Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms

Global analysis of protein expression in yeast

Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750

Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786

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

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

Structure, function, and formation of biological iron-sulfur clusters

Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438 · cited 4×

The WD repeat: a common architecture for diverse functions

Smith, T. F., Gaitatzes, C. G., Saxena, K., & Neer, E. J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01384-5 · Cited by 1,256

Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin

Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921

Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits

Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738

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

Assembly of Iron-Sulfur Clusters

Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 650

Occurrence, Classification, and Biological Function of Hydrogenases: An Overview

Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,617

Function and biogenesis of iron-sulphur proteins

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

Evolution of Photosynthesis

Hohmann-Marriott, M. F., & Blankenship, R. E. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042110-103811 · Cited by 744

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

Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 694

Mitochondrial metabolism promotes adaptation to proteotoxic stress

Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645

Plastid evolution

Gould, S. B., Waller, R. F., & McFadden, G. I. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092915 · Cited by 634

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 605

Copper and iron disorders of the brain

Madsen, E., & Gitlin, J. D. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094232 · Cited by 557

Intracellular iron transport and storage: from molecular mechanisms to health implications

Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526

Cristae formation—linking ultrastructure and function of mitochondria

Zick, M., Rabl, R., & Reichert, A. S. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.06.013 · Cited by 506

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 467

Mitochondria-targeted antioxidants for treatment of Parkinson's disease: Preclinical and clinical outcomes

Jin, H., Kanthasamy, A., Ghosh, A., Anantharam, V., Kalyanaraman, B., & Kanthasamy, A. G. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.007 · Cited by 372

Cell biology of molybdenum

Mendel, R. R., & Bittner, F. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.03.013 · Cited by 365

Mammalian iron transport

Anderson, G. J., & Vulpe, C. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0051-1 · Cited by 317

MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone

Paddock, M. L., Wiley, S. E., Axelrod, H. L., Cohen, A. E., Roy, M., Abresch, E. C., Capraro, D. T., Murphy, A. N., Nechushtai, R., Dixon, J. E., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707189104 · Cited by 307

Ascorbate as seen through plant evolution: the rise of a successful molecule?

Gest, N., Gautier, H., & Stevens, R. G. (2012) · Journal of Experimental Botany · doi:10.1093/jxb/ers297 · Cited by 301

Structural Insights into Radical Generation by the Radical SAM Superfamily

Vey, J. L., & Drennan, C. L. (2011) · Chemical Reviews · doi:10.1021/cr9002616 · Cited by 254

Biogenesis of cytosolic and nuclear iron–sulfur proteins and their role in genome stability

Paul, V. D., & Lill, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.018 · Cited by 251

Metabolic Impairment in Heart Failure

Doehner, W., Frenneaux, M. P., & Anker, S. D. (2014) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2014.04.083 · Cited by 241

A cysteine-selective fluorescent probe for the cellular detection of cysteine

Jung, H. S., Han, J. H., Pradhan, T., Kim, S., Lee, S. W., Sessler, J. L., Kim, T. W., Kang, C., & Kim, J. S. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.10.040 · Cited by 233

Transition metal homeostasis: from yeast to human disease

Bleackley, M. R., & MacGillivray, R. T. A. (2011) · BioMetals · doi:10.1007/s10534-011-9451-4 · Cited by 240

Localization and functionality of microsporidian iron–sulphur cluster assembly proteins

Goldberg, A. V., Molik, S., Tsaousis, A. D., Neumann, K., Kuhnke, G., Delbac, F., Vivarès, C. P., Hirt, R. P., Lill, R., & Embley, T. M. (2008) · Nature · doi:10.1038/nature06606 · Cited by 230

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

Identification of FRA1 and FRA2 as Genes Involved in Regulating the Yeast Iron Regulon in Response to Decreased Mitochondrial Iron-Sulfur Cluster Synthesis

Kumánovics, A., Chen, O. S., Li, L., Bagley, D., Adkins, E. M., Lin, H., Dingra, N. N., Outten, C. E., Keller, G., Winge, D. R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801160200 · Cited by 215

Multi-Copper Oxidases and Human Iron Metabolism

Vashchenko, G., & MacGillivray, R. T. A. (2013) · Nutrients · doi:10.3390/nu5072289 · Cited by 223

Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer

Fontecave, M., & de Choudens, S. O. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.12.014 · Cited by 215

Small RNA‐induced differential degradation of the polycistronic mRNA iscRSUA

Desnoyers, G., Morissette, A., Prévost, K., & Massé, É. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.116 · Cited by 200

Organelles in Blastocystis that Blur the Distinction between Mitochondria and Hydrogenosomes

Stechmann, A., Hamblin, K. A., Pérez‐Brocal, V., Gaston, D., Richmond, G. S., van der Giezen, M., Clark, C. G., & Roger, A. J. (2008) · Current Biology · doi:10.1016/j.cub.2008.03.037 · Cited by 208

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 202

Structure–function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease

Tamir, S., Paddock, M. L., Darash-Yahana-Baram, M., Holt, S. H., Sohn, Y. S., Agranat-Tamir, L., Michaeli, D., Stofleth, J. T., Lipper, C. H., Morcos, F., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.014 · Cited by 198

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

Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation

Vickery, L. E., & Cupp‐Vickery, J. R. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701322298 · Cited by 188

Mitochondrial Proteomics of the Retinal Pigment Epithelium at Progressive Stages of Age-Related Macular Degeneration

Nordgaard, C. L., Karunadharma, P. P., Feng, X., Olsen, T. W., & Ferrington, D. A. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-1352 · Cited by 194

Small ncRNA transcriptome analysis from Aspergillus fumigatus suggests a novel mechanism for regulation of protein synthesis

Jöchl, C., Rederstorff, M., Jana Hertel, A., Stadler, P. F., Hofacker, I. L., Schrettl, M., Haas, H., & Hüttenhofer, A. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn123 · Cited by 186

A Proteomic Survey of Chlamydomonas reinhardtii Mitochondria Sheds New Light on the Metabolic Plasticity of the Organelle and on the Nature of the -Proteobacterial Mitochondrial Ancestor

Atteia, A., Adrait, A., Brugière, S., Tardif, M., van Lis, R., Deusch, O., Dagan, T., Kühn, L., Gontero, B., Martin, W. F., et al. (2009) · Molecular Biology and Evolution · doi:10.1093/molbev/msp068 · Cited by 185

Maturation of cytosolic and nuclear iron–sulfur proteins

Netz, D. J. A., Mascarenhas, J., Stehling, O., Pierik, A. J., & Lill, R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.005 · Cited by 184

The human iron-proteome†

Andreini, C., Putignano, V., Rosato, A., & Banci, L. (2018) · Metallomics · doi:10.1039/c8mt00146d · Cited by 183

SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly

Layer, G., Gaddam, S. A., Ayala-Castro, C. N., de Choudens, S. O., Lascoux, D., Fontecave, M., & Outten, F. W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608555200 · Cited by 182

The Bacterial Response to the Chalcogen Metalloids Se and Te

Zannoni, D., Borsetti, F., Harrison, J. J., & Turner, R. J. (2007) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(07)53001-8 · Cited by 187

The Cfd1–Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol

Netz, D. J. A., Pierik, A. J., Stümpfig, M., Mühlenhoff, U., & Lill, R. (2007) · Nature Chemical Biology · doi:10.1038/nchembio872 · Cited by 174

Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism

Fox, N. G., Yu, X., Feng, X., Bailey, H., Martelli, A., Nabhan, J. F., Strain-Damerell, C. M., Bulawa, C., Yue, W. W., & Han, S. (2019) · Nature Communications · doi:10.1038/s41467-019-09989-y · Cited by 176

Specialized Function of Yeast Isa1 and Isa2 Proteins in the Maturation of Mitochondrial [4Fe-4S] Proteins

Mühlenhoff, U., Richter, N., Pines, O., Pierik, A. J., & Lill, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.296152 · Cited by 178

Iron–sulfur cluster biosynthesis

Bandyopadhyay, S., Chandramouli, K., & Johnson, M. K. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361112 · Cited by 179

Mitochondrial Iba57p Is Required for Fe/S Cluster Formation on Aconitase and Activation of Radical SAM Enzymes

Gelling, C. L., Dawes, I. W., Richhardt, N., Lill, R., & Mühlenhoff, U. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01963-07 · Cited by 170

Candida albicans Hap43 Is a Repressor Induced under Low-Iron Conditions and Is Essential for Iron-Responsive Transcriptional Regulation and Virulence

Hsu, P.-C., Yang, C.-Y., & Lan, C.-Y. (2011) · Eukaryotic Cell · doi:10.1128/ec.00158-10 · Cited by 157

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 156

ErpA, an iron–sulfur (Fe–S) protein of the A-type essential for respiratory metabolism in Escherichia coli

Loiseau, L., Gerez, C., Bekker, M., de Choudens, S. O., Py, B., Sanakis, Y., de Mattos, J. T., Fontecave, M., & Barras, F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705829104 · Cited by 154

Metabolic Pathways in the Apicoplast of Apicomplexa

Seeber, F., & Soldati‐Favre, D. (2010) · International review of cytology · doi:10.1016/s1937-6448(10)81005-6 · Cited by 152

Molecular modulated cysteine-selective fluorescent probe

Jung, H. S., Pradhan, T., Han, J. H., Heo, K. J., Lee, J. H., Kang, C., & Kim, J. S. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.08.009 · Cited by 154

NfuA, a New Factor Required for Maturing Fe/S Proteins in Escherichia coli under Oxidative Stress and Iron Starvation Conditions*

Angelini, S., Gerez, C., Choudens, S. O., Sanakis, Y., Fontecave, M., Barras, F., & Py, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709405200 · Cited by 141

Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron–Sulfur Cluster Biosynthesis

Cai, K., Tonelli, M., Frederick, R. O., & Markley, J. L. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b00447 · Cited by 148

From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme

Swenson, S. A., Moore, C. M., Marcero, J. R., Medlock, A. E., Reddi, A. R., & Khalimonchuk, O. (2020) · Cells · doi:10.3390/cells9030579 · Cited by 155

Glutathione, Glutaredoxins, and Iron

Berndt, C., & Lillig, C. H. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7132 · Cited by 148

DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster

Wu, Y., & Brosh, R. M. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks039 · Cited by 150

CGFS-Type Monothiol Glutaredoxins from the Cyanobacterium Synechocystis PCC6803 and Other Evolutionary Distant Model Organisms Possess a Glutathione-Ligated [2Fe-2S] Cluster

Picciocchi, A., Saguez, C., Boussac, A., Cassier‐Chauvat, C., & Chauvat, F. (2007) · Biochemistry · doi:10.1021/bi7013272 · Cited by 140

Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase

McCarthy, E. L., & Booker, S. J. (2017) · Science · doi:10.1126/science.aan4574 · Cited by 139

The functional duality of iron regulatory protein 1

Volz, K. W. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.12.010 · Cited by 138

Iron–sulphur clusters in nucleic acid processing enzymes

White, M. F., & Dillingham, M. S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.11.004 · Cited by 138

An Iron-Sulfur Cluster in the C-terminal Domain of the p58 Subunit of Human DNA Primase

Weiner, B. E., Huang, H., Dattilo, B. M., Nilges, M. J., Fanning, E., & Chazin, W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705826200 · Cited by 136

A Novel Role for Human Nfs1 in the Cytoplasm

Marelja, Z., Stöcklein, W., Nimtz, M., & Leimkühler, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804064200 · Cited by 136

Mechanistic study of mitochondria-dependent programmed cell death induced by aluminium phytotoxicity using fluorescence techniques

Li, Z., & Xing, D. (2010) · Journal of Experimental Botany · doi:10.1093/jxb/erq279 · Cited by 131

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 133

Thio-modification of Yeast Cytosolic tRNA Requires a Ubiquitin-related System That Resembles Bacterial Sulfur Transfer Systems

Nakai, Y., Nakai, M., & Hayashi, H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804043200 · Cited by 126

A Pathway of Protein Translocation in Mitochondria Mediated by the AAA-ATPase Bcs1

Wagener, N., Ackermann, M., Funes, S., & Neupert, W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.036 · Cited by 124

Iron-Based Redox Switches in Biology

Outten, F. W., & Theil, E. C. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2296 · Cited by 127

Structural Organization of Essential Iron-Sulfur Clusters in the Evolutionarily Highly Conserved ATP-binding Cassette Protein ABCE1

Barthelme, D., Scheele, U., Dinkelaker, S., Janoschka, A., MacMillan, F., Albers, S., Driessen, A. J. M., Salomone‐Stagni, M., Bill, E., Meyer‐Klaucke, W., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700825200 · Cited by 122

Biogenesis of the cytochrome bc1 complex and role of assembly factors

Smith, P. M., Fox, J. L., & Winge, D. R. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.11.009 · Cited by 119

Iron-sulfur cluster proteins: electron transfer and beyond.

Brzóska, K., Meczyńska, S., & Kruszewski, M. (2006) · Acta Biochimica Polonica · doi:10.18388/abp.2006_3296 · Cited by 117

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

Oxidant-Responsive Induction of the suf Operon, Encoding a Fe-S Assembly System, through Fur and IscR in Escherichia coli

Lee, K.-C., Yeo, W., & Roe, J. (2008) · Journal of Bacteriology · doi:10.1128/jb.01161-08 · Cited by 108

Identification of Global Ferredoxin Interaction Networks in Chlamydomonas reinhardtii

Peden, E. A., Boehm, M., Mulder, D. W., Davis, R., Old, W. M., King, P. W., Ghirardi, M. L., & Dubini, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483727 · Cited by 107

Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions

Marsh, E. N. G., Patterson, D. P., & Li, L. (2010) · ChemBioChem · doi:10.1002/cbic.200900777 · Cited by 104

A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation

Netz, D. J. A., Pierik, A. J., Stümpfig, M., Bill, E., Sharma, A. K., Pallesen, L. J., Walden, W. E., & Lill, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328914 · Cited by 106

In vitro synthesis of the iron–molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins

Curatti, L., Hernández, J. A., Igarashi, R. Y., Soboh, B., Zhao, D., & Rubio, L. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703050104 · Cited by 104

Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease

Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103

Mitochondrial iron metabolism and its role in diseases

Gao, J., Zhou, Q., Wu, D., & Chen, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.12.005 · Cited by 111

Metal Ion availability in mitochondria

Pierrel, F., Cobine, P. A., & Winge, D. R. (2007) · BioMetals · doi:10.1007/s10534-006-9052-9 · Cited by 105

Iron–Sulfur Clusters: Biogenesis, Molecular Mechanisms, and Their Functional Significance

Xu, X. M., & Møller, S. G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3259 · Cited by 102

Expression Pattern of Human Glutaredoxin 2 Isoforms: Identification and Characterization of Two Testis/Cancer Cell-Specific Isoforms

Lönn, M. E., Hudemann, C., Berndt, C., Cherkasov, V., Capani, F., Holmgren, A., & Lillig, C. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1821 · Cited by 99

Reactive oxygen species production induced by ethanol inSaccharomyces cerevisiaeincreases because of a dysfunctional mitochondrial iron-sulfur cluster assembly system

Pérez‐Gallardo, R. V., Sánchez‐Briones, L. A., Díaz-Pérez, A. L., Gutiérrez, S., Rodríguez‐Zavala, J. S., & Campos‐García, J. (2013) · FEMS Yeast Research · doi:10.1111/1567-1364.12090 · Cited by 97

Iron–sulfur cluster biosynthesis and trafficking – impact on human disease conditions

Wachnowsky, C., Fidai, I., & Cowan, J. A. (2017) · Metallomics · doi:10.1039/c7mt00180k · Cited by 99

Analysis of iron–sulfur protein maturation in eukaryotes

Pierik, A. J., Netz, D. J. A., & Lill, R. (2009) · Nature Protocols · doi:10.1038/nprot.2009.39 · Cited by 94

The apicomplexan plastid and its evolution

Sato, S. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0646-1 · Cited by 94

Metabolic engineering of Saccharomyces cerevisiae for production of butanol isomers

Generoso, W. C., Schadeweg, V., Oreb, M., & Boles, E. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.09.004 · Cited by 94

Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis

Uhrigshardt, H., Singh, A., Kovtunovych, G., Ghosh, M. C., & Rouault, T. A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq301 · Cited by 93

A general map of iron metabolism and tissue-specific subnetworks

Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97

X-ray Structure of the Complete ABC Enzyme ABCE1 from Pyrococcus abyssi

Kärcher, A., Schele, A., & Hopfner, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707347200 · Cited by 91

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