steinbicker, A. U., & Rauner, M. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2022.06.004 · Cited by 37

Hypoxia enhances H2O2-mediated upregulation of hepcidin: Evidence for NOX4-mediated iron regulation

da Silva, I. P., Rausch, V., Peccerella, T., Millonig, G., Seitz, H. K., & Mueller, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.02.005 · Cited by 35

Amelioration of chronic kidney disease-associated anemia by vadadustat in mice is not dependent on erythroferrone

Hanudel, M. R., Wong, S. F., Jung, G., Qiao, B., Gabayan, V. R., Zuk, A., & Ganz, T. (2021) · Kidney International · doi:10.1016/j.kint.2021.03.019 · Cited by 38

Blood Iron Homeostasis: Newly Discovered Proteins and Iron Imbalance

Bleackley, M. R., Wong, A. Y. K., Hudson, D. M., Wu, C., & MacGillivray, R. T. A. (2009) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2008.12.001 · Cited by 38

Repulsive guidance molecules (RGMs) and neogenin in bone morphogenetic protein (BMP) signaling

Tian, C., & Liu, J. (2013) · Molecular Reproduction and Development · doi:10.1002/mrd.22199 · Cited by 35

Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells

Maxson, J. E., Enns, C. A., & Zhang, A. (2008) · Blood · doi:10.1182/blood-2008-08-174565 · Cited by 35

Hemojuvelin: The Hepcidin Story Continues

Małyszko, J. (2009) · Kidney & Blood Pressure Research · doi:10.1159/000208988 · Cited by 35

New and old players in the hepcidin pathway

Camaschella, C., & Silvestri, L. (2008) · Haematologica · doi:10.3324/haematol.13724 · Cited by 33

Iron and oxygen sensing: a tale of 2 interacting elements?

Simpson, R. J., & McKie, A. T. (2014) · Metallomics · doi:10.1039/c4mt00225c · Cited by 32

Hemojuvelin N-terminal mutants reach the plasma membrane but do not activate the hepcidin response

Pagani, A., Silvestri, L., Nai, A., & Camaschella, C. (2008) · Haematologica · doi:10.3324/haematol.12508 · Cited by 31

The relationship between systemic iron homeostasis and erythropoiesis

Rishi, G., & Subramaniam, V. N. (2017) · Bioscience Reports · doi:10.1042/bsr20170195 · Cited by 35

Does Hypoxia Cause Carcinogenic Iron Accumulation in Alcoholic Liver Disease (ALD)?

da Silva, I. S., Rausch, V., Seitz, H. K., & Mueller, S. (2017) · Cancers · doi:10.3390/cancers9110145 · Cited by 31

Does Hepatic Hepcidin Play an Important Role in Exercise-Associated Anemia in Rats?

Liu, Y.-Q., Chang, Y., Zhao, B., Wang, H.-T., & Duan, X. (2011) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.21.1.19 · Cited by 30

Molecular Mechanisms Regulating Hepcidin Revealed by Hepcidin Disorders

Camaschella, C., & Silvestri, L. (2011) · The Scientific World JOURNAL · doi:10.1100/tsw.2011.130 · Cited by 28

Mechanisms and Regulation of Intestinal Iron Transport

Collins, J. F., Flores, S. R., Wang, X., & Anderson, G. J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00060-8 · Cited by 30

Non-renal-Related Mechanisms of FGF23 Pathophysiology

Hanudel, M. R., Laster, M. L., & Salusky, I. B. (2018) · Current Osteoporosis Reports · doi:10.1007/s11914-018-0492-2 · Cited by 30

Novel insights into alcoholic liver disease: Iron overload, iron sensing and hemolysis

Mueller, S., Chen, C., Mueller, J. H., & Wang, S. (2022) · Journal of Translational Internal Medicine · doi:10.2478/jtim-2021-0056 · Cited by 30

Hepcidin: a real-time biomarker of iron need

Hare, D. J. (2017) · Metallomics · doi:10.1039/c7mt00047b · Cited by 29

The interplay between iron and oxygen homeostasis with a particular focus on the heart

Lakhal‐Littleton, S., & Robbins, P. A. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00237.2017 · Cited by 29

Immunoassay for human serum hemojuvelin

Brasse‐Lagnel, C., Poli, M., Lesueur, C., Grandchamp, B., Lavoinne, A., Beaumont, C., & Bekri, S. (2010) · Haematologica · doi:10.3324/haematol.2010.022129 · Cited by 28

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex

Malinauskas, T., Peer, T. V., Bishop, B., Mueller, T. D., & Siebold, C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000561117 · Cited by 28

20 years of Hepcidin: How far we have come

Colucci, S., Marques, O., & Altamura, S. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.05.001 · Cited by 28

Functional Roles of Furin in Cardio-Cerebrovascular Diseases

Wichaiyo, S., Koonyosying, P., & Morales, N. P. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00325 · Cited by 26

Biomarkers of iron metabolism in chronic kidney disease

Głogowski, T., Wojtaszek, E., & Małyszko, J. (2020) · International Urology and Nephrology · doi:10.1007/s11255-020-02663-z · Cited by 33

Hippocampal Iron Accumulation Impairs Synapses and Memory via Suppressing Furin Expression and Downregulating BDNF Maturation

Zhang, Y., Bai, X., Zhang, Y., Yao, S., Cui, Y., You, L., Yu, P., Chang, Y., & Gao, G. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02929-w · Cited by 27

Hemojuvelin Modulates Iron Stress During Acute Kidney Injury: Improved by Furin Inhibitor

Young, G., Huang, T., Wu, C., Lai, C., Hou, C., Peng, K., Liang, C., Lin, S., Chang, S., Tsai, H., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5366 · Cited by 26

Hemojuvelin–hepcidin axis modeled and analyzed using Petri nets

Formanowicz, D., Kozak, A., Głowacki, T., Radom, M., & Formanowicz, P. (2013) · Journal of Biomedical Informatics · doi:10.1016/j.jbi.2013.07.013 · Cited by 28

BMP Signaling Modulates Hepcidin Expression in Zebrafish Embryos Independent of Hemojuvelin

Gibert, Y., Lattanzi, V. J., Zhen, A. W., Vedder, L. M., Brunet, F., Faasse, S. A., Babitt, J. L., Lin, H. Y.-F., Hammerschmidt, M., & Fraenkel, P. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014553 · Cited by 29

Development and Prospects of Furin Inhibitors for Therapeutic Applications

Ivachtchenko, A. V., Khvat, A. V., & Shkil, D. O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179199 · Cited by 25

Serum hepcidin levels and muscle iron proteins in humans injected with low‐ or high‐dose erythropoietin

Robach, P., Recalcati, S., Girelli, D., Campostrini, N., Kempf, T., Wollert, K. C., Corbella, M., Santambrogio, P., Perbellini, L., Brasse‐Lagnel, C., et al. (2013) · European Journal Of Haematology · doi:10.1111/ejh.12122 · Cited by 25

Iron Mining for Erythropoiesis

Correnti, M., Gammella, E., Cairo, G., & Recalcati, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105341 · Cited by 30

Identification of TMPRSS 6 cleavage sites of hemojuvelin

Rausa, M., Ghitti, M., Pagani, A., Nai, A., Campanella, A., Musco, G., Camaschella, C., & Silvestri, L. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12462 · Cited by 24

Pathogenesis, Diagnosis and Treatment of Hemochromatosis

Zoller, H., & Henninger, B. (2016) · Digestive Diseases · doi:10.1159/000444549 · Cited by 24

Characterization of plasma metal profiles in Alzheimer’s disease using multivariate statistical analysis

Guan, C., Dang, R., Cui, Y., Liu, L., Chen, X., Wang, X., Zhu, J., Li, D., Li, J., & Wang, D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178271 · Cited by 26

Hypoxia-Inducible Factor Stabilizers: a New Avenue for Reducing BP While Helping Hemoglobin?

Yousaf, F., & Spinowitz, B. (2016) · Current Hypertension Reports · doi:10.1007/s11906-016-0629-6 · Cited by 23

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0472-z · Cited by 23

Molecular Mechanisms of Intestinal Iron Transport

Collins, J. F., & Anderson, G. J. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00071-3 · Cited by 22

Signaling pathways regulating hepcidin

Rishi, G., & Subramaniam, V. N. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.003 · Cited by 23

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_1 · Cited by 22

Hepcidin regulation in a mouse model of acute hypoxia

Ravasi, G., Pelucchi, S., Comani, G. B., Greni, F., Mariani, R., Pelloni, I., Bombelli, S., Perego, R., Barisani, D., & Piperno, A. (2018) · European Journal Of Haematology · doi:10.1111/ejh.13062 · Cited by 22

Hepatocyte neogenin is required for hemojuvelin-mediated hepcidin expression and iron homeostasis in mice

Enns, C. A., Jue, S. F., & Zhang, A. (2021) · Blood · doi:10.1182/blood.2020009485 · Cited by 22

Serum Erythroferrone During Pregnancy Is Related to Erythropoietin but Does Not Predict the Risk of Anemia

Delaney, K. M., Guillet, R., Pressman, E. K., Ganz, T., Nemeth, E., & O'Brien, K. O. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab093 · Cited by 22

Hepcidin in chronic kidney disease anemia

Santos‐Silva, A., Ribeiro, S., Reis, F., & Belo, L. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.012 · Cited by 23

Effect of atorvastatin on iron metabolism regulation in patients with chronic kidney disease – a randomized double blind crossover study

Masajtis‐Zagajewska, A., & Nowicki, M. P. (2018) · Renal Failure · doi:10.1080/0886022x.2018.1535983 · Cited by 21

Iron overload suppresses hippocampal neurogenesis in adult mice: Implication for iron dysregulation‐linked neurological diseases

Li, J., Ding, Y., Zhang, J.-H., Zhang, Y.-T., Cui, Y., Zhang, Y., Chang, S., Chang, Y.-Z., & Gao, G. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14394 · Cited by 23

Acute Acetaminophen Intoxication Leads to Hepatic Iron Loading by Decreased Hepcidin Synthesis

van Swelm, R. P. L., Laarakkers, C. M., Blous, L., Peters, J. G. P., Davidson, E. N. B., van der Kraan, P. M., Swinkels, D. W., Masereeuw, R., & Rüssel, F. G. M. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs176 · Cited by 20

Correlative Microscopy to Localize and Characterize Iron Deposition in Alzheimer’s Disease

Madsen, S. J., DiGiacomo, P. S., Zeng, Y., Goubran, M., Chen, Y., Rutt, B. K., Born, D. E., Vogel, H. S., Sinclair, R., & Zeineh, M. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200234 · Cited by 20

Iron metabolism gene expression in human skeletal muscle

Polonifi, A., Politou, M., Kalotychou, V., Xiromeritis, K., Tsironi, M., Berdoukas, V., Vaiopoulos, G., & Aessopos, A. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.07.002 · Cited by 19

Effect of Iron Overload and Iron Deficiency on Liver Hemojuvelin Protein

Krijt, J., Frýdlová, J., Kukačková, L., Fujikura, Y., Přikryl, P., Vokurka, M., & Nečas, E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037391 · Cited by 20

Decrease in APP and CP mRNA expression supports impairment of iron export in Alzheimer's disease patients

Guerreiro, C. C., Silva, B. D. R., Crespo, Â. C., Marques, L., Costa, S., Timóteo, Â., Marcelino, E., Maruta, C., Vilares, A., Matos, M., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.017 · Cited by 19

Hepcidin downregulation by repeated bleeding is not mediated by soluble hemojuvelin.

Krijt, J., Fujikura, Y., Šefc, L., Vokurka, M., Hlobenová, T., & Necas, E. (2010) · PubMed · doi:10.33549/physiolres.931706 · Cited by 16

Insights on the role of the protein hemojuvelin in the maintenance of systemic iron homeostasis

Gkouvatsos, K. (2013) · eScholarship@McGill (McGill) · doi:10.82308/36096

Iron-Dependent Regulation of Hepcidin in Hjv−/− Mice: Evidence That Hemojuvelin Is Dispensable for Sensing Body Iron Levels

Gkouvatsos, K., Fillebeen, C., Daba, A., Wagner, J., Sebastiani, G., & Pantopoulos, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085530 · Cited by 33

Sensing Iron: Reciprocal Regulation of Hepcidin mRNA by Soluble and Cell-Associated Hemojuvelin.

Lin, L., Goldberg, Y. P., & Ganz, T. (2005) · Blood · doi:10.1182/blood.v106.11.512.512 · Cited by 1

Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin

Lin, L., Goldberg, Y. P., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2005-05-1845 · Cited by 241