The Effects of Mitochondrial Iron Homeostasis on Cofactor Specificity of Superoxide Dismutase 2

Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase

Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789 · see citing works

Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase

Rae, T., Schmidt, P. J., Pufahl, R. A., Culotta, V., & O’Halloran, T. V. (1999) · Science · doi:10.1126/science.284.5415.805 · Cited by 1,628 · see citing works

Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis

Outten, C. E., & O'Halloran, A. T. V. (2001) · Science · doi:10.1126/science.1060331 · Cited by 1,489 · see citing works

Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria.

Daum, G., Böhni, P. C., & Schatz, G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33617-2 · Cited by 1,152 · see citing works

Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors

Finney, L. A., & O'Halloran, T. V. (2003) · Science · doi:10.1126/science.1085049 · Cited by 1,100 · see citing works

Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice

Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023 · see citing works

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 · see citing works

Metallochaperones, an Intracellular Shuttle Service for Metal Ions

O'Halloran, T. V., & Culotta, V. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000006200 · Cited by 806 · 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

Metal ion chaperone function of the soluble Cu(I) receptor Atx1.

Pufahl, R. A., Singer, C. P., Peariso, K. L., Lin, S.-J., Schmidt, P. J., Fahrni, C. J., Culotta, V. C., Penner-Hahn, J. E., & O'Halloran, T. V. (1997) · Science · doi:10.1126/science.278.5339.853 · Cited by 691 · see citing works

IMPORT OF PROTEINS INTO MITOCHONDRIA

Glick, B. S., & Schatz, G. (1991) · Annual Review of Genetics · doi:10.1146/annurev.ge.25.120191.000321 · Cited by 579 · see citing works

The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles

Borgstahl, G. E. O., Parge, H. E., Hickey, M. J., Beyer, W. F., Hallewell, R. A., & Tainer, J. A. (1992) · Cell · doi:10.1016/0092-8674(92)90270-m · Cited by 472 · 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

Iron–sulphur cluster biogenesis and mitochondrial iron homeostasis

Rouault, T. A., & Tong, W.-H. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1620 · Cited by 432 · 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

Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria

Foury, F., & Cazzalini, O. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00734-5 · Cited by 378 · 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

AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae.

Yamaguchi‐Iwai, Y., Dancis, A., & Klausner, R. D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07106.x · Cited by 358 · see citing works

Iron‐regulated DNA binding by the AFT1 protein controls the iron regulon in yeast.

Yamaguchi‐Iwai, Y., Stearman, R. S., Dancis, A., & Klausner, R. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00703.x · Cited by 337 · see citing works

Iron–sulfur-protein biogenesis in eukaryotes

Lill, R., & Mühlenhoff, U. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.01.006 · Cited by 333 · see citing works

The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins

Mühlenhoff, U. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.17.2025 · Cited by 326 · see citing works

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

Gray, H. B. (2000) · Cited by 307 · 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

The ABC transporter Atm1p is required for mitochondrial iron homeostasis

Kispál, G., Csere, P., Guiard, B., & Lill, R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01414-2 · Cited by 276 · see citing works

A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins

Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272 · see citing works

Activation of the Iron Regulon by the Yeast Aft1/Aft2 Transcription Factors Depends on Mitochondrial but Not Cytosolic Iron-Sulfur Protein Biogenesis

Rutherford, J. C., Ojeda, L. D., Balk, J., Mühlenhoff, U., Lill, R., & Winge, D. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413731200 · Cited by 242 · see citing works

Friedreich ataxia: the oxidative stress paradox

Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · Cited by 219 · see citing works

Transcription of the Yeast Iron Regulon Does Not Respond Directly to Iron but Rather to Iron-Sulfur Cluster Biosynthesis

Chen, O. S., Crisp, R. J., Valachovic, M., Bard, M., Winge, D. R., & Kaplan, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403209200 · Cited by 202 · see citing works

Yeast Mitochondrial Protein, Nfs1p, Coordinately Regulates Iron-Sulfur Cluster Proteins, Cellular Iron Uptake, and Iron Distribution

Li, J., Kogan, M., Knight, S. A. B., Pain, D., & Dancis, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33025 · Cited by 201 · see citing works

A Specific Role of the Yeast Mitochondrial Carriers Mrs3/4p in Mitochondrial Iron Acquisition under Iron-limiting Conditions

Mühlenhoff, U., Stadler, J. A., Richhardt, N., Seubert, A., Eickhorst, T., Schweyen, R. J., Lill, R., & Wiesenberger, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307847200 · Cited by 193 · see citing works

Aft1p and Aft2p Mediate Iron-responsive Gene Expression in Yeast through Related Promoter Elements

Rutherford, J. C., Jaron, S., & Winge, D. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300076200 · Cited by 192 · see citing works

Desferrioxamine-mediated Iron Uptake in Saccharomyces cerevisiae

Yun, C., Ferea, T., Rashford, J., Ardon, O., Brown, P. O., Botstein, D., Kaplan, J., & Philpott, C. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10709 · Cited by 183 · see citing works

SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness

Friedman, J. S., Lopez, M. F., Fleming, M. D., Rivera, A., Martin, F. M., Welsh, M. L., Boyd, A. S., Doctrow, S. R., & Burakoff, S. J. (2004) · Blood · doi:10.1182/blood-2003-11-3858 · Cited by 183 · see citing works

Isolation and characterization of a manganese-containing superoxide dismutase from yeast.

Ravindranath, S. D., & Fridovich, I. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41165-4 · Cited by 182 · see citing works

Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae

Strain, J., Lorenz, C. R., Bode, J., Garland, S., Smolen, G. A., Ta, D. T., Vickery, L. E., & Culotta, V. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31138 · Cited by 181 · see citing works

A Simple Proposal That Can Explain the Inactivity of Metal-Substituted Superoxide Dismutases

Vance, C. K., & Miller, A. (1998) · Journal of the American Chemical Society · doi:10.1021/ja972060j · Cited by 179 · see citing works

Mitochondrial Control of Iron Homeostasis

Foury, F., & Talibi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005804200 · Cited by 176 · see citing works

Mt-Hsp70 Homolog, Ssc2p, Required for Maturation of Yeast Frataxin and Mitochondrial Iron Homeostasis

Knight, S. A. B., Sepuri, N. B. V., Pain, D., & Dancis, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18389 · Cited by 173 · see citing works

Deletion of the Mitochondrial Carrier Genes MRS3 andMRS4 Suppresses Mitochondrial Iron Accumulation in a Yeast Frataxin-deficient Strain

Foury, F., & Roganti, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111789200 · Cited by 171 · see citing works

A Sod2 Null Mutation Confers Severely Reduced Adult Life Span in Drosophila

Duttaroy, A., Paul, A., Kundu, M., & Belton, A. (2003) · Genetics · doi:10.1093/genetics/165.4.2295 · Cited by 153 · see citing works

Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis

Chen, O. S., Hemenway, S., & Kaplan, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192449599 · Cited by 152 · see citing works

Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1 , a member of the mitochondrial carrier family

Luk, E., Carroll, M., Baker, M., & Culotta, V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632471100 · Cited by 146 · see citing works

RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila

Anderson, P. R., Kirby, K., Hilliker, A. J., & Phillips, J. P. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi367 · Cited by 144 · see citing works

Manganese Superoxide Dismutase in Saccharomyces cerevisiae Acquires Its Metal Co-factor through a Pathway Involving the Nramp Metal Transporter, Smf2p

Luk, E., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108923200 · Cited by 137 · see citing works

Manganese Activation of Superoxide Dismutase 2 in the Mitochondria of Saccharomyces cerevisiae

Luk, E., Yang, M., Jensen, L. T., Bourbonnais, Y., & Culotta, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504257200 · Cited by 125 · see citing works

Isa1p Is a Component of the Mitochondrial Machinery for Maturation of Cellular Iron-Sulfur Proteins and Requires Conserved Cysteine Residues for Function

Kaut, A., Lange, H., Diekert, K., Kispál, G., & Lill, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909502199 · Cited by 122 · see citing works

In vivo competition between iron and manganese for occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli.

Beyer, W. F., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52435-2 · Cited by 116 · see citing works

Frataxin and Mitochondrial Carrier Proteins, Mrs3p and Mrs4p, Cooperate in Providing Iron for Heme Synthesis

Zhang, Y., Lyver, E. R., Knight, S. A. B., Lesuisse, E., & Dancis, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500397200 · Cited by 111 · see citing works

Iron on the brain

Rouault, T. A. (2001) · Nature Genetics · doi:10.1038/91036 · Cited by 110 · see citing works

A Mitochondrial-Vacuolar Signaling Pathway in Yeast That Affects Iron and Copper Metabolism

Li, L., & Kaplan, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403146200 · Cited by 109 · see citing works

MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast, are new members of the mitochondrial carrier family

Wiesenberger, G., Link, T. A., von Ahsen, U., Waldherr, M., & Schweyen, R. J. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90608-9 · Cited by 99 · see citing works

Specificity and Phenetic Relationships of Iron- and Manganese-containing Superoxide Dismutases on the Basis of Structure and Sequence Comparisons

Wintjens, R. T., Noël, C. J., May, A. C. W., Gerbod, D., Dufernez, F., Capron, M., Viscogliosi, É., & Rooman, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312329200 · Cited by 88 · see citing works

Characterization of Two Homologous Yeast Genes That Encode Mitochondrial Iron Transporters

Li, L., & Kaplan, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28485 · Cited by 85 · see citing works

Regulation of Saccharomyces cerevisiae FET4 by Oxygen and Iron

Jensen, L. T., & Culotta, V. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00093-1 · Cited by 67 · see citing works

Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli.

Privalle, C. T., & Fridovich, I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50400-8 · Cited by 66 · see citing works

The irony of manganese superoxide dismutase

Whittaker, J. W. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311318 · Cited by 65 · see citing works

In Vivo and in Vitro Kinetics of Metal Transfer by the Klebsiella aerogenes Urease Nickel Metallochaperone, UreE

Colpas, G. J., & Hausinger, R. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10731 · Cited by 64 · see citing works

Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets of Genes

Bellı́, G., Molina‐Navarro, M. M., García‐Martínez, J., Pérez-Ortín, J. E., & Herrero, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311879200 · Cited by 61 · see citing works

Calorimetric Studies on the Tight Binding Metal Interactions of Escherichia coli Manganese Superoxide Dismutase

Mizuno, K., Whittaker, M. M., Bächinger, H. P., & Whittaker, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400813200 · Cited by 58 · see citing works

Isolation and characterization of a Saccharomyces cerevisiae mutant disrupted for the succinate dehydrogenase flavoprotein subunit.

Robinson, K. M., von Kieckebusch-Gück, A., & Lemire, B. D. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54641-x · Cited by 55 · see citing works

[3] Flavinylation of succinate: Ubiquinone oxidoreductase from Saccharomyces cerevisiae

Robinson, K. M., & Lemire, B. D. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)60128-7 · Cited by 45 · see citing works

Genome-Wide Screen for Genes With Effects on Distinct Iron Uptake Activities in Saccharomyces cerevisiae

Lesuisse, E., Knight, S. A. B., Courel, M., Santos, R., Camadro, J., & Dancis, A. (2004) · Genetics · doi:10.1534/genetics.104.035873 · Cited by 45 · see citing works

How to make a metalloprotein.

Bartnikas, T. B., & Gitlin, J. D. (2001) · Nature Structural Biology · doi:10.1038/nsb0901-733 · Cited by 35 · see citing works

Mutations in Saccharomyces cerevisiae Iron-Sulfur Cluster Assembly Genes and Oxidative Stress Relevant to Cu,Zn Superoxide Dismutase*

Jensen, L. T., Sanchez, R. J., Srinivasan, C., Valentine, J., & Culotta, V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402795200 · Cited by 35 · see citing works

Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl)

Hänsch, R., & Mendel, R. R. (2009) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2009.05.006 · Cited by 1,702 · see citing works

Superoxide dismutases and superoxide reductases

Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081 · see citing works

Metals, oxidative stress and neurodegeneration: A focus on iron, manganese and mercury

Farina, M., Ávila, D. S., da Rocha, J. B. T., & Aschner, M. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.006 · Cited by 558 · see citing works

Activation of superoxide dismutases: Putting the metal to the pedal

Culotta, V., Yang, M., & O’Halloran, T. V. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.003 · Cited by 509 · see citing works

Battles with Iron: Manganese in Oxidative Stress Protection

Aguirre, J. D., & Culotta, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.312181 · Cited by 304 · see citing works

Copper and iron homeostasis in Arabidopsis : responses to metal deficiencies, interactions and biotechnological applications

Puig, S., Andrés‐Colás, N., Garcia‐Molina, A., & Peñarrubia, L. (2007) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2007.01642.x · Cited by 288 · see citing works

MnSOD in Oxidative Stress Response-Potential Regulation via Mitochondrial Protein Influx

Candas, D., & Li, J. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5305 · Cited by 287 · see citing works

Iron Acquisition and Transcriptional Regulation

Kaplan, C. D., & Kaplan, J. (2009) · Chemical Reviews · doi:10.1021/cr9001676 · Cited by 275 · see citing works

Divalent Metal Ions in Plant Mitochondria and Their Role in Interactions with Proteins and Oxidative Stress-Induced Damage to Respiratory Function

Tan, Y., O’Toole, N., Taylor, N. L., & Millar, A. H. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.147942 · Cited by 229 · 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

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

Antioxidant Therapy in Cancer: Rationale and Progress

Luo, M., Zhou, L., Huang, Z., Li, B., Nice, E. C., Xu, J., & Huang, C. (2022) · Antioxidants · doi:10.3390/antiox11061128 · Cited by 201 · see citing works

Friedreich Ataxia: Molecular Mechanisms, Redox Considerations, and Therapeutic Opportunities

Santos, R., Lefevre, S. D., Sliwa, D., Seguin, A., Camadro, J., & Lesuisse, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3015 · Cited by 191 · 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

Post-translational modifications of superoxide dismutase

Yamakura, F., & Kawasaki, H. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.10.010 · Cited by 178 · see citing works

Calcium Increases Xylella fastidiosa Surface Attachment, Biofilm Formation, and Twitching Motility

Cruz, L. F., Cobine, P. A., & Fuente, L. D. L. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.06501-11 · Cited by 167 · see citing works

Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia

Campanella, A., Rovelli, E., Santambrogio, P., Cozzi, A., Taroni, F., & Levi, S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn308 · Cited by 162 · 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

Mitochondrial Matrix Copper Complex Used in Metallation of Cytochrome Oxidase and Superoxide Dismutase

Cobine, P. A., Pierrel, F., Bestwick, M. L., & Winge, D. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606839200 · 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

Redox dynamics of manganese as a mitochondrial life-death switch

Smith, M. R., Fernandes, J., Go, Y., & Jones, D. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.126 · Cited by 150 · see citing works

Metal Acquisition and Availability in the Mitochondria

Atkinson, A., & Winge, D. R. (2009) · Chemical Reviews · doi:10.1021/cr900006y · Cited by 146 · see citing works

The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence

Varesi, A., Chirumbolo, S., Campagnoli, L. I. M., Pierella, E., Piccini, G. B., Carrara, A., Ricevuti, G., Scassellati, C., Bonvicini, C., & Pascale, A. (2022) · Antioxidants · doi:10.3390/antiox11071224 · Cited by 145 · see citing works

Frataxin and Mitochondrial FeS Cluster Biogenesis

Stemmler, T. L., Lesuisse, E., Pain, D., & Dancis, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.118679 · Cited by 145 · see citing works

Lysosome-related Organelles as Mediators of Metal Homeostasis

Blaby, C., & Merchant, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.592618 · Cited by 134 · see citing works

Recent progress in structure–function analyses of Nramp proton-dependent metal-ion transportersThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.

Courville, P., Chaloupka, R., & Cellier, M. F. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-193 · Cited by 132 · see citing works

Redox Tuning over Almost 1 V in a Structurally Conserved Active Site: Lessons from Fe-Containing Superoxide Dismutase

Miller, A. (2008) · Accounts of Chemical Research · doi:10.1021/ar700237u · Cited by 128 · see citing works

The Iron Metallome in Eukaryotic Organisms

Dlouhy, A. C., & Outten, C. E. (2012) · Metal ions in life sciences · doi:10.1007/978-94-007-5561-1_8 · Cited by 121 · see citing works

Copper Import into the Mitochondrial Matrix in Saccharomyces cerevisiae Is Mediated by Pic2, a Mitochondrial Carrier Family Protein

Vest, K. E., Leary, S. C., Winge, D. R., & Cobine, P. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470674 · Cited by 112 · see citing works

The yeast mitochondrial carrier proteins Mrs3p/Mrs4p mediate iron transport across the inner mitochondrial membrane

Froschauer, E. M., Schweyen, R. J., & Wiesenberger, G. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.03.004 · Cited by 110 · see citing works

Factors Required for Activation of Urease as a Virulence Determinant in Cryptococcus neoformans

Singh, A., Panting, R. J., Varma, A., Saijo, T., Waldron, K. J., Jong, A., Ngamskulrungroj, P., Chang, Y. C., Rutherford, J. C., & Kwon-Chung, K. J. (2013) · mBio · doi:10.1128/mbio.00220-13 · Cited by 108 · see citing works

Myeloperoxidase and superoxide dismutase 2 polymorphisms comodulate the risk of hepatocellular carcinoma and death in alcoholic cirrhosis #

Nahon, P., Sutton, A., Rufat, P., Ziol, M., Akouche, H., Laguillier, C., Charnaux, N., Ganne‐Carrié, N., Grando–Lemaire, V., Nkontchou, G., et al. (2009) · Hepatology · doi:10.1002/hep.23187 · Cited by 106 · see citing works

Intracellular Distribution of Manganese by the Trans-Golgi Network Transporter NRAMP2 Is Critical for Photosynthesis and Cellular Redox Homeostasis

Alejandro, S., Cailliatte, R., Alcon, C., Dirick, L., Domergue, F., Correia, D., Castaings, L., Briat, J., Mari, S., & Curie, C. (2017) · The Plant Cell · doi:10.1105/tpc.17.00578 · Cited by 105 · see citing works

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 · see citing works

Manganese Supplementation Protects Against Diet-Induced Diabetes in Wild Type Mice by Enhancing Insulin Secretion

Lee, S.-H., Jouihan, H. A., Cooksey, R. C., Jones, D., Kim, H. J., Winge, D. R., & McClain, D. A. (2013) · Endocrinology · doi:10.1210/en.2012-1445 · Cited by 103 · see citing works

Iron-Mediated Inhibition of Mitochondrial Manganese Uptake Mediates Mitochondrial Dysfunction in a Mouse Model of Hemochromatosis

Jouihan, H. A., Cobine, P. A., Cooksey, R. C., Hoagland, E. A., Boudina, S., Abel, E. D., Winge, D. R., & McClain, D. A. (2008) · Molecular Medicine · doi:10.2119/2007-00114.jouihan · Cited by 103 · see citing works

Mrs3p, Mrs4p, and Frataxin Provide Iron for Fe-S Cluster Synthesis in Mitochondria

Zhang, Y., Lyver, E. R., Knight, S. A. B., Pain, D., Lesuisse, E., & Dancis, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604246200 · Cited by 98 · see citing works

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95 · see citing works

Evaluation of flash and slow pyrolysis applied on heavy metal contaminated Sorghum bicolor shoots resulting from phytoremediation

Chami, Z. A., Amer, N., Smets, K., Yperman, J., Carleer, R., Dumontet, S., & Vangronsveld, J. (2014) · Biomass and Bioenergy · doi:10.1016/j.biombioe.2014.02.027 · Cited by 95 · see citing works

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 89 · see citing works

Potential use of Sorghum bicolor and Carthamus tinctorius in phytoremediation of nickel, lead and zinc

Chami, Z. A., Amer, N., Bitar, L. A., & Cavoski, I. (2015) · International Journal of Environmental Science and Technology · doi:10.1007/s13762-015-0823-0 · Cited by 83 · see citing works

A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi

Aguirre, J. D., Clark, H. M., McIlvin, M., Vazquez, C., Palmere, S. L., Grab, D. J., Seshu, J., Hart, P. J., Saito, M., & Culotta, V. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433540 · Cited by 82 · see citing works

Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,

Dowling, D., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2010) · Biochemistry · doi:10.1021/bi1005046 · Cited by 81 · see citing works

Fe Sparing and Fe Recycling Contribute to Increased Superoxide Dismutase Capacity in Iron-Starved Chlamydomonas reinhardtii

Page, M. D., Allen, M. D., Kropat, J., Urzica, E. I., Karpowicz, S. J., Hsieh, S. I., Loo, J. A., & Merchant, S. (2012) · The Plant Cell · doi:10.1105/tpc.112.098962 · Cited by 81 · see citing works

Genetic and Biochemical Analysis of High Iron Toxicity in Yeast

Lin, H., Li, L., Jia, X., Ward, D. M., & Kaplan, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190959 · Cited by 75 · see citing works

Interchangeable utilization of metals: New perspectives on the impacts of metal ions employed in ancient and extant biomolecules

Smethurst, D. G. J., & Shcherbik, N. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101374 · Cited by 74 · see citing works

Evaluation ofAtriplex Halimus,Medicago LupulinaandPortulaca OleraceaFor Phytoremediation of Ni, Pb, and Zn

Amer, N., Chami, Z. A., Bitar, L. A., Mondelli, D., & Dumontet, S. (2012) · International Journal of Phytoremediation · doi:10.1080/15226514.2012.716102 · Cited by 70 · see citing works

The Interaction of Mitochondrial Iron with Manganese Superoxide Dismutase

Naranuntarat, A., Jensen, L. T., Pazicni, S., Penner-Hahn, J. E., & Culotta, V. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026773 · Cited by 66 · see citing works

Molecular Alterations in a Mouse Cardiac Model of Friedreich Ataxia

Anzovino, A., Chiang, S., Brown, B. E., Hawkins, C. L., Richardson, D. R., & Huang, M. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.08.021 · Cited by 64 · see citing works

Iron Dysregulation in Friedreich Ataxia

Wilson, R. B. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.005 · Cited by 59 · see citing works

Labile Low-Molecular-Mass Metal Complexes in Mitochondria: Trials and Tribulations of a Burgeoning Field

Lindahl, P. A., & Moore, M. J. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00216 · Cited by 57 · see citing works

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Marelja, Z., Leimkühler, S., & Missirlis, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00050 · Cited by 57 · see citing works

The critical role of glutathione in maintenance of the mitochondrial genome

Ayer, A., Tan, S., Grant, C. M., Meyer, A. J., Dawes, I. W., & Perrone, G. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.023 · Cited by 54 · see citing works

Malfunctioning of the Iron–Sulfur Cluster Assembly Machinery in Saccharomyces cerevisiae Produces Oxidative Stress via an Iron-Dependent Mechanism, Causing Dysfunction in Respiratory Complexes

Gómez-Gallardo, M., Pérez‐Gallardo, R. V., Sánchez, L. A., Díaz-Pérez, A. L., Cortés‐Rojo, C., Meza‐Carmen, V., Saavedra‐Molina, A., Lara‐Romero, J., Jiménez‐Sandoval, S., Rodríguez, F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111585 · Cited by 54 · see citing works

Artificial Evolution of Graphene Oxide Chemzyme with Enantioselectivity and Near‐Infrared Photothermal Effect for Cascade Biocatalysis Reactions

Xu, C., Zhao, C., Li, M., Wu, L. J., Ren, J., & Qu, X. (2014) · Small · doi:10.1002/smll.201302750 · Cited by 54 · see citing works

Hammering out details: regulating metal levels in eukaryotes

Ehrensberger, K. M., & Bird, A. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.07.002 · Cited by 53 · see citing works

Iron-Dependent Autophagic Cell Death Induced by Radiation in MDA-MB-231 Breast Cancer Cells

Ma, S., Fu, X., Liu, L., Liu, Y., Feng, H., Jiang, H., Liu, X., Liu, R., Liang, Z., Li, M., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.723801 · Cited by 49 · see citing works

Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress

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

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

Shawn, the Drosophila Homolog of SLC25A39/40, Is a Mitochondrial Carrier That Promotes Neuronal Survival

Slabbaert, J. R., Kuenen, S., Swerts, J., Maes, I., Uytterhoeven, V., Kasprowicz, J., Fernandes, A. C., Blust, R., & Verstreken, P. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3432-15.2016 · Cited by 50 · see citing works

Evidence that yeast frataxin is not an iron storage protein in vivo

Seguin, A., Šuťák, R., Bulteau, A., García‐Serres, R., Oddou, J., Lefevre, S. D., Santos, R., Dancis, A., Camadro, J., Latour, J., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.03.008 · Cited by 46 · see citing works

Rim2, a pyrimidine nucleotide exchanger, is needed for iron utilization in mitochondria

Yoon, H., Zhang, Y., Pain, J., Lyver, E. R., Lesuisse, E., Pain, D., & Dancis, A. (2011) · Biochemical Journal · doi:10.1042/bj20111036 · Cited by 45 · see citing works

Synthesis and spectroscopic characterization of medicinal azo derivatives and metal complexes of Indandion

Ahmad, K., Naseem, H. A., Parveen, S., Shah, H. U. R., Shah, S. S. A., Shaheen, S., Ashfaq, A., Jamil, J., Ahmad, M., & Ashfaq, M. H. (2019) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2019.126885 · Cited by 43 · see citing works

Mitochondrial Iron Metabolism and Sideroblastic Anemia

Sheftel, A. D., Richardson, D. R., Prchal, J. T., & Ponka, P. (2009) · Acta Haematologica · doi:10.1159/000243796 · Cited by 41 · see citing works

Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage

Irazusta, V. P., Òbis, È., Moreno-Cermeño, A., Cabiscol, E., Ros, J., & Tamarit, J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.010 · Cited by 41 · see citing works

High density array screening to identify the genetic requirements for transition metal tolerance in Saccharomyces cerevisiae

Bleackley, M. R., Young, B. P., Loewen, C. J. R., & MacGillivray, R. T. A. (2011) · Metallomics · doi:10.1039/c0mt00035c · Cited by 41 · see citing works

Prolonged ethanol administration depletes mitochondrial DNA in MnSOD-overexpressing transgenic mice, but not in their wild type littermates

Larosche, I., Choumar, A., Fromenty, B., Lettéron, P., Abbey‐Toby, A., Remmen, H. V., Epstein, C. J., Richardson, A. G., Feldmann, G., Pessayre, D., et al. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.11.004 · Cited by 38 · see citing works

Metal uptake by manganese superoxide dismutase

Whittaker, J. W. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.08.014 · Cited by 37 · see citing works

Old Dogs, New Tricks: New Insights into the Iron/Manganese Superoxide Dismutase Family

Frye, K. A., Sendra, K. M., Waldron, K. J., & Kehl-Fie, T. E. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.111748 · Cited by 36 · see citing works

The Mtm1p carrier and pyridoxal 5′-phosphate cofactor trafficking in yeast mitochondria

Whittaker, M. M., Penmatsa, A., & Whittaker, J. W. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.01.021 · Cited by 36 · see citing works

The mitochondrial ABC transporter Atm1 plays a role in iron metabolism and virulence in the human fungal pathogen Cryptococcus neoformans

Do, E., Park, S., Li, M., Wang, J.-M., Ding, C., Kronstad, J. W., & Jung, W. H. (2017) · Medical Mycology · doi:10.1093/mmy/myx073 · Cited by 36 · see citing works

Blood Iron Homeostasis: Newly Discovered Proteins and Iron Imbalance

Bleackley, M. R., Wong, A. Y. K., Hudson, D. M., Wu, C., & MacGillivray, R. T. A. (2009) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2008.12.001 · Cited by 37 · see citing works

Transition Metal Nutrition

Hanikenne, M., Merchant, S., & Hamel, P. P. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-370873-1.00018-6 · Cited by 36 · see citing works

Inhibition of electron transport chain assembly and function promotes photodynamic killing of Candida

Chabrier‐Roselló, Y., Giesselman, B. R., Andino, F. D. J., Foster, T. H., Mitra, S., & Haidaris, C. G. (2010) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2010.03.005 · Cited by 34 · see citing works

AtMTM1, a novel mitochondrial protein, may be involved in activation of the manganese-containing superoxide dismutase in Arabidopsis

Su, Z. Z., Chai, M., Lu, P., An, R. F., Chen, J., & Wang, X. (2007) · Planta · doi:10.1007/s00425-007-0547-6 · Cited by 33 · see citing works

Trace elements profile is associated with insulin resistance syndrome and oxidative damage in thyroid disorders: Manganese and selenium interest in Algerian participants with dysthyroidism

Maouche, N., Meskine, D., Alamir, B., & Koceir, E.-A. (2015) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2015.07.002 · Cited by 29 · see citing works

Drosophila melanogaster Mitochondrial Carriers: Similarities and Differences with the Human Carriers

Curcio, R., Lunetti, P., Zara, V., Ferramosca, A., Marra, F., Fiermonte, G., Cappello, A. R., Leonardis, F. D., Capobianco, L., & Dolce, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176052 · Cited by 28 · see citing works

Posttranslational Regulation of the Scaffold for Fe-S Cluster Biogenesis, Isu

Andrew, A. J., Song, J.-Y., Schilke, B. A., & Craig, E. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0622 · Cited by 28 · see citing works

Manganese-driven CoQ deficiency

Diessl, J., Berndtsson, J., Broeskamp, F., Habernig, L., Kohler, V., Vazquez‐Calvo, C., Nandy, A., Peselj, C., Drobysheva, S., Pélosi, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33641-x · Cited by 26 · see citing works

Loss of Ssq1 leads to mitochondrial dysfunction, activation of autophagy and cell cycle arrest due to iron overload triggered by mitochondrial iron–sulfur cluster assembly defects in Candida albicans

Dong, Y., Zhang, D., Yu, Q., Zhao, Q., Xiao, C., Zhang, K., Jia, C., Chen, S., Zhang, B., Zhang, B., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.01.021 · Cited by 26 · see citing works

Biophysical probes of iron metabolism in cells and organelles

Lindahl, P. A., & Holmes‐Hampton, G. P. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.01.007 · Cited by 26 · see citing works

In vitro preparation of iron-substituted human manganese superoxide dismutase: Possible toxic properties for mitochondria

Yamakura, F., Kobayashi, K., Furukawa, S., & Suzuki, Y. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.04.024 · Cited by 26 · see citing works

PICOT alleviates myocardial ischemia-reperfusion injury by reducing intracellular levels of reactive oxygen species

Kim, J., Kim, J., Kook, H. Y., & Park, W. J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.136 · Cited by 26 · see citing works

Intestinal response to dietary manganese depletion in Drosophila

Vásquez-Procopio, J., Osorio, B., Cortés‐Martínez, L., Hernández‐Hernández, F. D. L. C., Contreras, O. M., Ríos‐Castro, E., Comjean, A., Li, F., Hu, Y., Mohr, S. E., et al. (2019) · Metallomics · doi:10.1039/c9mt00218a · Cited by 26 · see citing works

MnSOD Overexpression Prevents Liver Mitochondrial DNA Depletion after an Alcohol Binge but Worsens This Effect after Prolonged Alcohol Consumption in Mice

Mansouri, A., Tarhuni, A., Larosche, I., Reyl-Desmars, F., Demeilliers, C., Degoul, F., Nahon, P., Sutton, A., Moreau, R., Fromenty, B., et al. (2010) · Digestive Diseases · doi:10.1159/000324284 · Cited by 24 · see citing works

Ni induces the CRR1-dependent regulon revealing overlap and distinction between hypoxia and Cu deficiency responses in Chlamydomonas reinhardtii

Blaby, C., Castruita, M., Fitz‐Gibbon, S. T., Kropat, J., & Merchant, S. (2016) · Metallomics · doi:10.1039/c6mt00063k · Cited by 22 · see citing works

Mitochondrial superoxide dismutase Sod2 suppresses nuclear genome instability during oxidative stress

Gupta, S. V., Campos, L., & Schmidt, K. H. (2023) · Genetics · doi:10.1093/genetics/iyad147 · Cited by 22 · see citing works

The manganese superoxide dismutase Ala16Val dimorphism modulates iron accumulation in human hepatoma cells

Nahon, P., Charnaux, N., Friand, V., Prost‐Squarcioni, C., Ziol, M., Lievre, N., Trinchet, J., Beaugrand, M., Gattegno, L., Pessayre, D., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.011 · Cited by 22 · see citing works

Insights into the iron-ome and manganese-ome of Δmtm1 Saccharomyces cerevisiae mitochondria

Park, J., McCormick, S. P., Chakrabarti, M., & Lindahl, P. A. (2013) · Metallomics · doi:10.1039/c3mt00041a · Cited by 22 · see citing works

Gene variants encoding proteins involved in antioxidant defense system and the clinical expression of Wilson disease

Gromadzka, G., Kruszyńska, M., Wierzbicka, D., Litwin, T., Dzieżyc, K., Wierzchowska‐Ciok, A., Chabik, G., & Członkowska, A. (2014) · Liver International · doi:10.1111/liv.12493 · Cited by 21 · see citing works

Mitochondrial Calcium Uniporter Affects Neutrophil Bactericidal Activity during Staphylococcus aureus Infection

Monteith, A. J., Miller, J. M., Beavers, W. N., Maloney, K. N., Seifert, E. L., Hajnóczky, G., & Skaar, E. P. (2021) · Infection and Immunity · doi:10.1128/iai.00551-21 · Cited by 20 · see citing works

Impacts of Mn, Fe, and Oxidative Stressors on MnSOD Activation by AtMTM1 and AtMTM2 in Arabidopsis

Hu, S.-H., & Jinn, T.-L. (2022) · Plants · doi:10.3390/plants11050619 · Cited by 19 · see citing works

Purified Glycosaminoglycans from Cooked Haddock May Enhance Fe Uptake Via Endocytosis in a Caco‐2 Cell Culture Model

Laparra, J. M., Barberá, R., Alegrı́a, A., Glahn, R. P., & Miller, D. D. (2009) · Journal of Food Science · doi:10.1111/j.1750-3841.2009.01216.x · Cited by 18 · see citing works

Deficiency in frataxin homologue YFH1 in the yeast Pichia guilliermondii leads to missregulation of iron acquisition and riboflavin biosynthesis and affects sulfate assimilation

Pynyaha, Y. V., Boretsky, Y. R., Fedorovych, D. V., Fayura, L. R., Levkiv, A. I., Ubiyvovk, V. M., Protchenko, O. V., Philpott, C. C., & Sibirny, A. А. (2009) · BioMetals · doi:10.1007/s10534-009-9256-x · Cited by 16 · see citing works

Proteomic studies of micronutrient deficiency and toxicity

Ali, A., Bhat, B. A., Rather, G. A., Malla, B. A., & Ganie, S. A. (2020) · Plant Micronutrients · doi:10.1007/978-3-030-49856-6_11 · Cited by 15 · see citing works

MTM1 plays an important role in the regulation of zinc tolerance in Saccharomyces cerevisiae

Bian, J., Wang, L., Jie, W., Simth, N., Zhang, L., Wang, Y., & Wu, X. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126759 · Cited by 15 · see citing works

Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae

Whittaker, M. M., & Whittaker, J. W. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.04.016 · Cited by 15 · see citing works

Iron-mediated degradation of ribosomes under oxidative stress is attenuated by manganese

Smethurst, D. G. J., Kovalev, N., McKenzie, E. R., Pestov, D. G., & Shcherbik, N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015025 · Cited by 15 · see citing works

Colocalization of MnSOD expression in response to oxidative stress

Li, Y., Reuter, N. P., Li, X., Liu, Q., Zhang, J., & Martin, R. C. G. (2009) · Molecular Carcinogenesis · doi:10.1002/mc.20575 · Cited by 14 · see citing works

Selenium–Chromium(VI) Interaction Regulates the Contents and Correlations of Trace Elements in Chicken Brain and Serum

Zhu, Y., Chen, P., Wan, H., Wang, Y., Pan, H., Liu, Y., & Liu, J. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-1038-7 · Cited by 14 · see citing works

The Interaction of Mitochondrial Iron with Manganese Superoxide Dismutase

Naranuntarat, A., Jensen, L. T., Pazicni, S., Penner-Hahn, J. E., & Culotta, V. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026773 · Cited by 66 · see citing works

Iron toxicity and mitochondrial oxidative stress

Culotta, V., & Yang, M. (2006) · The FASEB Journal · doi:10.1096/fasebj.20.4.a36-c

Structures of native and Fe-substituted SOD2 fromSaccharomyces cerevisiae

Kang, Y., He, Y.-X., Zhao, M.-X., & Li, W. F. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111029186 · Cited by 13 · see citing works

Insights into the iron-ome and manganese-ome of Δmtm1 Saccharomyces cerevisiae mitochondria

Park, J., McCormick, S. P., Chakrabarti, M., & Lindahl, P. A. (2013) · Metallomics · doi:10.1039/c3mt00041a · Cited by 22 · see citing works

Manganese Activation of Superoxide Dismutase 2 in the Mitochondria of Saccharomyces cerevisiae

Luk, E., Yang, M., Jensen, L. T., Bourbonnais, Y., & Culotta, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504257200 · Cited by 125 · see citing works