The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860

Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.

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

Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells

Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544

Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464

Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.

The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370

Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage in Saccharomyces cerevisiae

Rodríguez‐Manzaneque, M. T., Ros, J., Cabiscol, E., Albert Sorribas, B., & Herrero, E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8180 · Cited by 302

Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation

Bekri, S., Kispál, G., Lange, H., Fitzsimons, E. J., Tolmie, J., Lill, R., & Bishop, D. F. (2000) · Blood · doi:10.1182/blood.v96.9.3256 · Cited by 281

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

Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload

Mims, M. P., Guan, Y., Pospı́šilová, D., Priwitzerova, M., Indrák, K., Ponka, P., Divoký, V., & Prchal, J. T. (2005) · Blood · doi:10.1182/blood-2004-07-2966 · Cited by 224

Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)

Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 224

Iron-dependent functions of mitochondria—relation to neurodegeneration

Gille, G., & Reichmann, H. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0503-7 · Cited by 77

The emerging role of iron dyshomeostasis in the mitochondrial decay of aging

Xu, J., Marzetti, E., Seo, A. Y., Kim, J., Prolla, T. A., & Leeuwenburgh, C. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.04.007 · Cited by 77

Recent advances in the understanding of inherited sideroblastic anaemia

Camaschella, C. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07290.x · Cited by 79

Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9

Schmitz-Abe, K., Ciesielski, S. J., Schmidt, P. J., Campagna, D. R., Rahimov, F., Schilke, B. A., Cuijpers, M., Rieneck, K., Lausen, B., Linenberger, M. L., et al. (2015) · Blood · doi:10.1182/blood-2015-09-659854 · Cited by 75

From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis

Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0117 · Cited by 73

Hereditary sideroblastic anemia: pathophysiology and gene mutations

Harigae, H., & Furuyama, K. (2010) · International Journal of Hematology · doi:10.1007/s12185-010-0688-4 · Cited by 75

Iron: Effect of Overload and Deficiency

Hider, R. C., & Kong, X. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_8 · Cited by 78

Iron-sulfur cluster biogenesis, trafficking, and signaling: Roles for CGFS glutaredoxins and BolA proteins

Talib, E. A., & Outten, C. E. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118847 · Cited by 68

A mammalian monothiol glutaredoxin, Grx3, is critical for cell cycle progression during embryogenesis

Cheng, N., Zhang, W., Chen, W., Jin, J., Cui, X., Butte, N. F., Chan, L., & Hirschi, K. D. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08178.x · Cited by 71

Multiple determinants within iron-responsive elements dictate iron regulatory protein binding and regulatory hierarchy

Goforth, J. B., Anderson, S. A., Nizzi, C. P., & Eisenstein, R. S. (2010) · RNA · doi:10.1261/rna.1857210 · Cited by 71

Ring sideroblasts and sideroblastic anemias

Cazzola, M., & Invernizzi, R. (2011) · Haematologica · doi:10.3324/haematol.2011.044628 · Cited by 71

ATP-dependent Mitochondrial Porphyrin Importer ABCB6 Protects against Phenylhydrazine Toxicity

Ulrich, D. L., Lynch, J., Wang, Y., Fukuda, Y., Nachagari, D., Du, G., Sun, D., Fan, Y., Tsurkan, L. G., Potter, P. M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336180 · Cited by 71

Friedreich's ataxia: the vicious circle hypothesis revisited

Bayot, A., Santos, R., Camadro, J., & Rustin, P. (2011) · BMC Medicine · doi:10.1186/1741-7015-9-112 · Cited by 74

Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations

Ducamp, S., Kannengiesser, C., Touati, M., Garçon, L., Guerci‐Bresler, A., Guichard, J. F., Vermylen, C., Dochir, J., Poirel, H. A., Fouyssac, F., et al. (2011) · Human Mutation · doi:10.1002/humu.21455 · Cited by 69

Zebrafish as a model system for mitochondrial biology and diseases

Steele, S. L., Prykhozhij, S. V., & Berman, J. N. (2013) · Translational research · doi:10.1016/j.trsl.2013.08.008 · Cited by 67

Saccharomyces cerevisiae Grx6 and Grx7 Are Monothiol Glutaredoxins Associated with the Early Secretory Pathway

Izquierdo, A., Casas, C., Mühlenhoff, U., Lillig, C. H., & Herrero, E. (2008) · Eukaryotic Cell · doi:10.1128/ec.00133-08 · Cited by 66

Distinct iron architecture in SF3B1-mutant myelodysplastic syndrome patients is linked to an SLC25A37 splice variant with a retained intron

Visconte, V., Avishai, N., Mahfouz, R. Z., Tabarroki, A., Cowen, J., Sharghi-Moshtaghin, R., Hitomi, M., Rogers, H. J., Hasrouni, E., Phillips, J., et al. (2014) · Leukemia · doi:10.1038/leu.2014.170 · Cited by 64

Intracellular iron and heme trafficking and metabolism in developing erythroblasts

Kafina, M. D., & Paw, B. H. (2017) · Metallomics · doi:10.1039/c7mt00103g · Cited by 65

Understanding Sideroblastic Anemia: An Overview of Genetics, Epidemiology, Pathophysiology and Current Therapeutic Options

Abu-Zeinah, G. F., & DeSancho, M. T. (2020) · Journal of Blood Medicine · doi:10.2147/jbm.s232644 · Cited by 63

Biophysical Characterization of Iron in Mitochondria Isolated from Respiring and Fermenting Yeast

Morales, J. G., Holmes‐Hampton, G. P., Miao, R., Guo, Y., Münck, E., & Lindahl, P. A. (2010) · Biochemistry · doi:10.1021/bi100558z · Cited by 60

Differential diagnosis of lipoic acid synthesis defects

Tort, F., Ferrer-Cortés, X., & Ribes, A. (2016) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-016-9975-4 · Cited by 60

Inherited disorders of iron metabolism

Camaschella, C., & Poggiali, E. (2011) · Current Opinion in Pediatrics · doi:10.1097/mop.0b013e3283425591 · Cited by 59

The ins and outs of mitochondrial iron-loading: the metabolic defect in Friedreich’s ataxia

Richardson, D. R., Huang, M. L. H., Whitnall, M., Becker, E., Ponka, P., & Rahmanto, Y. S. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0565-x · Cited by 59

BOLA1 Is an Aerobic Protein That Prevents Mitochondrial Morphology Changes Induced by Glutathione Depletion

Willems, P. H. G. M., Wanschers, B. F. J., Esseling, J. J., Szklarczyk, R., Kudla, U., Duarte, I., Forkink, M., Nooteboom, M., Swarts, H. G. P., Gloerich, J., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4253 · Cited by 58

Disorders associated with systemic or local iron overload: from pathophysiology to clinical practice

Sebastiani, G., & Pantopoulos, K. (2011) · Metallomics · doi:10.1039/c1mt00082a · Cited by 58

Cardiac iron overload in chronically transfused patients with thalassemia, sickle cell anemia, or myelodysplastic syndrome

de Montalembert, M., Ribeil, J., Brousse, V. A. M., Guerci‐Bresler, A., Stamatoullas, A., Vannier, J., Dumesnil, C., Lahary, A., Touati, M., Bouabdallah, K. K., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172147 · Cited by 57

The Multidomain Thioredoxin-Monothiol Glutaredoxins Represent a Distinct Functional Group

Hoffmann, B., Uzarska, M. A., Berndt, C., Godoy, J. R., Haunhorst, P., Lillig, C. H., Lill, R., & Mühlenhoff, U. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3811 · Cited by 55

Iron Metabolism and Its Disorders

Harvey, J. W. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-370491-7.00009-x · Cited by 57

Dysregulation of the glutaredoxin/S-glutathionylation redox axis in lung diseases

Chia, S. B., Elko, E. A., Aboushousha, R., Manuel, A. M., van de Wetering, C., Druso, J. E., van der Velden, J. L. J., Seward, D. J., Anathy, V., Irvin, C. G., et al. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00410.2019 · Cited by 55

Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism

Ferring–Appel, D., Hentze, M. W., & Galy, B. (2008) · Blood · doi:10.1182/blood-2008-05-155093 · Cited by 53

Pathophysiology and genetic mutations in congenital sideroblastic anemia

Fujiwara, T., & Harigae, H. (2013) · Pediatrics International · doi:10.1111/ped.12217 · Cited by 53

Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis

Maio, N., Kim, K. S., Holmes‐Hampton, G. P., Singh, A., & Rouault, T. A. (2019) · Haematologica · doi:10.3324/haematol.2018.214320 · Cited by 53

Rare anemias due to genetic iron metabolism defects

Brissot, P., Bernard, D. G., Brissot, É., Loréal, O., & Troadec, M. (2018) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2018.06.003 · Cited by 51

Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism

Mühlenhoff, U., Braymer, J. J., Christ, S., Rietzschel, N., Uzarska, M. A., Weiler, B. D., & Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0237 · Cited by 52

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Avagyan, S., & Zon, L. I. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.024 · Cited by 53

X‐linked sideroblastic anemia due to ALAS2 intron 1 enhancer element GATA‐binding site mutations

Campagna, D. R., de Bie, C. I., Schmitz‐Abe, K., Sweeney, M. C., Sendamarai, A. K., Schmidt, P. J., Heeney, M. M., Yntema, H. G., Kannengiesser, C., Grandchamp, B., et al. (2013) · American Journal of Hematology · doi:10.1002/ajh.23616 · Cited by 50

Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review

Trnka, D., Hossain, M. F., Jordt, L. M., Gellert, M., & Lillig, C. H. (2020) · Molecules · doi:10.3390/molecules25173860 · Cited by 52

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Camaschella, C. (2013) · British Journal of Haematology · doi:10.1111/bjh.12081 · Cited by 49

Mechanisms of cellular iron sensing, regulation of erythropoiesis and mitochondrial iron utilization

Maio, N., Zhang, D., Ghosh, M. C., Jain, A., SantaMaria, A. M., & Rouault, T. A. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.06.001 · Cited by 50

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Römer, A., Linn, T., & Petry, S. F. (2021) · Antioxidants · doi:10.3390/antiox10020293 · Cited by 52

Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress

Linares, G. R., Xing, W., Govoni, K. E., Chen, S., & Mohan, S. (2009) · Bone · doi:10.1016/j.bone.2009.01.003 · Cited by 48

The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis

Sheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 49

Molecular pathophysiology and genetic mutations in congenital sideroblastic anemia

Fujiwara, T., & Harigae, H. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.008 · Cited by 47

Iron redistribution as a therapeutic strategy for treating diseases of localized iron accumulationThis review is one of a selection of papers published in a Special Issue on Oxidative Stress in Health and Disease.

Kakhlon, O., Breuer, W. V., Münnich, A., & Cabantchik, Z. I. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y09-128 · Cited by 49

Heterozygous missense mutations in the GLRX5 gene cause sideroblastic anemia in a Chinese patient

Liu, G., Guo, S., Anderson, G. J., Camaschella, C., Han, B., & Nie, G. (2014) · Blood · doi:10.1182/blood-2014-08-598508 · Cited by 47

Erythropoiesis and Iron Sulfur Cluster Biogenesis

Ye, H., & Rouault, T. A. (2010) · Advances in Hematology · doi:10.1155/2010/329394 · 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

Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein

Liu, G., Wang, Y., Anderson, G. J., Camaschella, C., Chang, Y., & Nie, G. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25267 · Cited by 43

Regulation and tissue-specific expression of δ-aminolevulinic acid synthases in non-syndromic sideroblastic anemias and porphyrias

Peoc’h, K., Nicolas, G., Schmitt, C., Mirmiran, A., Daher, R., Lefèbvre, T., Gouya, L., Karim, Z., & Puy, H. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.01.015 · Cited by 43

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Zuris, J. A., Ali, S. S., Yeh, H., Nguyen, T. A., Nechushtai, R., Paddock, M. L., & Jennings, P. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.319731 · Cited by 43

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Sheftel, A. D., Richardson, D. R., Prchal, J. T., & Ponka, P. (2009) · Acta Haematologica · doi:10.1159/000243796 · Cited by 42

Mono- and Dithiol Glutaredoxins in the Trypanothione-Based Redox Metabolism of Pathogenic Trypanosomes

Comini, M. A., Krauth‐Siegel, R. L., & Bellanda, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4932 · Cited by 43

Clinical and genetic characteristics of congenital sideroblastic anemia: comparison with myelodysplastic syndrome with ring sideroblast (MDS-RS)

Ohba, R., Furuyama, K., Yoshida, K., Fujiwara, T., Fukuhara, N., Onishi, Y., Manabe, A., Ito, E., Ozawa, K., Kojima, S., et al. (2012) · Annals of Hematology · doi:10.1007/s00277-012-1564-5 · Cited by 40

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Dutkiewicz, R., & Nowak, M. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1504-x · Cited by 41

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Payne, E. M., & Look, A. T. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07705.x · Cited by 41

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Cortassa, S. C., Juhaszova, M., Aon, M. A., Zorov, D. B., & Sollott, S. J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.11.013 · Cited by 39

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Pham, K., Pal, R., Qu, Y., Liu, X., Yu, H. K., Shiao, S. L., Wang, X., Smith, E. O., Cui, X., Rodney, G. G., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.003 · Cited by 38

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Ali, V., & Nozaki, T. (2013) · Advances in Parasitology/Advances in parasitology · doi:10.1016/b978-0-12-407705-8.00001-x · Cited by 41

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Prudent, M., Crettaz, D., Delobel, J., Tissot, J., & Lion, N. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.07.008 · Cited by 39

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Shan, Y., & Cortopassi, G. A. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.12.005 · Cited by 39

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Zhong, H., Janer, A., Khalimonchuk, O., Antonická, H., Shoubridge, E. A., & Barrientos, A. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad842 · Cited by 37

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Johnson, N. B., Deck, K. M., Nizzi, C. P., & Eisenstein, R. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785741 · Cited by 38

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Gellert, M., Hossain, M. F., Berens, F. J. F., Bruhn, W., Urbainsky, C., Liebscher, V., & Lillig, C. H. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02943 · Cited by 38

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Berndt, C., Christ, L., Rouhier, N., & Mühlenhoff, U. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148317 · Cited by 37

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Ginzburg, Y. Z., An, X., Rivella, S., & Goldfarb, A. N. (2023) · eLife · doi:10.7554/elife.90189 · Cited by 44

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Maio, N., & Rouault, T. A. (2016) · Metallomics · doi:10.1039/c6mt00167j · Cited by 36

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Hoff, K. G., Culler, S. J., Nguyen, P. Q., McGuire, R. M., Silberg, J. J., & Smolke, C. D. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.11.011 · Cited by 32

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Cuijpers, M. L. H., Raymakers, R. A. P., MacKenzie, M. A., de Witte, T. J. M., & Swinkels, D. W. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.08051.x · Cited by 32

GLRX5 mutations impair heme biosynthetic enzymes ALA synthase 2 and ferrochelatase in Human congenital sideroblastic anemia

Daher, R., Mansouri, A., Martelli, A., Bayart, S., Manceau, H., Callebaut, I., Moulouel, B., Gouya, L., Puy, H., Kannengiesser, C., et al. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.12.012 · Cited by 31

Genotype/phenotype correlations of childhood‐onset congenital sideroblastic anaemia in a European cohort

Fouquet, C., Rouzic, M. L., Leblanc, T. M., Fouyssac, F., Leverger, G., Hessissen, L., Marlin, S., Bourrat, E., Fahd, M., Raffoux, E., et al. (2019) · British Journal of Haematology · doi:10.1111/bjh.16100 · Cited by 30

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Fidai, I., Wachnowsky, C., & Cowan, J. A. (2016) · Metallomics · doi:10.1039/c6mt00193a · Cited by 29

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Vanlander, A. V., & Coster, R. V. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1550-z · Cited by 29

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Camaschella, C., Pagani, A., Silvestri, L., & Nai, A. (2022) · International Journal of Hematology · doi:10.1007/s12185-022-03384-y · Cited by 36

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Peña‐Diaz, P., & Lukeš, J. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1556-6 · Cited by 28

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Maio, N., & Rouault, T. A. (2022) · IUBMB Life · doi:10.1002/iub.2597 · Cited by 28

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Khuong-Quang, D.-A., Schwartzentruber, J., Westerman, M. E., Lepage, P., Finberg, K. E., Majewski, J., & Jabado, N. (2013) · PEDIATRICS · doi:10.1542/peds.2012-1303 · Cited by 28

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Bolstad, H. M., Botelho, D., & Wood, M. J. A. (2010) · Journal of Proteome Research · doi:10.1021/pr1006087 · Cited by 28

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Kumar, S., Wang, J., Rani, R., & Gandhi, C. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147864 · Cited by 28

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Malcovati, L., & Cazzola, M. (2016) · British Journal of Haematology · doi:10.1111/bjh.14215 · Cited by 29

Systematic Surveys of Iron Homeostasis Mechanisms Reveal Ferritin Superfamily and Nucleotide Surveillance Regulation to be Modified by PINK1 Absence

Key, J., Şen, N.-E., Arsović, A., Krämer, S., Hülse, R., Khan, N. N., Meierhofer, D., Gispert, S., Koepf, G., & Auburger, G. W. J. (2020) · Cells · doi:10.3390/cells9102229 · Cited by 29

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Ricci, A., Betto, G. D., Bergamini, E., Buzzetti, E., Corradini, E., & Ventura, P. (2022) · Metabolites · doi:10.3390/metabo12090819 · Cited by 30

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Jain, A., Singh, A., Maio, N., & Rouault, T. A. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa172 · Cited by 25

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Camaschella, C., & Pagani, A. (2010) · International Journal of Hematology · doi:10.1007/s12185-010-0743-1 · Cited by 27

Is There a Role for Glutaredoxins and BOLAs in the Perception of the Cellular Iron Status in Plants?

Rey, P., Taupin-Broggini, M., Couturier, J., Vignols, F., & Rouhier, N. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00712 · Cited by 26

Iron metabolism in erythroid cells and patients with congenital sideroblastic anemia

Furuyama, K., & Kaneko, K. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2368-0 · Cited by 26

Biochemical Analyses of Human Iron–Sulfur Protein Biogenesis and of Related Diseases

Stehling, O., Paul, V. D., Bergmann, J., Basu, S., & Lill, R. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.004 · Cited by 26

Iron overload and impaired iron handling contribute to the dystrophic pathology in models of Duchenne muscular dystrophy

Alves, F. M., Kysenius, K., Caldow, M. K., Hardee, J. P., Chung, J. D., Trieu, J., Hare, D. J., Crouch, P. J., Ayton, S., Bush, A. I., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12950 · Cited by 25

SOD2 Deficient Erythroid Cells Up-Regulate Transferrin Receptor and Down-Regulate Mitochondrial Biogenesis and Metabolism

Martin, F. M., Xu, X., von Löhneysen, K., Gilmartin, T. J., & Friedman, J. S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016894 · Cited by 25

Phylogenetic distribution and structural analyses of cyanobacterial glutaredoxins (Grxs)

Mondal, S., Kumar, V., & Singh, S. P. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107141 · Cited by 25

Early Deferasirox Treatment in a Patient with Myelodysplastic Syndrome Results in a Long-Term Reduction in Transfusion Requirements

Capalbo, S. F., Spinosa, G., Franzese, M. G., & Palumbo, G. (2009) · Acta Haematologica · doi:10.1159/000209206 · Cited by 25

Zebrafish as a model system to delineate the role of heme and iron metabolism during erythropoiesis

Zhang, J., & Hamza, I. (2018) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.12.007 · Cited by 25

Novel aberrant genetic and epigenetic events in Friedreich׳s ataxia

Quesada, M. P., Jones, J., Rodríguez‐Lozano, F. J., Moraleda, J. M., & Martı́nez, S. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.04.013 · Cited by 23

Iron-Sulfur Protein Assembly in Human Cells

Saha, P. P., Vishwanathan, V., Bankapalli, K., & D’Silva, P. (2017) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2017_5 · Cited by 22

Mitochondrial iron-sulfur cluster biogenesis and neurological disorders

Selvanathan, A., & Sankaran, B. P. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.10.004 · Cited by 21

A leaky splicing mutation in NFU1 is associated with a particular biochemical phenotype. Consequences for the diagnosis

Ferrer-Cortés, X., Narbona, J., Bujan, N., Matalonga, L., del Toro, M., Arranz, J. A., Riudor, E., García‐Cazorla, À., Jou, C., O’Callaghan, M., et al. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.12.004 · Cited by 21

Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co‐chaperone proteins

Maio, N., & Rouault, T. A. (2022) · IUBMB Life · doi:10.1002/iub.2593 · Cited by 21

Iron Chelation Therapy in Myelodysplastic Syndromes

Messa, E., Cilloni, D., & Saglio, G. N. (2010) · Advances in Hematology · doi:10.1155/2010/756289 · Cited by 20

Splicing factor mutations in MDS RARS and MDS/MPN-RS-T

Yoshimi, A., & Abdel-Wahab, O. I. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2242-0 · Cited by 20

Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe–2S] cluster chirality, ligand exchange and transfer chemistry

Sen, S., & Cowan, J. A. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1485-9 · Cited by 21

Disulfide-masked iron prochelators: Effects on cell death, proliferation, and hemoglobin production

Akam, E. A., Utterback, R. D., Marcero, J. R., Dailey, H. A., & Tomat, E. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.12.016 · Cited by 20

Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts

Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J. F., Camaschella, C., & Rouault, T. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40372 · Cited by 246

The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood 110:1353–1358

Camaschella, C., Campanella, R., Falco, L. D., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., Iolascon, A., Articles, R. C., Camaschella, C., et al. (2007)

The Zebrafish Hypochromic Mutant [iItalic]Shiraz[/iItalic] Encodes a Novel Mitochondrial Glutaredoxin That Establishes a Link between Heme and Fe/S Production.

Wingert, R. A., Barut, B., Foott, H., Fraenkel, P. G., Dooley, K. A., Kingsley, P. D., Palis, J., Shubert, H., Chen, O. S., Kaplan, J., et al. (2004) · Blood · doi:10.1182/blood.v104.11.51.51

Heterozygous missense mutations in the GLRX5 gene cause sideroblastic anemia in a Chinese patient

Liu, G., Guo, S., Anderson, G. J., Camaschella, C., Han, B., & Nie, G. (2014) · Blood · doi:10.1182/blood-2014-08-598508 · Cited by 47

Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein

Liu, G., Wang, Y., Anderson, G. J., Camaschella, C., Chang, Y., & Nie, G. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25267 · Cited by 43