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

Iron-sulfur clusters: nature's modular, multipurpose structures

Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944 · see citing works

Balancing Acts

Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works

Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.

Mootha, V. K., Bunkenborg, J., Olsen, J. V., Hjerrild, M., Wisniewski, J. R., Stahl, E., Bolouri, M. S., Ray, H. N., Sihag, S., Kamal, M., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00926-7 · Cited by 889 · see citing works

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins

Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works

Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System

Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670 · see citing works

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 · see citing works

Mutation of a Putative Mitochondrial Iron Transporter Gene (ABC7) in X-Linked Sideroblastic Anemia and Ataxia (XLSA/A)

Allikmets, R. L., Raskind, W. H., Hutchinson, A. A., Schueck, N. D., Dean, M. C., & Koeller, D. M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.5.743 · Cited by 406 · see citing works

Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p

Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg446 · Cited by 383 · see citing works

Maturation of cellular Fe–S proteins: an essential function of mitochondria

Lill, R., & Kispal, G. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01589-9 · Cited by 358 · see citing works

Antioxidative stress–associated genes in circulating progenitor cells: evidence for enhanced resistance against oxidative stress

Dernbach, E., Urbich, C., Brandes, R. P., Hofmann, W. K., Zeiher, A. M., & Dimmeler, S. (2004) · Blood · doi:10.1182/blood-2003-12-4103 · Cited by 331 · see citing works

Maturation of cellular Fe-S proteins: an essential function of mitochondria

Gray, H. B. (2000) · Cited by 307 · see citing works

Prostate-specific Antigen Expression Is Regulated by an Upstream Enhancer

Schuur, E. R., Henderson, G. A., Kmetec, L. A., Miller, J. D., Lamparski, H., & Henderson, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.7043 · Cited by 302 · see citing works

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 · see citing works

Iron trafficking in the mitochondrion: novel pathways revealed by disease

Napier, I. A., Ponka, P., & Richardson, D. R. (2004) · Blood · doi:10.1182/blood-2004-10-3856 · Cited by 287 · see citing works

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 · see citing works

Characterization of zebrafish mutants with defects in embryonic hematopoiesis

Ransom, D. G., Haffter, P., Odenthal, J., Brownlie, A., Vogelsang, E., Kelsh, R. N., Brand, M., van Eeden, F. J. M., Furutani-Seiki, M., Granato, M., et al. (1996) · Development · doi:10.1242/dev.123.1.311 · Cited by 264 · see citing works

Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia

Brownlie, A., Donovan, A., Pratt, S. J. P., Paw, B. H., Oates, A. C., Brugnara, C., Witkowska, H. E., Sassa, S., & Zon, L. I. (1998) · Nature Genetics · doi:10.1038/3049 · Cited by 244 · see citing works

Iron-sulfur clusters as biosensors of oxidants and iron.

Rouault, T. A., & Klausner, R. D. (1996) · PubMed · Cited by 238 · see citing works

Iron-sulfur clusters as biosensors of oxidants and iron

Rouault, T. A., & Klausner, R. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10024-4 · Cited by 207 · see citing works

Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells

Tong, W., & Rouault, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5692 · Cited by 194 · see citing works

Targeting of a Human Iron–Sulfur Cluster Assembly Enzyme, nifs, to Different Subcellular Compartments Is Regulated through Alternative AUG Utilization

Land, T., & Rouault, T. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80295-6 · Cited by 180 · see citing works

Biochemical Characterization of Yeast Mitochondrial Grx5 Monothiol Glutaredoxin

Tamarit, J., Bellı́, G., Cabiscol, E., Herrero, E., & Ros, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303477200 · Cited by 129 · see citing works

Iron Regulatory Proteins 1 and 2 Bind Distinct Sets of RNA Target Sequences

Henderson, B. R., Menotti, E., & Kühn, L. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4900 · Cited by 112 · see citing works

Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload

Nakajima, O., Takahashi, S., Harigae, H., Furuyama, K., Hayashi, N., Sassa, S., & Yamamoto, M. P. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6282 · Cited by 108 · see citing works

The interaction between the iron-responsive element binding protein and its cognate RNA is highly dependent upon both RNA sequence and structure

Jaffrey, S. R., Haile, D. J., Klausner, R. D., & Harford, J. B. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.19.4627 · Cited by 103 · see citing works

Erythropoietic and hepatic porphyrias

Groß, U., Hoffmann, G. F., & Manfred Otto, D. O. S. S. (2000) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005645624262 · Cited by 83 · see citing works

Structure-Function Analysis of Yeast Grx5 Monothiol Glutaredoxin Defines Essential Amino Acids for the Function of the Protein

Bellı́, G., Polaina, J., Tamarit, J., de la Torre-Ruiz, M. Á., Rodríguez‐Manzaneque, M. T., Ros, J., & Herrero, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201688200 · Cited by 74 · see citing works

X‐linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L

Maguire, A., Hellier, K. D., Hammans, S. R., & May, A. M. (2001) · British Journal of Haematology · doi:10.1046/j.1365-2141.2001.03015.x · Cited by 72 · see citing works

The chianti zebrafish mutant provides a model for erythroid-specific disruption of transferrin receptor 1

Wingert, R. A., Brownlie, A., Galloway, J. L., Dooley, K. A., Fraenkel, P. G., Axe, J. L., Davidson, A. J., Barut, B., Noriega, L., Sheng, X., et al. (2004) · Development · doi:10.1242/dev.01540 · Cited by 65 · see citing works

Evolution and cellular function of monothiol glutaredoxins: involvement in iron–sulphur cluster assembly

Vilella, F., Alves, R., Rodríguez‐Manzaneque, M. T., Bellí, G., Swaminathan, S., Sunnerhagen, P., & Herrero, E. (2004) · Comparative and Functional Genomics · doi:10.1002/cfg.406 · Cited by 54 · see citing works

Genetic analysis of iron citrate toxicity in yeast: Implications for mammalian iron homeostasis

Chen, O. S., Hemenway, S., & Kaplan, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232392299 · Cited by 49 · see citing works

Predictive reconstruction of the mitochondrial iron‐sulfur cluster assembly metabolism. II. Role of glutaredoxin Grx5

Alves, R., Herrero, E., & Albert Sorribas, B. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20228 · Cited by 33 · see citing works

Differential gene expression during early murine yolk sac development

Palis, J., & Kingsley, P. D. (1995) · Molecular Reproduction and Development · doi:10.1002/mrd.1080420104 · Cited by 29 · see citing works

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production

Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459 · see citing works

A Red carpet for iron metabolism

Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319 · see citing works

Function and biogenesis of iron-sulphur proteins

Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167 · see citing works

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes

Deponte, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.018 · Cited by 1,104 · see citing works

The role of iron regulatory proteins in mammalian iron homeostasis and disease

Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055 · see citing works

Regulation of cellular iron metabolism

Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works

Mechanisms controlling cellular and systemic iron homeostasis

Galy, B., Conrad, M., & Muckenthaler, M. U. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00648-1 · Cited by 806 · see citing works

Thioredoxin and Related Molecules–From Biology to Health and Disease

Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724 · see citing works

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 · see citing works

Thioredoxins, Glutaredoxins, and Peroxiredoxins—Molecular Mechanisms and Health Significance: from Cofactors to Antioxidants to Redox Signaling

Hanschmann, E., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 649 · see citing works

Forging a field: the golden age of iron biology.

Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases

Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 595 · see citing works

The Role of Glutathione in Photosynthetic Organisms: Emerging Functions for Glutaredoxins and Glutathionylation

Rouhier, N., Lemaire, S. D., & Jacquot, J. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092811 · Cited by 571 · see citing works

Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol

Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536 · see citing works

Glutaredoxin systems

Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 563 · see citing works

Mammalian iron metabolism and its control by iron regulatory proteins

Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works

Biosynthesis of heme in mammals

Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493 · see citing works

The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism

Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · see citing works

Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology

Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 482 · see citing works

Redox control and oxidative stress in yeast cells

Herrero, E., Ros, J., Bellı́, G., & Cabiscol, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.004 · Cited by 488 · see citing works

Reactive Oxygen Species: Impact on Skeletal Muscle

Powers, S. K., Ji, L. L., Kavazis, A. N., & Jackson, M. J. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100054 · Cited by 508 · see citing works

Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes

Chiabrando, D., Vinchi, F., Fiorito, V., Mercurio, S., & Tolosano, E. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00061 · Cited by 455 · see citing works

Iron–sulfur cluster biogenesis and human disease

Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 387 · see citing works

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 · see citing works

Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms

Lill, R., & Mühlenhoff, U. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104538 · Cited by 365 · see citing works

Regulation of Mitochondrial Iron Import through Differential Turnover of Mitoferrin 1 and Mitoferrin 2

Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362 · see citing works

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system

Berndt, C., Lillig, C. H., & Holmgren, A. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01162.2006 · Cited by 350 · see citing works

Mitochondrial Thiols in Antioxidant Protection and Redox Signaling: Distinct Roles for Glutathionylation and Other Thiol Modifications

Murphy, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 338 · see citing works

Genes of the antioxidant system of the honey bee: annotation and phylogeny

Corona, M., & Robinson, G. E. (2006) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2006.00695.x · Cited by 313 · see citing works

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

Camaschella, C., Campanella, A., De Falco, L., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., & Iolascon, A. (2007) · Blood · doi:10.1182/blood-2007-02-072520 · Cited by 306 · see citing works

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 301 · see citing works

Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis

Tong, W.-H., & Rouault, T. A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.003 · Cited by 294 · see citing works

Iron sensing and signalling

Evstatiev, R., & Gasché, C. (2011) · Gut · doi:10.1136/gut.2010.214312 · Cited by 292 · see citing works

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 · see citing works

Thioredoxins and glutaredoxins as facilitators of protein folding

Berndt, C., Lillig, C. H., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.02.003 · Cited by 273 · see citing works

Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters

Bandyopadhyay, S., Gama, F., Molina‐Navarro, M. M., Gualberto, J. M., Claxton, R., Naik, S., Huynh, B. H., Herrero, E., Jacquot, J., Johnson, M. K., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.50 · Cited by 267 · see citing works

Protoporphyrin IX: the Good, the Bad, and the Ugly

Sachar, M., Anderson, K. E., & Ma, X. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.228130 · Cited by 259 · see citing works

Mitochondrial iron–sulfur protein biogenesis and human disease

Stehling, O., Wilbrecht, C., & Lill, R. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.010 · Cited by 272 · see citing works

A precious metal: Iron, an essential nutrient for all cells

Cairo, G., Bernuzzi, F., & Recalcati, S. (2006) · Genes & Nutrition · doi:10.1007/bf02829934 · Cited by 252 · see citing works

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 239 · see citing works

Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease

Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · Cited by 238 · see citing works

The Role of Mitochondria in Cellular Iron-Sulfur Protein Biogenesis: Mechanisms, Connected Processes, and DiseasesPreprint

Stehling, O., & Lill, R. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011312 · Cited by 228 · see citing works

Monothiol glutaredoxins: a common domain for multiple functions

Herrero, E., & de la Torre-Ruiz, M. Á. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6554-8 · Cited by 226 · see citing works

Mechanistic and Kinetic Details of Catalysis of Thiol-Disulfide Exchange by Glutaredoxins and Potential Mechanisms of Regulation

Gallogly, M. M., Starke, D. W., & Mieyal, J. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2291 · Cited by 224 · see citing works

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Maio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 215 · see citing works

Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis

Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 213 · see citing works

The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation

Sheftel, A. D., Wilbrecht, C., Stehling, O., Niggemeyer, B., Elsässer, H., Mühlenhoff, U., & Lill, R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0772 · Cited by 213 · see citing works

The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron–sulfur cluster biogenesis

Pondarré, C., Antiochos, B., Campagna, D. R., Clarke, S. L., Greer, E. L., Deck, K. M., McDonald, A. A., Han, A., Medlock, A. E., Kutok, J. L., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl012 · Cited by 208 · see citing works

Splice Mutation in the Iron-Sulfur Cluster Scaffold Protein ISCU Causes Myopathy with Exercise Intolerance

Mochel, F., Knight, M. A., Tong, W.-H., Hernandez, D. G., Ayyad, K., Taivassalo, T., Andersen, P. M., Singleton, A., Rouault, T. A., Fischbeck, K. H., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.12.012 · Cited by 208 · see citing works

Glutaredoxins: roles in iron homeostasis

Rouhier, N., Couturier, J., Johnson, M. K., & Jacquot, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.08.005 · Cited by 209 · see citing works

Iron-sulfur cluster deficiency can be sensed by IRP2 and regulates iron homeostasis and sensitivity to ferroptosis independent of IRP1 and FBXL5

Terzi, E. M., Sviderskiy, V. O., Alvarez, S. W., Whiten, G. C., & Possemato, R. (2021) · Science Advances · doi:10.1126/sciadv.abg4302 · Cited by 195 · see citing works

Iron–sulfur proteins in health and disease

Sheftel, A. D., Stehling, O., & Lill, R. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.12.006 · Cited by 203 · see citing works

The role of iron in mitochondrial function

Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 195 · see citing works

Mitochondrial iron metabolism and its role in neurodegeneration

Horowitz, M. P., & Greenamyre, J. T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100354 · Cited by 195 · see citing works

Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe–2S] cluster in poplar glutaredoxin C1

Rouhier, N., Unno, H., Bandyopadhyay, S., Masip, L., Kim, S., Hirasawa, M., Gualberto, J. M., Lattard, V., Kusunoki, M., Knaff, D. B., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702268104 · Cited by 194 · see citing works

Glutaredoxin: Discovery, redox defense and much more

Ogata, F. T., Branco, V., Vale, F. F., & Coppo, L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101975 · Cited by 189 · see citing works

Genome-wide analysis of plant glutaredoxin systems

Rouhier, N. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erl001 · Cited by 189 · see citing works

Selective Translational Control of the Alzheimer Amyloid Precursor Protein Transcript by Iron Regulatory Protein-1

Cho, H.-H., Cahill, C. M., Vanderburg, C. R., Scherzer, C. R., Wang, B., Huang, X., & Rogers, J. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149161 · Cited by 188 · see citing works

Iron and Copper in Mitochondrial Diseases

Xu, W., Barrientos, T., & Andrews, N. C. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.004 · Cited by 182 · see citing works

Heme and erythropoieis: more than a structural role

Chiabrando, D., Mercurio, S., & Tolosano, E. (2014) · Haematologica · doi:10.3324/haematol.2013.091991 · Cited by 192 · see citing works

Mitochondrial Glutathione: Regulation and Functions

Calabrese, G., Morgan, B., & Riemer, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7121 · Cited by 182 · see citing works

Zebrafish in hematology: sushi or science?

Carradice, D., & Lieschke, G. J. (2008) · Blood · doi:10.1182/blood-2007-10-052761 · Cited by 176 · see citing works

[4Fe-4S] Cluster Assembly in Mitochondria and Its Impairment by Copper

Brancaccio, D., Gallo, A., Piccioli, M., Novellino, E., Ciofi‐Baffoni, S., & Banci, L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09567 · Cited by 170 · see citing works

Mechanisms of iron–sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes

Lill, R., Dutkiewicz, R., Elsässer, H., Hausmann, A., Netz, D. J. A., Pierik, A. J., Stehling, O., Urzica, E. I., & Mühlenhoff, U. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.011 · Cited by 170 · see citing works

Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways

Rouault, T. A., & Maio, N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.789537 · Cited by 160 · see citing works

The system biology of thiol redox system in Escherichia coli and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis

Tolédano, M. B., Kumar, C., Moan, N. L., Spector, D., & Tacnet, F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.07.002 · Cited by 159 · see citing works

Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis

Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 158 · see citing works

Protein Tyrosine Phosphorylation and Protein Tyrosine Nitration in Redox Signaling

Monteiro, H. P., Arai, R. J., & Travassos, L. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1853 · Cited by 157 · see citing works

The Impact of Iron Overload and Ferroptosis on Reproductive Disorders in Humans: Implications for Preeclampsia

Ng, S., Norwitz, S. G., & Norwitz, E. R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133283 · Cited by 158 · see citing works

RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload

Cavadini, P., Biasiotto, G., Poli, M., Levi, S., Verardi, R., Zanella, I., Derosas, M., Ingrassia, R., Corrado, M., & Arosio, P. (2006) · Blood · doi:10.1182/blood-2006-08-041632 · Cited by 155 · see citing works

Molecular basis of inherited microcytic anemia due to defects in iron acquisition or heme synthesis

Iolascon, A., Falco, L. D., & Beaumont, C. (2009) · Haematologica · doi:10.3324/haematol.13619 · Cited by 153 · see citing works

AtGRXcp, an Arabidopsis Chloroplastic Glutaredoxin, Is Critical for Protection against Protein Oxidative Damage

Cheng, N., Liu, J., Brock, A. M., Nelson, R. S., & Hirschi, K. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601354200 · Cited by 150 · see citing works

Reversible Sequestration of Active Site Cysteines in a 2Fe-2S-bridged Dimer Provides a Mechanism for Glutaredoxin 2 Regulation in Human Mitochondria

Johansson, C., Kavanagh, K. L., Gileadi, O., & Oppermann, U. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608179200 · Cited by 147 · see citing works

Monothiol CGFS Glutaredoxins and BolA-like Proteins: [2Fe-2S] Binding Partners in Iron Homeostasis

Li, H., & Outten, C. E. (2012) · Biochemistry · doi:10.1021/bi300393z · Cited by 148 · see citing works

Involvement of thio-, peroxi-, and glutaredoxins in cellular redox-dependent processes

Kalinina, E. V., Chernov, N., & Saprin, A. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908130099 · Cited by 159 · see citing works

Potential Role of Sulfur-Containing Antioxidant Systems in Highly Oxidative Environments

Mukwevho, E., Ferreira, Z., & Ayeleso, A. O. (2014) · Molecules · doi:10.3390/molecules191219376 · Cited by 143 · see citing works

Glutathione, Glutaredoxins, and Iron

Berndt, C., & Lillig, C. H. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7132 · Cited by 141 · see citing works

Systematic molecular genetic analysis of congenital sideroblastic anemia: Evidence for genetic heterogeneity and identification of novel mutations

Bergmann, A. K., Campagna, D. R., McLoughlin, E. M., Agarwal, S., Fleming, M. D., Bottomley, S. S., & Neufeld, E. J. (2009) · Pediatric Blood & Cancer · doi:10.1002/pbc.22244 · Cited by 139 · see citing works

Redox Regulation via Glutaredoxin-1 and Protein S -Glutathionylation

Matsui, R., Ferrán, B., Oh, A., Croteau, D., Shao, D., Han, J., Pimentel, D. R., & Bachschmid, M. M. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7963 · Cited by 139 · see citing works

Redox Regulation of Cell Survival by the Thioredoxin Superfamily: An Implication of Redox Gene Therapy in the Heart

Ahsan, M., Lekli, I., Ray, D., Yodoi, J., & Das, D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2683 · Cited by 134 · see citing works

Iron and Porphyrin Trafficking in Heme Biogenesis

Schultz, I. J., Chen, C., Paw, B. H., & Hamza, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.119503 · Cited by 129 · see citing works

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation

Uzarska, M. A., Dutkiewicz, R., Freibert, S., Lill, R., & Mühlenhoff, U. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0644 · Cited by 128 · see citing works

Erythroid Heme Biosynthesis and Its DisordersPreprint

Dailey, H. A., & Meissner, P. N. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011676 · Cited by 127 · see citing works

Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

Michelet, L., Zaffagnini, M., Massot, V., Keryer, E., Vanacker, H., Miginiac-Maslow, M., Issakidis-Bourguet, E., & Lemaire, S. (2006) · Photosynthesis Research · doi:10.1007/s11120-006-9096-2 · Cited by 120 · see citing works

Redox atlas of the mouse

Godoy, J. R., Funke, M., Ackermann, W., Haunhorst, P., Oesteritz, S., Capani, F., Elsässer, H., & Lillig, C. H. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.05.006 · Cited by 124 · see citing works

The crystal structure of human GLRX5: iron–sulfur cluster co-ordination, tetrameric assembly and monomer activity

Johansson, C., Roos, A. K., Montaño, S., Sengupta, R., Filippakopoulos, P., Guo, K., von Delft, F., Holmgren, A., Oppermann, U. C. T., & Kavanagh, K. L. (2010) · Biochemical Journal · doi:10.1042/bj20101286 · Cited by 123 · see citing works

The roles of glutaredoxins ligating Fe–S clusters: Sensing, transfer or repair functions?

Couturier, J., Przybyla‐Toscano, J., Roret, T., Claude Didierjean, B., & Rouhier, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.018 · Cited by 122 · see citing works

Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells

Philpott, C. C., Ryu, M., Frey, A. G., & Patel, S. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.791962 · Cited by 125 · see citing works

Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development

Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 123 · see citing works

The molecular genetics of sideroblastic anemia

Ducamp, S., & Fleming, M. D. (2019) · Blood · doi:10.1182/blood-2018-08-815951 · Cited by 136 · see citing works

Protein networks in the maturation of human iron–sulfur proteins

Ciofi‐Baffoni, S., Nasta, V., & Banci, L. (2017) · Metallomics · doi:10.1039/c7mt00269f · Cited by 116 · see citing works

Zebrafish nephrogenesis involves dynamic spatiotemporal expression changes in renal progenitors and essential signals from retinoic acid and irx3b

Wingert, R. A., & Davidson, A. J. (2011) · Developmental Dynamics · doi:10.1002/dvdy.22691 · Cited by 118 · see citing works

Iron-regulatory proteins: molecular biology and pathophysiological implications

Cairo, G., & Recalcati, S. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000531 · Cited by 124 · see citing works

Genome-wide expression analysis suggests glutaredoxin genes response to various stresses in cotton

Malik, W. A., Wang, X., Wang, X., Shu, N., Cui, R., Chen, X., Wang, D., Lu, X., Yin, Z., Wang, J., et al. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.021 · Cited by 113 · see citing works

Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery

Crooks, D. R., Ghosh, M. C., Haller, R. G., Tong, W.-H., & Rouault, T. A. (2009) · Blood · doi:10.1182/blood-2009-09-243105 · Cited by 112 · see citing works

Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis

Hausmann, A., Samans, B., Lill, R., & Mühlenhoff, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705570200 · Cited by 111 · see citing works

Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation

Haunhorst, P., Hanschmann, E.-M., Bräutigam, L., Stehling, O., Hoffmann, B., Mühlenhoff, U., Lill, R., Berndt, C., & Lillig, C. H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0648 · Cited by 111 · see citing works

Nucleoredoxin, a Novel Thioredoxin Family Member Involved in Cell Growth and Differentiation

Funato, Y., & Miki, H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1550 · Cited by 114 · see citing works

Mitochondrial [4Fe-4S] protein assembly involves reductive [2Fe-2S] cluster fusion on ISCA1–ISCA2 by electron flow from ferredoxin FDX2

Weiler, B. D., Brück, M.-C., Kothe, I., Bill, E., Lill, R., & Mühlenhoff, U. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003982117 · Cited by 110 · see citing works

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

Portrait of anaemia in sir zebrafish

Amoils, S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1751

Erythropoiesis and Iron Sulfur Cluster Biogenesis

Ye, H., & Rouault, T. A. (2010) · Advances in Hematology · doi:10.1155/2010/329394 · Cited by 44 · see citing works

doi:10.1155/2010/329394 Review Article Erythropoiesis and Iron Sulfur Cluster Biogenesis

Ye, H., & Rouault, T. A. (2013)

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 239 · see citing works