Cited by 306Iron Metabolism and DisordersHemoglobinopathies and Related DisordersNeurological diseases and metabolism

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

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

Open access

Camaschella, Clara, Campanella, Alessandro, De Falco, Luigia, Boschetto, Loredana, Merlini, Roberta, Silvestri, Laura, Levi, Sonia, Iolascon, Achille·2007·Blood

DOI 10.1182/blood-2007-02-072520

Open this paper in CoChat — free account Open PDF

Abstract

Inherited microcytic-hypochromic anemias in rodents and zebrafish suggest the existence of corresponding human disorders. The zebrafish mutant shiraz has severe anemia and is embryonically lethal because of glutaredoxin 5 (GRLX5) deletion, insufficient biogenesis of mitochondrial iron-sulfur (Fe/S) clusters, and deregulated iron-regulatory protein 1 (IRP1) activity. This leads to stabilization of transferrin receptor 1 (TfR) RNA, repression of ferritin, and ALA-synthase 2 (ALAS2) translation with impaired heme synthesis. We report the first case of GLRX5 deficiency in a middle-aged anemic male with iron overload and a low number of ringed sideroblasts. Anemia was worsened by blood transfusions but partially reversed by iron chelation. The patient had a homozygous (c.294A>G) mutation that interferes with intron 1 splicing and drastically reduces GLRX5 RNA. As in shiraz, aconitase and H-ferritin levels were low and TfR level was high in the patient's cells, compatible with increased IRP1 binding. Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron. Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia. GLRX5 function is highly conserved, but at variance with zebrafish, its defect in humans leads to anemia and iron overload.

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 · 10.1182/blood-2007-02-072520

Cites

23 of 23 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.

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

Show all 23 references

Sorted by citations

Items 201–300 of 306

CIAO1 loss of function causes a neuromuscular disorder with compromise of nucleocytoplasmic Fe-S enzymes
Maio, N., Orbach, R., Zaharieva, I. T., Töpf, A., Donkervoort, S. C., Munot, P., Mueller, J., Willis, T. A., Verma, S., Perić, S., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci179559 · Cited by 21
Congenital sideroblastic anemia: Advances in gene mutations and pathophysiology
Long, Z., Li, H., Du, Y., & Han, B. (2018) · Gene · doi:10.1016/j.gene.2018.05.074 · Cited by 19
Actualité du métabolisme du fer
Beaumont, C., & Karim, Z. (2012) · La Revue de Médecine Interne · doi:10.1016/j.revmed.2012.04.006 · Cited by 22
Abnormal body iron distribution and erythropoiesis in a novel mouse model with inducible gain of iron regulatory protein (IRP)-1 function
Casarrubea, D., Viatte, L., Hallas, T., Vasanthakumar, A., Eisenstein, R. S., Schümann, K., Hentze, M. W., & Galy, B. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1008-2 · Cited by 19
Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5
Olive, J. A., & Cowan, J. A. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.04.007 · Cited by 18
Cardiac‐specific ablation of glutaredoxin 3 leads to cardiac hypertrophy and heart failure
Donelson, J., Wang, Q., Monroe, T. O., Jiang, X., Zhou, J., Yu, H. K., Mo, Q., Sun, Q., Marini, J. C., Wang, X., et al. (2019) · Physiological Reports · doi:10.14814/phy2.14071 · Cited by 18
Iron chelation improves ineffective erythropoiesis and iron overload in myelodysplastic syndrome mice
An, W., Feola, M., Aluri, S., Ruíz-Martínez, M., Shridharan, A., Levy, M., Fibach, E., Zhu, X., Verma, A., & Ginzburg, Y. Z. (2023) · eLife · doi:10.7554/elife.83103 · Cited by 17
Mutation analysis of Chinese sporadic congenital sideroblastic anemia by targeted capture sequencing
An, W., Zhang, J., Chang, L., Zhang, Y., Wan, Y., Ren, Y., Niu, D., Wu, J., Zhu, X., & Guo, Y. (2015) · Journal of Hematology & Oncology · doi:10.1186/s13045-015-0154-0 · Cited by 15
Zebrafish larvae as a model to demonstrate secondary iron overload
Nasrallah, G. K., Younes, N., Baji, M. H., Shraim, A. M., & Mustafa, I. (2018) · European Journal Of Haematology · doi:10.1111/ejh.13035 · Cited by 13
Distinct Shift in Beta-Cell Glutaredoxin 5 Expression Is Mediated by Hypoxia and Lipotoxicity Both In Vivo and In Vitro
Petry, S. F., Sun, L. M., Knapp, A., Reinl, S., & Linn, T. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00084 · Cited by 13
Cellular Iron Physiology
Muckenthaler, M. U., & Lill, R. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_2 · Cited by 13
Les hémochromatoses. Nouvelle compréhension, nouveaux traitements
Brissot, P. (2009) · Gastroentérologie Clinique et Biologique · doi:10.1016/j.gcb.2009.04.004 · Cited by 13
Morphology of Blood Cells
BS, F. B. J. B. M. (2014) · Wiley eBooks · doi:10.1002/9781118817322.ch3 · Cited by 13
Mammalian mitochondrial iron–sulfur cluster biogenesis and transfer and related human diseases
Wenxin, Z., Xu, L., Hongting, Z., & Li, K. (2021) · Biophysics Reports · doi:10.52601/bpr.2021.200038 · Cited by 12
Molecular basis of hereditary iron homeostasis defects
Horváthová, M., Ponka, P., & Divoký, V. (2010) · Hematology · doi:10.1179/102453310x12583347009810 · Cited by 12
Iron Metabolism and Disease
Sebastiani, G., & Pantopoulos, K. (2010) · CRC Press eBooks · doi:10.1201/9781420059984-c13 · Cited by 12
Differential expression of islet glutaredoxin 1 and 5 with high reactive oxygen species production in a mouse model of diabesity
Petry, S. F., Sharifpanah, F., Sauer, H., & Linn, T. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176267 · Cited by 12
Congenital sideroblastic anaemia with a novel frameshift mutation in SLC25A38
Wong, W., Wong, H.-F., Cheng, C., Chang, K., Chan, N. P.-H., Ng, M. H. L., & Wong, K.-F. (2014) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2014-202211 · Cited by 11
Loss of glutaredoxin 3 impedes mammary lobuloalveolar development during pregnancy and lactation
Pham, K., Dong, J., Jiang, X., Qu, Y., Yu, H. K., Yang, Y., Olea, W., Marini, J. C., Chan, L., Wang, J., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00150.2016 · Cited by 11
Ferritin Hinders Ferroptosis in Non-Tumorous Diseases: Regulatory Mechanisms and Potential Consequences
Xie, Z., Hou, Q., He, Y., Xie, Y., Mo, Q., Wang, Z., Zhao, Z., Chen, X., Peng, T., Li, L., et al. (2024) · Current Protein and Peptide Science · doi:10.2174/0113892037315874240826112422 · Cited by 11
Mitochondrial glutaredoxin Grx5 functions as a central hub for cellular iron-sulfur cluster assembly
Pandey, A. K., Pain, J., Singh, P., Dancis, A., & Pain, D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108391 · Cited by 10
Regulation of Mitochondrial Energy Metabolism by Glutaredoxin 5 in the Apicomplexan Parasite Neospora caninum
Song, X., Xu, Y., Ying, Z., Wu, K., Liu, J., & Liu, Q. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03091-22 · Cited by 10
Mitochondrial Disorders Due to Nuclear OXPHOS Gene Defects
Ugalde, C., Morán, M., Blázquez, A., Arenas, J., & Martín, M. A. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-90-481-2813-6_7 · Cited by 10
Studying disorders of vertebrate iron and heme metabolism using zebrafish
van der Vorm, L. N., & Paw, B. H. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2016.10.008 · Cited by 10
Biocompatible Magnetic Oxide Nanoparticles with Metal Ions Coated with Organic Shell as Potential Therapeutic Agents in Cancer
Caizer, C., Buteică, S. A., & Mîndrilă, I. (2017) · Springer eBooks · doi:10.1007/978-3-319-63790-7_11 · Cited by 9
The significance of glutaredoxins for diabetes mellitus and its complications
Zhou, M., Hanschmann, E.-M., Römer, A., Linn, T., & Petry, S. F. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103043 · Cited by 9
New Mutation in Erythroid-Specific Delta-Aminolevulinate Synthase as the Cause of X-Linked Sideroblastic Anemia Responsive to Pyridoxine
Kučerová, J., Horváthová, M., Mojzíková, R., Bělohlávková, P., Čermák, J., & Divoký, V. (2011) · Acta Haematologica · doi:10.1159/000322870 · Cited by 8
Novel frameshift variant (c.409dupG) in SLC25A38 is a common cause of congenital sideroblastic anaemia in the Indian subcontinent
Ravindra, N., Aaron, R., Eswari, S., Sumithra, S., Kulkarni, U. P., Fouzia, N. A., Korula, A., Velayudhan, S. R., George, B., & Edison, E. S. (2020) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2020-206647 · Cited by 8
Heme metabolism as an integral part of iron homeostasis
Lipiński, P., Starzyński, R. R., Styś, A., Gajowiak, A., & Staroń, R. (2014) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/17322693.1102284 · Cited by 8
Investigation of glutathione-derived electrostatic and hydrogen-bonding interactions and their role in defining Grx5 [2Fe–2S] cluster optical spectra and transfer chemistry
Sen, S., Bonfio, C., Mansy, S. S., & Cowan, J. A. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1525-5 · Cited by 8
Minimum Length of Homology Arms Required for Effective Red/ET Recombination
Fujimoto, R., OSAKABE, T., Saito, M., Kurosawa, N., & Isobe, M. (2009) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90584 · Cited by 8
GLRX5-associated [Fe-S] cluster biogenesis disorder: further characterisation of the neurological phenotype and long-term outcome
Sankaran, B. P., Gupta, S. K., Tchan, M. C., Devanapalli, B., Rahman, Y., Procopis, P., & Bhattacharya, K. (2021) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-021-02073-z · Cited by 7
Purification and characterization of sideroblasts from patients with acquired and hereditary sideroblastic anaemia
Martin, F. M., Prchal, J. T., Nieva, J. J., Saven, A., Andrey, J., Bethel, K. J., Barton, J. C., Aripally, G., Bottomley, S. S., & Friedman, J. S. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07358.x · Cited by 7
Thioredoxins and Glutaredoxins. Functions and Metal Ion Interactions
Lillig, C. H., & Berndt, C. (2009) · Royal Society of Chemistry eBooks · doi:10.1039/9781847559531-00413 · Cited by 7
Iron rusting in the mitochondria?
Gattermann, N. (2016) · Blood · doi:10.1182/blood-2016-08-732966 · Cited by 6
Molecular Characterization and Expression Analysis of Glutaredoxin 5 in Black Tiger Shrimp (Penaeus monodon) and Correlation Analysis Between the SNPs of PmGrx5 and Ammonia-N Stress Tolerance Trait
Fan, R., Jiang, S., Li, Y., Yang, Q., Jiang, S., Huang, J., Yang, L., Chen, X., & Zhou, F. (2022) · Frontiers in Marine Science · doi:10.3389/fmars.2022.909827 · Cited by 7
Cellular Iron Metabolism – The IRP/IRE Regulatory Network
Joshi, R. S., Moran, E. L., & Sánchez, M. (2012) · BiblioBoard Library Catalog (Open Research Library) · doi:10.5772/34987 · Cited by 6
Heme Biosynthesis and Its Disorders
Fuller, S. J., & Wiley, J. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-35762-3.00038-x · Cited by 6
The Role of Metal Ions in Mitochondria: From Energy Metabolism to Cell Destiny
Li, C., Liu, H., Mao, Q., Fu, J., Yin, Y., Zhu, L., Li, K., Li, R. Y., & Zhang, P. (2026) · Biological Trace Element Research · doi:10.1007/s12011-026-05112-7 · Cited by 5
Two new mutations in the GLRX5 gene cause sideroblastic anemia
Arias, A. F. M., Escribano-Serrat, S., Nieto, J. M., Salazar, F. M., Gradilla, P. R., Cuesta, C. B., & Fernández, F. A. G. (2023) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2023.102763 · Cited by 5
Iron Deficiency Caused by Intestinal Iron Loss—Novel Candidate Genes for Severe Anemia
Huettmann, C., Stelljes, M., Sivalingam, S., Fobker, M., Vrachimis, A., Exler, A., Wenning, C., Wempe, C., Penke, M., Buneß, A., et al. (2021) · Genes · doi:10.3390/genes12121869 · Cited by 5
Remission from transfusion‐dependence in a patient with congenital dyserythropoietic anemia (CDA) and increased intensity of iron chelation
Bergmann, A. K., Tamary, H., & Neufeld, E. J. (2009) · Pediatric Blood & Cancer · doi:10.1002/pbc.22204 · Cited by 5
Mendelian inheritance of anemia due to disturbed iron homeostasis
Camaschella, C., & Pagani, A. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.05.003 · Cited by 5
Self-citation
Loss and Recovery of Glutaredoxin 5 Is Inducible by Diet in a Murine Model of Diabesity and Mediated by Free Fatty Acids In Vitro
Petry, S. F., Römer, A., Rawat, D., Brunner, L., Lerch, N., Zhou, M., Grewal, R., Sharifpanah, F., Sauer, H., Eckert, G. P., et al. (2022) · Antioxidants · doi:10.3390/antiox11040788 · Cited by 5
Métabolisme du fer : physiologie et pathologie
Beaumont, C., & Girot, R. (2010) · Encyclopédie médico-chirurgicale. Hématologie · doi:10.1016/s1155-1984(10)49948-3 · Cited by 7
Disorders of Red Cells and Platelets
MBBS, F. B. J. B. (2014) · Wiley eBooks · doi:10.1002/9781118817322.ch8 · Cited by 5
The role of genetic testing in accurate diagnosis of X-linked sideroblastic anemia: novel ALAS2 mutations and the impact of X-chromosome inactivation
Solavera, D. J., Rámila, M., Ferrer-Cortés, X., Olivella, M., Venturi, V., Morado, M., Hernández‐Rodríguez, I., Khan, A., Pérez-Montero, S., Tornador, C., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-95590-x · Cited by 5
Surcharges héréditaires en fer
Brissot, P., Bardou‐Jacquet, E., Latournerie, M., Ropert, M., Island, M., Loréal, O., & Jouanolle, A. (2009) · Pathologie Biologie · doi:10.1016/j.patbio.2009.10.011 · Cited by 5
Thioredoxin and glutaredoxin systems under oxidative and nitrosative stress
Ren, X. (2017) · Figshare · Cited by 4
Morphology of blood cells
MBBS, F. B. J. B. (2021) · Wiley eBooks · doi:10.1002/9781119820307.ch3 · Cited by 4
Loss of Function of the Cytoplasmic Fe-S Assembly Protein CIAO1 Causes a Neuromuscular Disorder with Compromise of Nucleocytoplasmic Fe-S EnzymesPreprint
Maio, N., Orbach, R., Zaharieva, I. T., Töpf, A., Donkervoort, S. C., Munot, P., Mueller, J., Willis, T. A., Verma, S., Perić, S., et al. (2023) · medRxiv · doi:10.1101/2023.12.20.23300170 · Cited by 4
HSPA9 frameshift and loss‐of‐function mutations in a patient manifesting syndromic sideroblastic anemia and congenital anomalies
Watanabe, A., Fujiwara, T., Ohta, A., Shimizu, Y., & Tanaka, R. (2022) · Pediatric Blood & Cancer · doi:10.1002/pbc.29971 · Cited by 2
Molecular Identification of the Glutaredoxin 5 Gene That Plays Important Roles in Antioxidant Defense in Arma chinensis (Fallou)
Luo, Q., Shen, Z., Kanjana, N., Guo, X., Wu, H., & Zhang, L. (2024) · Insects · doi:10.3390/insects15070537 · Cited by 2
Disorders of Red Cell Production and the Iron-Loading Anemias
Rivella, S. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_16 · Cited by 2
Is Iron-Chelation Therapy Useful in Persons with Myelodysplastic Syndrome Receive?
Hershko, C., & Gale, R. P. (2011) · Open Journal of Blood Diseases · doi:10.4236/ojbd.2011.11002 · Cited by 2
Sideroblastic anemia
May, A. M. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7020-3147-2.00014-6 · Cited by 2
Anémies microcytaires rares
Puy, H., Manceau, H., Karim, Z., & Kannengiesser, C. (2016) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)30764-2 · Cited by 2
Hematologic Manifestations in Primary Mitochondrial Diseases
Selvanathan, A., Teo, J., & Sankaran, B. P. (2024) · Journal of Pediatric Hematology/Oncology · doi:10.1097/mph.0000000000002890 · Cited by 2
Disorders of Erythropoiesis, Granulopoiesis and Thrombopoiesis
MBBS, F. B. J. B., Clark, M. D. M., Lampert, I. A., & DM, B. S. W. (2001) · doi:10.1002/9780470757130.ch8 · Cited by 2
Disorders of Erythropoiesis, Granulopoiesis and Thrombopoiesis
MBBS, F. B. J. B., Clark, M. D. M., & DM, B. S. W. (2009) · doi:10.1002/9781444309782.ch8 · Cited by 2
Iron-Loading Anemias
Levy, M., & Ginzburg, Y. Z. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_11 · Cited by 1
Iron transport: From enterocyte to mitochondria
Özbek, N. Y. (2010) · Turkish Journal of Hematology · doi:10.5152/tjh.2010.20 · Cited by 1
Case report: Unveiling genetic and phenotypic variability in Nonketotic hyperglycinemia: an atypical early onset case associated with a novel GLRX5 variant
Marin, V., Lebreton, L., Guibet, C., Mesli, S., Redonnet‐Vernhet, I., Dexant, M., Lamireau, D., Roche, S., Gaschignard, M., Delmas, J., et al. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1432272 · Cited by 1
A deep dive into future therapies for microcytic anemias and clinical considerations
Rodrigues, F., Coman, T., Fouquet, G., Côté, F., Courtois, G., Maciel, T. T., & Hermine, O. (2023) · Expert Review of Hematology · doi:10.1080/17474086.2023.2206556 · Cited by 1
In vivo functions of mammalian glutaredoxin 2
Lönn, M. E. (2008) · Figshare · Cited by 1
Iron and Heme Transport and Trafficking
Yien, Y. Y., & Paw, B. H. (2004) · Wiley eBooks · doi:10.1002/9781119951438.eibc2117 · Cited by 1
Disorders of red cells and platelets
MBBS, F. B. J. B. (2021) · Wiley eBooks · doi:10.1002/9781119820307.ch8 · Cited by 1
DISORDERS OF ERYTHROPOIESIS, GRANULOPOIESIS AND THROMBOPOIESIS
MBBS, F. B. J. B., Clark, M. D. M., & DM, B. S. W. (2019) · doi:10.1002/9781119398929.ch8 · Cited by 1
Mitochondrial fatty acid synthesis is essential for coordinated energy transformationPreprint
Haumann, F., Evangelakos, I., Worthmann, A., Liebold, I., Kotschi, S., Bischoff, A. T., Neuhofer, C. M., Schweizer, M., Heine, M., Büchner, B., et al. (2023) · medRxiv · doi:10.1101/2023.04.03.23288010 · Cited by 1
Hereditary sideroblastic anemias
Barton, J. C., Edwards, C. Q., Phatak, P. D., Britton, R. S., & Bacon, B. R. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511777035.027
Non-transferrin-bound iron in hematopoietic stem cell transplantation
Sahlstedt, L. (2015) · Työväentutkimus Vuosikirja
Zebrafish Models of Heme Synthesis and Iron Metabolism
Fraenkel, P. G. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_31
Surcharges génétiques en fer
Brissot, P., Latournerie, M., Bardou‐Jacquet, E., Loréal, O., Jouanolle, A., & Deugnier, Y. (2011) · EMC - Traité de médecine AKOS · doi:10.1016/s1634-6939(11)54630-7
Genetic and functional studies of hereditary myopathy with lactic acidosis
Nordin, A. (2011)
Genetic/Metabolic Effect of Iron Metabolism and Rare Anemias
Camaschella, C. (2013) · Thalassemia Reports · doi:10.4081/thal.2013.s1.e4
Self-citation
Causas genéticas de deficiência de ferro
Saad, S. T. O. (2010) · Revista Brasileira de Hematologia e Hemoterapia · doi:10.1590/s1516-84842010005000067
Isoforms of mammalian Glutaredoxin 2
Hudemann, C. (2009) · Figshare
IRON OVERLOAD: CAUSES, CONSEQUENCES, AND CONTROL
Bentley, D. P. (2014) · DOAJ (DOAJ: Directory of Open Access Journals)
Novel Molecules that Regulate Bone Formation and Bone Resorption
Linares, G. R. (2011) · The Scholars Repository - LLU (Loma Linda University)
Defining the Role of Hem25 in Mitochondrial Function: Implications for Congenital Sideroblastic Anemia
Dufay, J. N. (2015) · DalSpace (Dalhousie University)
immunodeficiency, periodic fevers, and developmental delay (SIFD) A novel syndrome of congenital sideroblastic anemia, B-cell
Bonney, D. K., Bottomley, S. S., Fleming, M. D., Kannengiesser, C., Thuret, I., Thompson, A. A., Marques, L., Giardina, P. J., Klaassen, R. J., Chakraborty, P. K., et al. (2013)
A metabolomics analysis to define the source of heme precursors during erythropoiesis
Burch, J. S. (2016)
Metabolizm hemu jako integralny element homeostazy żelaza* Heme metabolism as an integral part of iron homeostasis
Gajowiak, A. (2014)
[Advances in genes mutation and pathophysiology of congenital sideroblastic anemia].
Long, Z., Du, Y., & Han, B. (2016) · PubMed Central · doi:10.3760/cma.j.issn.0253-2727.2016.12.018
Assembly of Iron-Sulfur Clusters In Vivo
O’Carroll, I. P. (2009) · VTechWorks (Virginia Tech)
Nitric oxide cytotoxicity and functions of iron-sulfur enzymes in Escherichia coli
Ren, B. (2009) · Louisiana State University · doi:10.31390/gradschool_dissertations.3786
Hereditary sideroblastic anemia: pathophysiology and gene mutations
Furuyama, H. H. (2010)
Genetic Testing for Disorders of Iron Homeostasis
Barton, J. C., Lee, P. L., & Edwards, C. Q. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_26
HSPA9 frameshift and loss-of-function mutations in a patient manifesting syndromic sideroblastic anemia and various congenital anomaliesPreprint
Watanabe, A., Fujiwara, T., Ohta, A., Shimizu, Y., & Tanaka, R. (2022) · doi:10.22541/au.165009783.33851650/v1
Mitochondrial dysfunction and its consequences in the context of neurodegeneration
Key, J. (2021) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.62414
Functional plasticity in the thioredoxin family: FeS-thio- and glutaredoxins
Berndt, C., Wilms, C., Bodnar, Y., Gellert, M., & Lillig, C. H. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00002-9
Glutathione: Chemistry and Biochemistry
Perjési, P. (2023) · MDPI eBooks · doi:10.3390/books978-3-0365-8666-3
Naskórkowy czynnik Foxn1 regulatorem obrony antyoksydacyjnej skóry
Machcińska-Zielińska, S., & Gawrońska‐Kozak, B. (2023) · Postępy Biochemii · doi:10.18388/pb.2021_503
DISORDERS OF ERYTHROPOIESIS, GRANULOPOIESIS AND THROMBOPOIESIS
Barbara J. Bain MBBS, F., David M. Clark MD, M. (., Bridget S. Wilkins DM, P., & Vishakha Sovani MBBS, M. (2024) · doi:10.1002/9781394244843.ch8
Infant With a Severe Form of GLRX5 -Related Atypical Hyperglycinemia Exhibiting Novel Cardiac and Neurologic Disease Manifestations at Autopsy
Ferreira, E. O., Bigio, M. R. D., Morin, J., & Frosk, P. (2025) · Pediatric and Developmental Pathology · doi:10.1177/10935266251335065
Sideroblastic anemias
Cazzola, M. (2009) · Hematology Meeting Reports · doi:10.4081/hmr.v1i6.677
Meta-analysis of liver transcriptomic data identifies accurate disease classifiers and disease perturbed networks
Wang, Y. (2011) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
Suivi et traitement d’une hémochromatose
Brissot, P., Lan, C. L., & Bardou‐Jacquet, E. (2009) · Springer eBooks · doi:10.1007/978-2-287-99247-6_19
History of iron overload disorders
Barton, J. C., Edwards, C. Q., Phatak, P. D., Britton, R. S., & Bacon, B. R. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511777035.003
Congenital sideroblastic anemia: Unravelling molecular pathogenesis and advancing precision therapeutics
Zhao, D., Yang, J., Meng, D., Liu, L., Ge, J., Shi, X., & Long, Z. (2026) · Gene · doi:10.1016/j.gene.2026.150120

Authors: Camaschella, C., Campanella, A., De Falco, L., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., & Iolascon, A.
Affiliations: IRCCS San Raffaele Roma (IT)
Vita-Salute University and
Centre of Genetics Engineering (CEINGE) Advanced Biotechnologies, Naples;
CEINGE Biotecnologie Avanzate Franco Salvatore (Italy) (IT)
University of Turin (IT)
ORCID: Camaschella, Clara
Campanella, Alessandro
Silvestri, Laura
Levi, Sonia
Iolascon, Achille
Venue: Blood
Publisher: American Society of Hematology
Published: 2007-08-15
Volume: 110
Issue: 4
Pages: 1353-1358
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood-2007-02-072520
OpenAlex: W2095232221
Cited by: 306
References: 23
Citations by year: 2026: 3 · 2025: 4 · 2024: 7 · 2023: 10 · 2022: 12 · 2021: 13 · 2020: 17 · 2019: 12 · 2018: 11 · 2017: 18 · 2016: 15 · 2015: 14 · 2014: 27 · 2013: 21 · 2012: 15
FWCI: 16.90
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
PubMed (publishedVersion)
Archivio Istituzionale della Ricerca - Università Vita-Salute San Raffaele (submittedVersion)
Funders: Ministero dell’Istruzione, dell’Università e della Ricerca
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords: sideroblastic anemia, iron overload, microcytic anemia, iron regulatory protein 1, IRP2, transferrin receptor 1, heme biosynthesis, ALAS2, ferritin, iron chelation, zebrafish model, human disease
MeSH terms: Aconitate Hydratase, Anemia, Sideroblastic, Cells, Cultured, Enzyme-Linked Immunosorbent Assay, Humans, Male, Middle Aged, Mitochondria, Mutation, Oxidoreductases, Blotting, Western, Iron Overload, Reverse Transcriptase Polymerase Chain Reaction, Immunoprecipitation, Glutaredoxins

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

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

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