Iron–sulfur cluster biogenesis and trafficking in mitochondria

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,760

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 2×

Protein structure homology modeling using SWISS-MODEL workspace

Bordoli, L., Kiefer, F., Arnold, K., Benkert, P., Battey, J. N. D., & Schwede, T. F. (2008) · Nature Protocols · doi:10.1038/nprot.2008.197 · Cited by 1,233

Chaperone machines for protein folding, unfolding and disaggregation

Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,211

Function and biogenesis of iron-sulphur proteins

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

Iron-sulfur proteins: ancient structures, still full of surprises

Beinert, H. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050002 · Cited by 667

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

Structure of mammalian respiratory complex I

Zhu, J., Vinothkumar, K. R., & Hirst, J. (2016) · Nature · doi:10.1038/nature19095 · Cited by 587

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 513

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

The Origin and Diversification of Mitochondria

Roger, A. J., Muñoz-Gómez, S. A., & Kamikawa, R. (2017) · Current Biology · doi:10.1016/j.cub.2017.09.015 · Cited by 1,142

Iron metabolism and iron disorders revisited in the hepcidin era

Camaschella, C., Nai, A., & Silvestri, L. (2020) · Haematologica · doi:10.3324/haematol.2019.232124 · Cited by 734

Multifaceted mitochondria: moving mitochondrial science beyond function and dysfunction

Monzel, A. S., Enrı́quez, J. A., & Picard, M. A. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00783-1 · Cited by 632

Iron homeostasis and iron-regulated ROS in cell death, senescence and human diseases

Nakamura, T., Naguro, I., & Ichijo, H. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.06.010 · Cited by 529

Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology

Read, A. D., Bentley, R. E. T., Archer, S. L., & Dunham‐Snary, K. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102164 · Cited by 440

The Role of Iron Regulation in Immunometabolism and Immune-Related Disease

Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299

Assembly of mammalian oxidative phosphorylation complexes I–V and supercomplexes

Signes, A., & Fernandez-Vizarra, E. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170098 · Cited by 267

The multifaceted role of iron in renal health and disease

van Swelm, R. P. L., Wetzels, J. F. M., & Swinkels, D. W. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0197-5 · Cited by 282

The Functional Impact of Mitochondrial Structure Across Subcellular Scales

Glancy, B. C., Kim, Y., Katti, P., & Willingham, T. B. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.541040 · Cited by 270

Getting out what you put in: Copper in mitochondria and its impacts on human disease

Cobine, P. A., Moore, S. A., & Leary, S. C. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118867 · Cited by 259

Mechanistic concepts of iron-sulfur protein biogenesis in Biology

Braymer, J. J., Freibert, S., Rakwalska‐Bange, M., & Lill, R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118863 · Cited by 240

Cysteine Toxicity Drives Age-Related Mitochondrial Decline by Altering Iron Homeostasis

Hughes, C. E., Coody, T. K., Jeong, M.-Y., Berg, J. A., Winge, D. R., & Hughes, A. L. (2020) · Cell · doi:10.1016/j.cell.2019.12.035 · Cited by 222

Mitochondrial Iron in Human Health and Disease

Ward, D. M., & Cloonan, S. M. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114742 · Cited by 208

Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways

Tang, J. X., Thompson, K., Taylor, R. W., & Oláhová, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113820 · Cited by 205

Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin

Gervason, S., Larkem, D., Mansour, A. B., Botzanowski, T., Müller, C. S., Pecqueur, L., Pavec, G. L., Delaunay, A., Brun, O., Agramunt, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11470-9 · Cited by 187

The assembly of succinate dehydrogenase: a key enzyme in bioenergetics

Moosavi, B., Berry, E. A., Zhu, X., Yang, W., & Yang, G. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03200-7 · Cited by 184

Reactive sulfur species (RSS): persulfides, polysulfides, potential, and problems

Lau, N., & Pluth, M. D. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.08.012 · Cited by 172

Fluorescent proteins and genetically encoded biosensors

Wang, M., Da, Y., & Tian, Y. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00419d · Cited by 156

Yeast mitochondria: an overview of mitochondrial biology and the potential of mitochondrial systems biology

Malina, C., Larsson, C., & Nielsen, J. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy040 · Cited by 166

Nano-decocted ferrous polysulfide coordinates ferroptosis-like death in bacteria for anti-infection therapy

Shen, X., Ma, R., Huang, Y., Chen, L., Xu, Z., Li, D., Meng, X., Fan, K., Xi, J., Yan, X., et al. (2020) · Nano Today · doi:10.1016/j.nantod.2020.100981 · Cited by 156

Outlining the Complex Pathway of Mammalian Fe-S Cluster Biogenesis

Maio, N., & Rouault, T. A. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.02.001 · Cited by 147

Cysteine reactivity across the subcellular universe

Bak, D. W., Bechtel, T. J., Falco, J. A., & Weerapana, E. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.11.002 · Cited by 153

A PCBP1–BolA2 chaperone complex delivers iron for cytosolic [2Fe–2S] cluster assembly

Patel, S. J., Frey, A. G., Palenchar, D. J., Achar, S. R., Zumbrennen‐Bullough, K. B., Vashisht, A. A., Wohlschlegel, J. A., & Philpott, C. C. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0330-6 · Cited by 147

Ironing out mechanisms of iron homeostasis and disorders of iron deficiency

Koleini, N., Shapiro, J. S., Geier, J., & Ardehali, H. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148671 · Cited by 161

The molecular genetics of sideroblastic anemia

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

Mitochondria and Lysosomes: Discovering Bonds

Todkar, K. J., Ilamathi, H. S., & Germain, M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00106 · Cited by 140

The significance, trafficking and determination of labile iron in cytosol, mitochondria and lysosomes

Lv, H., & Shang, P. (2018) · Metallomics · doi:10.1039/c8mt00048d · Cited by 127

Suppression of PFKFB3-driven glycolysis restrains endothelial-to-mesenchymal transition and fibrotic response

Zeng, H., Pan, T. S., Zhan, M., Hailiwu, R., Liu, B., Yang, H. Q., & Li, P. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01097-6 · Cited by 122

The Multifaceted Regulation of Mitochondria in Ferroptosis

Wu, H., Wang, F., Ta, N., Zhang, T., & Gao, W. (2021) · Life · doi:10.3390/life11030222 · Cited by 111

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

Modulation of thiol-dependent redox system by metal ionsviathioredoxin and glutaredoxin systems

Ouyang, Y., Peng, Y., Li, J., Holmgren, A., & Lu, J. (2018) · Metallomics · doi:10.1039/c7mt00327g · Cited by 110

Roles and maturation of iron–sulfur proteins in plastids

Przybyla‐Toscano, J., Roland, M., Gaymard, F., Couturier, J., & Rouhier, N. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1532-1 · Cited by 106

Iron Metabolism in Aging and Age-Related Diseases

Tian, Y., Tian, Y., Yuan, Z., Zeng, Y., Wang, S., Fan, X., Yang, D., & Yang, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073612 · Cited by 110

Alterations in Cellular Iron Metabolism Provide More Therapeutic Opportunities for Cancer

Zhou, L., Zhao, B., Zhang, L., Wang, S., Dong, D., Lv, H., & Shang, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051545 · Cited by 102

Mutations in PMPCB Encoding the Catalytic Subunit of the Mitochondrial Presequence Protease Cause Neurodegeneration in Early Childhood

Vögtle, F. ‐., Brändl, B., Larson, A. A., Pendziwiat, M., Friederich, M. W., White, S. M., Basinger, A., Küçükköse, C., Muhle, H., Jähn, J. A., et al. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.02.014 · Cited by 98

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

Biochemical Reconstitution and Spectroscopic Analysis of Iron–Sulfur Proteins

Freibert, S., Weiler, B. D., Bill, E., Pierik, A. J., Mühlenhoff, U., & Lill, R. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.034 · Cited by 94

Down the Iron Path: Mitochondrial Iron Homeostasis and Beyond

Dietz, J. V., Fox, J. L., & Khalimonchuk, O. (2021) · Cells · doi:10.3390/cells10092198 · Cited by 98

Mitofusins: Disease Gatekeepers and Hubs in Mitochondrial Quality Control by E3 Ligases

Escobar‐Henriques, M., & Joaquim, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00517 · Cited by 85

Irp2 regulates insulin production through iron-mediated Cdkal1-catalyzed tRNA modification

Ferreira, M. C., Anderson, C. P., Neschen, S., Zumbrennen‐Bullough, K. B., Romney, S. J., Kahle, M., Rathkolb, B., Gailus‐Durner, V., Fuchs, H., Wolf, E., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14004-5 · Cited by 85

Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication

Barton, J. K., Silva, R. M. B., & O’Brien, E. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110644 · Cited by 77

Hydrosulfide complexes of the transition elements: diverse roles in bioinorganic, cluster, coordination, and organometallic chemistry

Pluth, M. D., & Tonzetich, Z. J. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00570f · Cited by 82

Mammalian iron–sulfur cluster biogenesis: Recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins

Maio, N., Jain, A., & Rouault, T. A. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.11.014 · Cited by 77

Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase

Liu, G., Sil, D., Maio, N., Tong, W.-H., Bollinger, J. M., Jr., Krebs, C., & Rouault, T. A. (2020) · Nature Communications · doi:10.1038/s41467-020-20145-9 · Cited by 76

Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli

Fontenot, C. R., Tasnim, H., Valdes, K. A., Popescu, C. V., & Ding, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014814 · Cited by 74

High Levels of Frataxin Overexpression Lead to Mitochondrial and Cardiac Toxicity in Mouse Models

Belbellaa, B., Reutenauer, L., Messaddeq, N., Monassier, L., & Puccio, H. M. (2020) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2020.08.018 · Cited by 78

Mitochondria-cytosol-nucleus crosstalk: learning from Saccharomyces cerevisiae

Guaragnella, N., Coyne, L. P., Chen, X. J., & Giannattasio, S. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy088 · Cited by 72

Understanding Long COVID; Mitochondrial Health and Adaptation—Old Pathways, New Problems

Nunn, A. V. W., Guy, G. W., Brysch, W., & Bell, J. D. (2022) · Biomedicines · doi:10.3390/biomedicines10123113 · Cited by 74

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

Exploring and exploiting the connection between mitochondria and the virulence of human pathogenic fungi

Verma, S., Shakya, V. P. S., & Idnurm, A. (2018) · Virulence · doi:10.1080/21505594.2017.1414133 · Cited by 67

Mitochondrial Iron Metabolism: The Crucial Actors in Diseases

Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 74

Targeting Mitochondrial Oxidative Stress as a Strategy to Treat Aging and Age-Related Diseases

Lee, Y. H., Kuk, M. U., So, M. K., Song, E. S., Lee, H., Ahn, S. K., Kwon, H. W., Park, J. T., & Park, S. C. (2023) · Antioxidants · doi:10.3390/antiox12040934 · Cited by 72

Iron and liver cancer: an inseparable connection

Hino, K., Yanatori, I., Hara, Y., & Nishina, S. (2021) · FEBS Journal · doi:10.1111/febs.16208 · Cited by 68

Effects of Oxidative Stress on Protein Translation: Implications for Cardiovascular Diseases

Ghosh, A., & Shcherbik, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082661 · Cited by 70

Interactions of reactive sulfur species with metalloproteins

Domán, A., Dóka, É., Garai, D., Bogdándi, V., Balla, G., Balla, J., & Nagy, P. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102617 · Cited by 68

Mitochondrial acyl carrier protein (ACP) at the interface of metabolic state sensing and mitochondrial function

Masud, A. J., Kastaniotis, A. J., Rahman, M., Autio, K. J., & Hiltunen, J. K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118540 · Cited by 67

Mito-Nuclear Communication by Mitochondrial Metabolites and Its Regulation by B-Vitamins

Janssen, J. J. E., Grefte, S., Keijer, J., & de Boer, V. C. J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00078 · Cited by 70

Metabolic features and regulation of the healing cycle—A new model for chronic disease pathogenesis and treatment

Naviaux, R. K. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.08.001 · Cited by 72

Unraveling the Role of Heme in Neurodegeneration

Chiabrando, D., Fiorito, V., Petrillo, S., & Tolosano, E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00712 · Cited by 68

Molecular Mechanism of ISC Iron–Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry

Lin, C.-W., McCabe, J. W., Russell, D. H., & Barondeau, D. P. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11454 · Cited by 65

Engineered mitochondria in diseases: mechanisms, strategies, and applications

Li, M., Wu, L., Si, H., Wu, Y., Liu, Y., Zeng, Y., & Shen, B. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02081-y · Cited by 71

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

Expression of mitochondrial dysfunction-related genes and pathways in paclitaxel-induced peripheral neuropathy in breast cancer survivors

Kober, K. M., Olshen, A. B., Conley, Y. P., Schumacher, M. A., Topp, K. S., Smoot, B. J., Mazor, M. B., Chesney, M. A., Hammer, M. J., Paul, S. M., et al. (2018) · Molecular Pain · doi:10.1177/1744806918816462 · Cited by 66

Iron–sulfur clusters as inhibitors and catalysts of viral replication

Ebrahimi, K. H., Ciofi‐Baffoni, S., Hagedoorn, P., Nicolet, Y., Brun, N. E. L., Hagen, W. R., & Armstrong, F. A. (2022) · Nature Chemistry · doi:10.1038/s41557-021-00882-0 · Cited by 63

Metabolic sensing and control in mitochondria

Liu, Y., & Birsoy, K. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.016 · Cited by 65

Linking Cancer Metabolic Dysfunction and Genetic Instability through the Lens of Iron Metabolism

Petronek, M. S., Spitz, D. R., Buettner, G. R., & Allen, B. G. (2019) · Cancers · doi:10.3390/cancers11081077 · Cited by 66

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

Tsaousis, A. D. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02478 · Cited by 62

SIRT3 Regulates Clearance of Apoptotic Cardiomyocytes by Deacetylating Frataxin

Gao, J., Huang, C., Kong, L., Zhou, W., Sun, M., Wei, T., & Shen, W. (2023) · Circulation Research · doi:10.1161/circresaha.123.323160 · Cited by 60

The critical roles of iron during the journey from fetus to adolescent: Developmental aspects of iron homeostasis

Donker, A. E., van der Staaij, H., & Swinkels, D. W. (2021) · Blood Reviews · doi:10.1016/j.blre.2021.100866 · Cited by 76

Establishment of strigolactone-producing bacterium-yeast consortium

Wu, S., Ma, X., Zhou, A., Valenzuela, A., Zhou, K., & Li, Y. (2021) · Science Advances · doi:10.1126/sciadv.abh4048 · Cited by 59

Additional oxidative stress reroutes the global response of Aspergillus fumigatus to iron depletion

Kurucz, V., Krüger, T., Antal, K., Dietl, A., Haas, H., Pócsi, I., Kniemeyer, O., & Emri, T. (2018) · BMC Genomics · doi:10.1186/s12864-018-4730-x · Cited by 61

IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex

Gourdoupis, S., Nasta, V., Calderone, V., Ciofi‐Baffoni, S., & Banci, L. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09061 · Cited by 60

Therapeutic potential of iron chelators on osteoporosis and their cellular mechanisms

Zhang, J., Zhao, H., Yao, G., Qiao, P., Li, L., & Wu, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111380 · Cited by 56

The mouse metallomic landscape of aging and metabolism

Morel, J., Sauzéat, L., Goeminne, L. J. E., Jha, P., Williams, E. G., Houtkooper, R. H., Aebersold, R. H., Auwerx, J. H., & Balter, V. (2022) · Nature Communications · doi:10.1038/s41467-022-28060-x · Cited by 57

The basic machineries for mitochondrial protein quality control

Vazquez‐Calvo, C., Suhm, T., Büttner, S., & Ott, M. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.10.003 · Cited by 56

The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway

Py, B., Gerez, C., Huguenot, A., Vidaud, C., Fontecave, M., de Choudens, S. O., & Barras, F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002160 · Cited by 53

Thioredoxin Network in Plant Mitochondria: Cysteine S-Posttranslational Modifications and Stress Conditions

Martí, M. C., Jiménez, A., & Sevilla, F. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.571288 · Cited by 55

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

EPR spectroscopy of complex biological iron–sulfur systems

Hagen, W. R. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1543-y · Cited by 51

Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system

Baussier, C., Fakroun, S., Aubert, C., Dubrac, S., Mandin, P., Py, B., & Barras, F. (2020) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2020.01.001 · Cited by 51

A novel complex neurological phenotype due to a homozygous mutation in FDX2

Gurgel‐Giannetti, J., Lynch, D. S., de Paiva, A. R. B., Lucato, L. T., Yamamoto, G. L., Thomsen, C., Basu, S., Freua, F., Giannetti, A. V., Della‐Ripa, B., et al. (2018) · Brain · doi:10.1093/brain/awy172 · Cited by 50

Iron-sensing is governed by mitochondrial, not by cytosolic iron–sulfur cluster biogenesis inAspergillus fumigatus

Misslinger, M., Lechner, B. E., Bacher, K., & Haas, H. (2018) · Metallomics · doi:10.1039/c8mt00263k · 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

A VDAC1-mediated NEET protein chain transfers [2Fe-2S] clusters between the mitochondria and the cytosol and impacts mitochondrial dynamics

Karmi, O., Marjault, H., Bai, F., Roy, S., Sohn, Y., Darash‐Yahana, M., Morcos, F., Ioannidis, K., Nahmias, Y., Jennings, P. A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121491119 · Cited by 51

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

Lipotoxic Impairment of Mitochondrial Function in β-Cells: A Review

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

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

Regulation of the redox metabolome and thiol proteome by hydrogen sulfide

Kumar, R., & Banerjee, R. V. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1893641 · Cited by 48

Iron–Sulfur Cluster Biogenesis as a Critical Target in Cancer

Petronek, M. S., Spitz, D. R., & Allen, B. G. (2021) · Antioxidants · doi:10.3390/antiox10091458 · Cited by 46

Evidence that a respiratory shield in Escherichia coli protects a low-molecular-mass FeII pool from O2-dependent oxidation

Wofford, J. D., Bolaji, N., Dziuba, N., Outten, F. W., & Lindahl, P. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005233 · Cited by 48

SINEUP non-coding RNAs rescue defective frataxin expression and activity in a cellular model of Friedreich's Ataxia

Bon, C., Luffarelli, R., Russo, R., Fortuni, S., Pierattini, B., Santulli, C., Fimiani, C., Persichetti, F., Cotella, D., Mallamaci, A., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz798 · Cited by 48

Iron Metabolism: An Under Investigated Driver of Renal Pathology in Lupus Nephritis

Wlazlo, E., Mehrad, B., Morel, L. M., & Scindia, Y. M. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.643686 · Cited by 44

Pulling back the mitochondria’s iron curtain

David, S. B. Z., Shkuri, L., & Ast, T. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-024-00045-y · Cited by 59

20,000 picometers under the OMM: diving into the vastness of mitochondrial metabolite transport

Cunningham, C. N., & Rutter, J. P. (2020) · EMBO Reports · doi:10.15252/embr.202050071 · Cited by 44

Sideroflexin 4 affects Fe-S cluster biogenesis, iron metabolism, mitochondrial respiration and heme biosynthetic enzymes

Paul, B. T., Tesfay, L., Winkler, C. R., Torti, F. M., & Torti, S. V. (2019) · Scientific Reports · doi:10.1038/s41598-019-55907-z · Cited by 45

Characterization of the novel mitochondrial genome segregation factor TAP110 in Trypanosoma brucei

Amodeo, S., Kalichava, A., Fradera-Sola, A., Bertiaux, E., Guichard, P., Butter, F., & Ochsenreiter, T. (2021) · Journal of Cell Science · doi:10.1242/jcs.254300 · Cited by 45

Regulation of cellular iron metabolism: Iron-dependent degradation of IRP by SCFFBXL5 ubiquitin ligase

Iwaï, K. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.011 · Cited by 46

A pathway for assembling [4Fe‐4S]2+ clusters in mitochondrial iron–sulfur protein biogenesis

Nasta, V., Suraci, D., Gourdoupis, S., Ciofi‐Baffoni, S., & Banci, L. (2019) · FEBS Journal · doi:10.1111/febs.15140 · Cited by 43

Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins

Stehling, O., Jeoung, J., Freibert, S., Paul, V. D., Bänfer, S., Niggemeyer, B., Rösser, R., Dobbek, H., & Lill, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1807762115 · Cited by 44

Taming the Dichalcogenides: Isolation, Characterization, and Reactivity of Elusive Perselenide, Persulfide, Thioselenide, and Selenosulfide Anions

Li, K., Zakharov, L. N., & Pluth, M. D. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c03766 · Cited by 43

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

The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins

Lill, R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C., & Kispál, G. (1999) · Biological Chemistry · doi:10.1515/bc.1999.147 · Cited by 156

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

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

Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis

Lill, R., & Freibert, S.-A. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111540 · Cited by 453