Copper-only superoxide dismutase enzymes and iron starvation stress in Candida fungal pathogens

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · see citing works

Pathways of Oxidative Damage

Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works

Isogenic strain construction and gene mapping in Candida albicans.

Fonzi, W. A., & Irwin, M. Y. (1993) · Genetics · doi:10.1093/genetics/134.3.717 · Cited by 1,695 · 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

Superoxide accelerates DNA damage by elevating free-iron levels

Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841 · see citing works

Systematic screens of a Candida albicans homozygous deletion library decouple morphogenetic switching and pathogenicity

Noble, S. M., French, S., Kohn, L. A., Chen, V., & Johnson, A. D. (2010) · Nature Genetics · doi:10.1038/ng.605 · Cited by 678 · see citing works

Genomic insights into multidrug-resistance, mating and virulence in Candida auris and related emerging species

Muñoz, J. F., Gade, L., Chow, N. A., Loparev, V. N., Juieng, P., Berkow, E. L., Farrer, R. A., Litvintseva, A. P., & Cuomo, C. A. (2018) · Nature Communications · doi:10.1038/s41467-018-07779-6 · Cited by 458 · see citing works

Granulocytes govern the transcriptional response, morphology and proliferation of <i>Candida albicans</i> in human blood

Fradin, C., De Groot, P., MacCallum, D., Schaller, M., Klis, F., Odds, F. C., & Hube, B. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04557.x · Cited by 455 · see citing works

Generation of reactive oxygen species by fungal NADPH oxidases is required for rice blast disease

Egan, M. J., Wang, Z., Jones, M. A., Smirnoff, N., & Talbot, N. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700574104 · Cited by 415 · see citing works

Faster superoxide dismutase mutants designed by enhancing electrostatic guidance

Getzoff, E. D., Cabelli, D. E., Fisher, C. L., Parge, H. E., Viezzoli, M. S., Banci, L., & Hallewell, R. A. (1992) · Nature · doi:10.1038/358347a0 · Cited by 399 · see citing works

The emerging pathogen Candida auris: growth phenotype, virulence factors, activity of antifungals, and effect of SCY-078, a novel glucan synthesis inhibitor, on growth morphology and biofilm formation

Larkin, E., Hager, C., Chandra, J., Mukherjee, P. K., Retuerto, M., Salem, I., Long, L., Isham, N., Kovanda, L., Borroto-Esoda, K., et al. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02396-16 · Cited by 395 · see citing works

Transcription Profiling of <i>Candida albicans</i> Cells Undergoing the Yeast-to-Hyphal Transition

Nantel, A., Dignard, D., Bachewich, C., Harcus, D., Marcil, A., Bouin, A.-P., Sensen, C. W., Hogues, H., van het Hoog, M., Gordon, P., et al. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-05-0272 · Cited by 378 · see citing works

Decreased Metallation and Activity in Subsets of Mutant Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis

Hayward, L. J., Rodriguez, J. A., Kim, J. W., Tiwari, A., Goto, J. J., Cabelli, D. E., Valentine, J. S., & Brown, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112087200 · Cited by 377 · see citing works

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

P., L. H., Tettelin, H., Vossen, J. H., Ram, A. F. J., ENDE, H. V. D., & Klis, F. M. (1997) · Yeast · doi:10.1002/(sici)1097-0061(199712)13:15 · Cited by 324 · see citing works

An iron homeostasis regulatory circuit with reciprocal roles in Candida albicans commensalism and pathogenesis

Chen, C., Pande, K., French, S. D., Tuch, B. B., & Noble, S. M. (2011) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2011.07.005 · Cited by 314 · see citing works

Superoxide Dismutases in <i>Candida albicans</i> : Transcriptional Regulation and Functional Characterization of the Hyphal-induced <i>SOD5</i> Gene

Martchenko, M., Alarco, A.-M., Harcus, D., & Whiteway, M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-03-0179 · Cited by 290 · see citing works

Genome-wide identification of fungal GPI proteins.

de Groot, P. W. J., Hellingwerf, K. J., & Klis, F. M. (2003) · Yeast · doi:10.1002/yea.1007 · Cited by 276 · see citing works

Candida albicans cell surface superoxide dismutases degrade host‐derived reactive oxygen species to escape innate immune surveillance

Frohner, I. E., Bourgeois, C., Yatsyk, K., Majer, O., & Kuchler, K. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06528.x · Cited by 267 · see citing works

Proteomic Analysis of Candida albicans Cell Walls Reveals Covalently Bound Carbohydrate-Active Enzymes and Adhesins

de Groot, P. W. J., de Boer, A. D., Cunningham, J., Dekker, H. L., de Jong, L., Hellingwerf, K. J., de Koster, C. G., & Klis, F. M. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.4.955-965.2004 · Cited by 266 · see citing works

Candida albicans biofilm–induced vesicles confer drug resistance through matrix biogenesis

Zarnowski, R., Sanchez, H., Covelli, A. S., Dominguez, E., Jaromin, A., Bernhardt, J., Mitchell, K. F., Heiss, C., Azadi, P., Mitchell, A., et al. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2006872 · Cited by 260 · see citing works

Oxidative Stress and the Homeodynamics of Iron Metabolism

Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works

Draft genome of a commonly misdiagnosed multidrug resistant pathogen Candida auris

Chatterjee, S., Alampalli, S. V., Nageshan, R. K., Chettiar, S. T., Joshi, S., & Tatu, U. S. (2015) · BMC Genomics · doi:10.1186/s12864-015-1863-z · Cited by 247 · see citing works

Can Multidrug-Resistant Candidaauris Be Reliably Identified in Clinical Microbiology Laboratories?

Mizusawa, M., Miller, H., Green, R., Lee, R. E., Jr., Durante, M., Perkins, R., Hewitt, C. M., Simner, P. J., Carroll, K. C., Hayden, R. T., et al. (2016) · Journal of Clinical Microbiology · doi:10.1128/jcm.02202-16 · Cited by 218 · see citing works

Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase

Cudd, A., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33779-7 · Cited by 211 · see citing works

Protection by Anti-β-Glucan Antibodies Is Associated with Restricted β-1,3 Glucan Binding Specificity and Inhibition of Fungal Growth and Adherence

Torosantucci, A., Chiani, P., Bromuro, C., de Bernardis, F., Palma, A., Liu, Y., Mignogna, G., Maras, B., Colone, M., Stringaro, A., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005392 · Cited by 195 · see citing works

NADPH Oxidases NOX-1 and NOX-2 Require the Regulatory Subunit NOR-1 To Control Cell Differentiation and Growth in Neurospora crassa

Cano-Domínguez, N., Álvarez-Delfín, K., Hansberg, W., & Aguirre, J. (2008) · Eukaryotic Cell · doi:10.1128/ec.00137-08 · Cited by 193 · see citing works

Copper–zinc superoxide dismutase: Why not pH-dependent?

Ellerby, L. M., Cabelli, D. E., Graden, J. A., & Valentine, J. S. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953845x · Cited by 184 · see citing works

Filamentation in <i>Candida auris</i> , an emerging fungal pathogen of humans: passage through the mammalian body induces a heritable phenotypic switch

Yue, H., Bing, J., Zheng, Q., Zhang, Y., Hu, T., Du, H., Wang, H., & Huang, G. (2018) · Emerging Microbes &amp; Infections · doi:10.1038/s41426-018-0187-x · Cited by 176 · see citing works

Comprehensive Analysis of Glycosylphosphatidylinositol-Anchored Proteins in <i>Candida albicans</i>

Richard, M. L., & Plaine, A. (2007) · Eukaryotic Cell · doi:10.1128/ec.00297-06 · Cited by 159 · see citing works

Extracellular Superoxide Dismutase Protects Histoplasma Yeast Cells from Host-Derived Oxidative Stress

Youseff, B. H., Holbrook, E. D., Smolnycki, K. A., & Rappleye, C. A. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002713 · Cited by 152 · see citing works

Unexpected Link between Iron and Drug Resistance of <i>Candida</i> spp.: Iron Depletion Enhances Membrane Fluidity and Drug Diffusion, Leading to Drug-SusceptibleCells

Prasad, T., Chandra, A., Mukhopadhyay, C. K., & Prasad, R. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00653-06 · Cited by 149 · see citing works

Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)

Banci, L., Bertini, I., Cantini, F., Kozyreva, T., Massagni, C., Palumaa, P., Rubino, J. T., & Zovo, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207493109 · Cited by 142 · see citing works

An Efficient, Rapid, and Recyclable System for CRISPR-Mediated Genome Editing in Candida albicans

Nguyen, N., Quail, M. M., & Hernday, A. D. (2017) · mSphere · doi:10.1128/mspheredirect.00149-17 · Cited by 137 · see citing works

Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense

Gleason, J. E., Galaleldeen, A., Peterson, R. L., Taylor, A. B., Holloway, S. P., Waninger‐Saroni, J., Cormack, B. P., Cabelli, D. E., Hart, P. J., & Culotta, V. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400137111 · Cited by 127 · see citing works

Yeast wall protein 1 of Candida albicans

Granger, B. L., Flenniken, M. L., Davis, D. A., Mitchell, A. P., & Cutler, J. E. (2005) · Microbiology · doi:10.1099/mic.0.27663-0 · Cited by 126 · see citing works

The role of arginine 143 in the electrostatics and mechanism of Cu, Zn superoxide dismutase: Computational and experimental evaluation by mutational analysis

Fisher, C. L., Cabelli, D. E., Tainer, J. A., Hallewell, R. A., & Getzoff, E. D. (1994) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340190105 · Cited by 125 · see citing works

Mechanism of Cu,Zn-Superoxide Dismutase Activation by the Human Metallochaperone hCCS

Rae, T., Torres, A. S., Pufahl, R. A., & O’Halloran, T. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008005200 · Cited by 125 · see citing works

Amino Acid Residues in the ω-Minus Region Participate in Cellular Localization of Yeast Glycosylphosphatidylinositol-Attached Proteins

Hamada, K., Terashima, H., Arisawa, M., Yabuki, N., & Kitada, K. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.13.3886-3889.1999 · Cited by 123 · see citing works

Cellular Responses of Candida albicans to Phagocytosis and the Extracellular Activities of Neutrophils Are Critical to Counteract Carbohydrate Starvation, Oxidative and Nitrosative Stress

Miramón, P., Dunker, C., Windecker, H., Bohovych, I., Brown, A. J. P., Kurzai, O., & Hube, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052850 · Cited by 123 · see citing works

Candida albicans adapts to host copper during infection by swapping metal cofactors for superoxide dismutase

Li, C. X., Gleason, J. E., Zhang, S. X., Bruno, V. M., Cormack, B. P., & Culotta, V. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513447112 · Cited by 121 · see citing works

A Relay Network of Extracellular Heme-Binding Proteins Drives C. albicans Iron Acquisition from Hemoglobin

Kuznets, G., Vigonsky, E., Weissman, Z., Lalli, D., Gildor, T., Kauffman, S. J., Turano, P., Becker, J., Lewinson, O., & Kornitzer, D. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004407 · Cited by 118 · see citing works

Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains

Robinett, N. G., Peterson, R. L., & Culotta, V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000182 · Cited by 118 · see citing works

Roles of Candida albicans Dfg5p and Dcw1p Cell Surface Proteins in Growth and Hypha Formation

Spreghini, E., Davis, D. A., Subaran, R. L., Kim, M. H., & Mitchell, A. P. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.4.746-755.2003 · Cited by 114 · see citing works

Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase

Oury, T. D., Crapo, J. D., Valnickova, Z., & Enghild, J. J. (1996) · Biochemical Journal · doi:10.1042/bj3170051 · Cited by 111 · see citing works

Candida albicans specializations for iron homeostasis: from commensalism to virulence

Noble, S. M. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.09.006 · Cited by 104 · see citing works

Hyphal induction in the human fungal pathogen Candida albicans reveals a characteristic wall protein profile

Heilmann, C. J., Sorgo, A. G., Siliakus, A. R., Dekker, H. L., Brul, S., de Koster, C. G., de Koning, L. J., & Klis, F. M. (2011) · Microbiology · doi:10.1099/mic.0.049395-0 · Cited by 103 · see citing works

The moonlighting protein Tsa1p is implicated in oxidative stress response and in cell wall biogenesis in Candida albicans

Urban, C. F., Xiong, X. B., Sohn, K., Schröppel, K., Brunner, H., & Rupp, S. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04771.x · Cited by 95 · see citing works

Mass spectrometric analysis of the secretome of <i>Candida albicans</i>

Sorgo, A. G., Heilmann, C. J., Dekker, H. L., Brul, S., de Koster, C. G., & Klis, F. M. (2010) · Yeast · doi:10.1002/yea.1775 · Cited by 93 · see citing works

Crystal Structure of the Second Domain of the Human Copper Chaperone for Superoxide Dismutase,

Lamb, A. L., Wernimont, A. K., Pufahl, R. A., O’Halloran, T. V., & Rosenzweig, A. C. (2000) · Biochemistry · doi:10.1021/bi992822i · Cited by 93 · see citing works

Yeast Lacking Cu-Zn Superoxide Dismutase Show Altered Iron Homeostasis

Freitas, J. M. D., Liba, A., Meneghini, R., Valentine, J. S., & Gralla, E. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11645 · Cited by 92 · see citing works

Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and secreted proteins of the ascomycetous fungi Neurospora crassa and Candida albicans

Maddi, A., Bowman, S. M., & Free, S. J. (2009) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2009.06.005 · Cited by 89 · see citing works

Multiple sequence signals determine the distribution of glycosylphosphatidylinositol proteins between the plasma membrane and cell wall in Saccharomyces cerevisiae

Frieman, M. B. (2004) · Microbiology · doi:10.1099/mic.0.27420-0 · Cited by 84 · see citing works

A Gain of Superoxide Dismutase (SOD) Activity Obtained with CCS, the Copper Metallochaperone for SOD1

Schmidt, P. J., Ramos‐Gómez, M., & Culotta, V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36952 · Cited by 84 · see citing works

Normal Adaptation of Candida albicans to the Murine Gastrointestinal Tract Requires Efg1p-Dependent Regulation of Metabolic and Host Defense Genes

Pierce, J. V., Dignard, D., Whiteway, M. S., & Kumamoto, C. A. (2012) · Eukaryotic Cell · doi:10.1128/ec.00236-12 · Cited by 84 · 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

Distinct contributions of one Fe- and two Cu/Zn-cofactored superoxide dismutases to antioxidation, UV tolerance and virulence of Beauveria bassiana

Li, F., Shi, H.-Q., Ying, S., & Feng, M. (2014) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2014.09.006 · Cited by 74 · see citing works

Early Colony Establishment in Neurospora crassa Requires a MAP Kinase Regulatory Network

Leeder, A. C., Jonkers, W., Li, J., & Glass, N. L. (2013) · Genetics · doi:10.1534/genetics.113.156984 · Cited by 74 · see citing works

Beyond the wall:Candida albicanssecret(e)s to survive

Sorgo, A. G., Heilmann, C. J., Brul, S., de Koster, C. G., & Klis, F. M. (2012) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12049 · Cited by 72 · see citing works

Candida albicans FRE8 encodes a member of the NADPH oxidase family that produces a burst of ROS during fungal morphogenesis

Rossi, D. C. P., Gleason, J. E., Sánchez, H., Schatzman, S. S., Culbertson, E. M., Johnson, C. J., McNees, C. A., Coelho, C., Nett, J. E., Andes, D. R., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006763 · Cited by 67 · see citing works

Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

Seetharaman, S. V., Winkler, D. D., Taylor, A. B., Cao, X., Whitson, L. J., Doucette, P. A., Valentine, J. S., Schirf, V. R., Demeler, B., Carroll, M. C., et al. (2010) · Biochemistry · doi:10.1021/bi100314n · Cited by 66 · see citing works

Identification and Analysis of the Role of Superoxide Dismutases Isoforms in the Pathogenesis of Paracoccidioides spp.

Tamayo, D. P., Muñoz, J. F., López, A., Urán, M. E., Herrera, J., Borges, C. L., Restrepo, Á., Soares, C. M. D. A., Taborda, C. P., Almeida, A. J., et al. (2016) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004481 · Cited by 64 · see citing works

Flavodoxin-Like Proteins Protect Candida albicans from Oxidative Stress and Promote Virulence

Li, L., Naseem, S., Sharma, S., & Konopka, J. B. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005147 · Cited by 61 · see citing works

Comparative Evolution of Morphological Regulatory Functions in Candida Species

Lackey, E., Vipulanandan, G., Childers, D. S., & Kadosh, D. (2013) · Eukaryotic Cell · doi:10.1128/ec.00164-13 · Cited by 61 · see citing works

Oxygen accessibility and iron levels are critical factors for the antifungal action of ciclopirox against Candida albicans

Sigle, H.-C., Thewes, S., Niewerth, M., Körting, H. C., Schäfer‐Korting, M., & Hube, B. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki089 · Cited by 58 · see citing works

Adaptive Prediction As a Strategy in Microbial Infections

Brunke, S., & Hube, B. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004356 · Cited by 57 · see citing works

Iron deprivation inducesEFG1-mediated hyphal development inCandida albicanswithout affecting biofilm formation

Hameed, S., Prasad, T., Banerjee, D., Chandra, A., Mukhopadhyay, C. K., Goswami, S. K., Lattif, A. A., Chandra, J., Mukherjee, P. K., Ghannoum, M. A., et al. (2008) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00394.x · Cited by 53 · see citing works

A pH-dependent superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein

Pantoliano, M. W. (1982) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80093-8 · Cited by 50 · see citing works

Chemical Warfare at the Microorganismal Level: A Closer Look at the Superoxide Dismutase Enzymes of Pathogens

Schatzman, S. S., & Culotta, V. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00026 · Cited by 48 · see citing works

Iron starvation leads to increased expression of Cu/Zn‐superoxide dismutase in Aspergillus

Oberegger, H., Zadra, I., Schoeser, M., & Haas, H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02206-7 · Cited by 47 · see citing works

Finding a Missing Gene: EFG1 Regulates Morphogenesis in Candida tropicalis

Mancera, E., Porman, A. M., Cuomo, C. A., Bennett, R. J., & Johnson, A. D. (2015) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.017566 · Cited by 46 · see citing works

Species-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans

Gleason, J. E., Li, C. X., Odeh, H. M., & Culotta, V. (2013) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-013-1045-x · Cited by 41 · see citing works

An Adaptation to Low Copper in Candida albicans Involving SOD Enzymes and the Alternative Oxidase

Broxton, C. N., & Culotta, V. C. (2016) · PLOS ONE · doi:10.1371/journal.pone.0168400 · Cited by 41 · see citing works

Iron restriction-induced adaptations in the wall proteome of Candida albicans

Sorgo, A. G., Brul, S., de Koster, C. G., de Koning, L. J., & Klis, F. M. (2013) · Microbiology · doi:10.1099/mic.0.065599-0 · Cited by 40 · see citing works

A family of secreted pathogenesis‐related proteins in C andida albicans

Rohm, M., Lindemann, E., Hiller, E., Ermert, D., Lemuth, K., Trkulja, D., Sogukpinar, O., Brunner, H., Rupp, S., Urban, C. F., et al. (2012) · Molecular Microbiology · doi:10.1111/mmi.12087 · Cited by 40 · see citing works

Iron Deficiency Generates Oxidative Stress and Activation of the SOS Response in Caulobacter crescentus

Leaden, L., Silva, L. G., Ribeiro, R. A., dos Santos, N. M., Lorenzetti, A. P. R., Alegria, T. G. P., Schulz, M. L., de Medeiros, M. H. G., Koide, T., & Marques, M. V. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02014 · Cited by 39 · see citing works

The Phylogeny and Active Site Design of Eukaryotic Copper-only Superoxide Dismutases

Peterson, R. L., Galaleldeen, A., Villarreal, J., Taylor, A. B., Cabelli, D. E., Hart, P. J., & Culotta, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.748251 · Cited by 38 · see citing works

The oxidative stress response in yeast cells involves changes in the stability of Aft1 regulon mRNAs

Castells‐Roca, L., Mühlenhoff, U., Lill, R., Herrero, E., & Bellı́, G. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07689.x · Cited by 36 · see citing works

Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human C u,Z n superoxide dismutase

Fisher, C. L., Cabelli, D. E., Hallewell, R. A., Beroza, P., Lo, T. P., Getzoff, E. D., & Tainer, J. A. (1997) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199709)29:1 · Cited by 32 · see citing works

ERG11 couples oxidative stress adaptation, hyphal elongation and virulence in Candida albicans

Wu, Y., Wu, M., Wang, Y., Chen, Y., Gao, J. Q., & Ying, C. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy057 · Cited by 31 · see citing works

The pH dependence of apparent binding constants between apo-superoxide dismutase and cupric ions

Hirose, J., Ohhira, T., Hirata, H., & Kidani, Y. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90334-4 · Cited by 29 · see citing works

Exploiting the vulnerable active site of a copper-only superoxide dismutase to disrupt fungal pathogenesis

Robinett, N. G., Culbertson, E. M., Peterson, R. L., Sánchez, H., Andes, D. R., Nett, J. E., & Culotta, V. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007095 · Cited by 25 · see citing works

The iron-dependent regulation of the Candida albicans oxidative stress response by the CCAAT-binding factor

Chakravarti, A., Camp, K., McNabb, D. S., & Pinto, I. (2017) · PLOS ONE · doi:10.1371/journal.pone.0170649 · Cited by 24 · see citing works

Proteogenomics of Candida tropicalis —An Opportunistic Pathogen with Importance for Global Health

Datta, K. K., Patil, A. H., Patel, K., Dey, G., Madugundu, A. K., Renuse, S., Kaviyil, J. E., Nirujogi, R. S., Arunima, A., Daswani, B., et al. (2016) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2015.0197 · Cited by 19 · see citing works

RacA-Mediated ROS Signaling Is Required for Polarized Cell Differentiation in Conidiogenesis of Aspergillus fumigatus

Chi, M., & Craven, K. D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149548 · Cited by 17 · see citing works

Cth2 Protein Mediates Early Adaptation of Yeast Cells to Oxidative Stress Conditions

Castells‐Roca, L., Pijuan, J., Ferrezuelo, F., Bellı́, G., & Herrero, E. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148204 · Cited by 11 · see citing works

Cold Shock as a Screen for Genes Involved in Cold Acclimatization in Neurospora crassa

Watters, M. K., Manzanilla, V., Howell, H., Mehreteab, A., Rose, E., Walters, N. A., Seitz, N. C., Nava, J., Kekelik, S., Knuth, L., et al. (2018) · G3 Genes Genomes Genetics · doi:10.1534/g3.118.200112 · Cited by 7 · see citing works

Superoxide dismutase and neurological disorders

Chidambaram, S. B., Anand, N., Varma, S. R., Ramamurthy, S., Vichitra, C., Sharma, A., Mahalakshmi, A. M., & Essa, M. M. (2024) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.11.007 · Cited by 141 · see citing works

Iron alters the cell wall composition and intracellular lactate to affect Candida albicans susceptibility to antifungals and host immune response

Tripathi, A., Liverani, E., Tsygankov, A. Y., & Puri, S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013413 · Cited by 56 · see citing works

Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking

Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 59 · see citing works

Emerging role of antioxidants in Alzheimer's disease: Insight into physiological, pathological mechanisms and management

Kamaljeet, Singh, S., Gupta, G. D., & Aran, K. R. (2023) · Pharmaceutical Science Advances · doi:10.1016/j.pscia.2023.100021 · Cited by 52 · see citing works

The Role of B-Cells and Antibodies against Candida Vaccine Antigens in Invasive Candidiasis

Shukla, M., Chandley, P., & Rohatgi, S. (2021) · Vaccines · doi:10.3390/vaccines9101159 · Cited by 43 · see citing works

Superoxide Dismutase: A Key Enzyme for the Survival of Intracellular Pathogens in Host

Maurya, R., & Namdeo, M. (2021) · Biochemistry · doi:10.5772/intechopen.100322 · Cited by 37 · see citing works

“Under Pressure” – How fungi evade, exploit, and modulate cells of the innate immune system

Lange, T., Kasper, L., Gresnigt, M., Brunke, S., & Hube, B. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101738 · Cited by 29 · see citing works

A Cu‐only superoxide dismutase from stripe rust fungi functions as a virulence factor deployed for counter defense against host‐derived oxidative stress

Zheng, P., Chen, L., Zhong, S., Wei, X., Zhao, Q., Pan, Q., Kang, Z., & Liu, J. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15236 · Cited by 28 · see citing works

Expanded role of the Cu‐sensing transcription factor Mac1p in Candida albicans

Culbertson, E. M., Bruno, V. M., Cormack, B. P., & Culotta, V. (2020) · Molecular Microbiology · doi:10.1111/mmi.14591 · Cited by 21 · see citing works

The role of manganese in morphogenesis and pathogenesis of the opportunistic fungal pathogen Candida albicans

Wildeman, A. S., Patel, N. K., Cormack, B. P., & Culotta, V. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011478 · Cited by 18 · see citing works

Transcriptomics integrated with metabolomics reveal the competitive relationship between co-cultured Trichoderma asperellum HG1 and Bacillus subtilis Tpb55

Li, Q., Lin, W., Zhang, X., Wang, M., Zheng, Y., Wang, X., Gao, G., Li, Y., Zhao, D., & Zhang, C. (2024) · Microbiological Research · doi:10.1016/j.micres.2023.127598 · Cited by 19 · see citing works

Oxidative Stress Causes Vacuolar Fragmentation in the Human Fungal Pathogen Cryptococcus neoformans

Kim, D., Song, M., Do, E., Choi, Y., Kronstad, J. W., & Jung, W. H. (2021) · Journal of Fungi · doi:10.3390/jof7070523 · Cited by 18 · see citing works

Sertraline Has Fungicidal Activity Against Candida Spp. and Acts by Inhibiting Membrane and Cell Wall Biosynthesis

Rodrigues, D. S., Cabral, V. P. D. F., Barbosa, A. D., Sá, L. G. D. A. V., da Silva, C. R., Moreira, L. E. A., Neto, J. B., Silva, J., dos Santos, H. S., Marinho, E. S., et al. (2023) · Future Microbiology · doi:10.2217/fmb-2022-0254 · Cited by 18 · see citing works

Alternative oxidase promotes high iron tolerance in Candida albicans

Sharma, R., Gibb, A., Barnts, K. L., Elrod, J. W., & Puri, S. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02157-23 · Cited by 17 · see citing works

Postharvest biocontrol ability and involved mechanism of volatile organic compounds from Serratia nematodiphila BC-SKRU-1 against Penicillium digitatum tangerine fruit

Boukaew, S., Yossan, S., Petlamul, W., Nooprom, K., Sakphet, N., Chumkaew, K., Srinuanpan, S., & Zhang, Z. (2024) · Food Control · doi:10.1016/j.foodcont.2024.110735 · Cited by 16 · see citing works

Insight into the Mechanisms and Clinical Relevance of Antifungal Heteroresistance

Su, Y., Li, Y., Yi, Q., Xu, Y., Sun, T., & Li, Y. (2025) · Journal of Fungi · doi:10.3390/jof11020143 · Cited by 18 · see citing works

Transcriptomic meta-analysis to identify potential antifungal targets in Candida albicans

Hefny, Z. A., Ji, B., Elsemman, I. E., Nielsen, J., & Dijck, P. V. (2024) · BMC Microbiology · doi:10.1186/s12866-024-03213-8 · Cited by 15 · see citing works

“We've got to get out”—Strategies of human pathogenic fungi to escape from phagocytes

Sonnberger, J., Kasper, L., Lange, T., Brunke, S., & Hube, B. (2023) · Molecular Microbiology · doi:10.1111/mmi.15149 · Cited by 14 · see citing works

Chemometric study on the biochemical marker of the manglicolous fungi to illustrate its potentiality as a bio indicator for heavy metal pollution in Indian Sundarbans

Mahanty, S., Tudu, P., Ghosh, S., Chatterjee, S., Das, P., Bhattacharyya, S., Das, S., Acharya, K., & Chaudhuri, P. (2021) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2021.113017 · Cited by 14 · see citing works

The good, the bad, and the hazardous: comparative genomic analysis unveils cell wall features in the pathogen Candidozyma auris typical for both baker’s yeast and Candida

Alvarado, M., Navajas, J. A. G., Muñoz, M. T. B., Gómez-Molero, E., Fernández-Sánchez, S., Eraso, E., Munro, C. A., Valentı́n, E., Mateo, E., & de Groot, P. W. J. (2024) · FEMS Yeast Research · doi:10.1093/femsyr/foae039 · Cited by 13 · see citing works

Copper Availability Influences the Transcriptomic Response of Candida albicans to Fluconazole Stress

Hunsaker, E. W., Yu, C.-H. A., & Franz, K. J. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab065 · Cited by 13 · see citing works

Cdc42 regulates reactive oxygen species production in the pathogenic yeast Candida albicans

Kowalewski, G. P., Wildeman, A. S., Bogliolo, S., Besold, A. N., Bassilana, M., & Culotta, V. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100917 · Cited by 13 · see citing works

Mechanisms and regulation of iron uptake and the role of iron in pathogenesis of <i>Candida albicans</i>

Zheng, D., Zhang, X., Ding, J., Yue, D., Yang, F., & Li, Y. (2025) · Critical reviews in microbiology · doi:10.1080/1040841x.2025.2510256 · Cited by 10 · see citing works

Berberine inhibitsCandida albicansgrowth by disrupting mitochondrial function through the reduction of iron absorption

Zheng, D., Yue, D., Shen, J., Li, D., Song, Z., Huang, Y., Yong, J., & Li, Y. (2023) · Journal of Applied Microbiology · doi:10.1093/jambio/lxad276 · Cited by 10 · see citing works

Copper only SOD repeat proteins likely act as an extracellular superoxide dismutase in oyster antioxidant defense

Tan, L., Liu, Y., Sun, Y., Liu, S., Lin, Z., & Xue, Q. (2025) · Scientific Reports · doi:10.1038/s41598-025-06156-w · Cited by 10 · see citing works

Transcriptome Analysis Reveals That C17 Mycosubtilin Antagonizes Verticillium dahliae by Interfering with Multiple Functional Pathways of Fungi

Zhang, Q., Lin, R., Yang, J., Zhao, J., Li, H., Liu, K., Xue, X., Zhao, H., Han, S., & Zhao, H. (2023) · Biology · doi:10.3390/biology12040513 · Cited by 10 · see citing works

The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans

Farci, D., Graça, A. T., Iesu, L., de Sanctis, D., & Piano, D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102784 · Cited by 10 · see citing works

Ceruloplasmin as a source of Cu for a fungal pathogen

Besold, A. N., Shanbhag, V., Petris, M. J., & Culotta, V. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111424 · Cited by 9 · see citing works

Antifungal Activity and Potential Mechanisms of Two Bafilomycin Analogues Isolated from Streptomyces sp. NEAU-Y11 against Colletotrichum orbiculare

Song, W., Yu, X., Yu, X., Zhang, H., Zhang, K., Guo, L., Wang, J., Tian, D., Yu, Q., Wang, X., et al. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c03728 · Cited by 8 · see citing works

Poacic Acid, a Plant-Derived Stilbenoid, Augments Cell Wall Chitin Production, but Its Antifungal Activity Is Hindered by This Polysaccharide and by Fungal Essential Metals

Yona, A., & Fridman, M. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00595 · Cited by 7 · see citing works

A response to iron involving carbon metabolism in the opportunistic fungal pathogen Candida albicans

Garg, R., Zhu, Z., Hernandez, F. G., Wang, Y., David, M. S., Bruno, V. M., & Culotta, V. (2025) · mSphere · doi:10.1128/msphere.00040-25 · Cited by 7 · see citing works

Xenosiderophore transporter gene expression and clade-specific filamentation in Candida auris killifish (Aphanius dispar) infection

Gifford, H., Bedekovic, T., Helmstetter, N., Gregory, J., Ma, Q., Brand, A., Wilson, D., Rhodes, J. L., Ramsdale, M., Kudoh, T., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-09321-z · Cited by 8 · see citing works

Insight into Virulence and Mechanisms of Amphotericin B Resistance in the Candida haemulonii Complex

Huang, Y., Su, Y., Chen, X., Xiao, M., & Xu, Y. (2024) · Journal of Fungi · doi:10.3390/jof10090615 · Cited by 7 · see citing works

Nutrition-Associated Processes Govern Fungal Pathogenicity

Gao, X., Fu, Y., & Ding, C. (2021) · Infectious Microbes & Diseases · doi:10.1097/im9.0000000000000055 · Cited by 6 · see citing works

A roadmap to chemically reactive species: how diverse oxidants affect Candida albican s and other fungi

Swenson, K. A., Alberti, L., Teele, K., Yadav, A., Shah, S. J., & Konopka, J. B. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00229-24 · Cited by 6 · see citing works

The emerging pathogen Candida auris: host interactions and disease drivers

Sanya, D. R. A., Arevalo, A. V., Onésime, D., & Nobile, C. J. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-026-01230-5 · Cited by 5 · see citing works

Biochemical Analysis of CaurSOD4, a Potential Therapeutic Target for the Emerging Fungal Pathogen Candida auris

Chandler, C. E., Hernandez, F. G., Totten, M., Robinett, N. G., Schatzman, S. S., Zhang, S. X., & Culotta, V. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00590 · Cited by 4 · see citing works

Deletion of RAP1 affects iron homeostasis, azole resistance, and virulence in Candida albicans

Yang, M.-C., Huang, W.-L., Chen, H., Lin, S.-H., Chang, Y.-S., Tseng, K., Lo, H., Wang, I., Lin, C.-J., & Lan, C. (2025) · mSphere · doi:10.1128/msphere.00155-25 · Cited by 3 · see citing works

Mitochondrial Complex Member VdNuo1 Recruits Superoxide Dismutases VdSOD2 /4 to Maintain Superoxide Anion Homeostasis During Pathogenesis in Verticillium dahliae

Li, H., Sheng, R., Wang, Y., Zhang, C., Wang, D., Klosterman, S. J., Zhang, D., Subbarao, K. V., Chen, F., & Chen, J. (2025) · Molecular Plant Pathology · doi:10.1111/mpp.70149 · Cited by 4 · see citing works

Genotype-Dependent Variations in Oxidative Stress Markers and Bioactive Proteins in Hereford Bulls: Associations with DGAT1, LEP, and SCD1 Genes

Kostusiak, P., Bagnicka, E., Żelazowska, B., Zalewska, M., Sakowski, T., Slósarz, J., Gołębiewski, M., & Puppel, K. (2024) · Biomolecules · doi:10.3390/biom14101309 · Cited by 2 · see citing works

Pseudogymnoascus destructans Transcriptional Response to Chronic Copper Stress

Anne, S., McDonald, M. R., Lü, Y., & Peterson, R. L. (2025) · Journal of Fungi · doi:10.3390/jof11050372 · Cited by 2 · see citing works

Crosstalk between iron and flavins in the opportunistic fungal pathogen Candida albicans

David, M. S., Zhu, Z., McDonald, M. R., Badiee, M., Mortimer, I. P., Leung, A. K. L., & Culotta, V. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110396 · Cited by 3 · see citing works

Xenosiderophore transporter gene expression and clade-specific filamentation in Candida auris killifish infectionPreprint

Gifford, H., Bedekovic, T., Helmstetter, N., Gregory, J., Ma, Q., Brand, A., Wilson, D., Rhodes, J. L., Ramsdale, M., Kudoh, T., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.22.619744 · Cited by 2 · see citing works

Role of Vaccines and Monoclonal Antibodies in Systemic Candidiasis: Past and Future Approaches

Chandley, P., & Rohatgi, S. (2025) · Fungal biology · doi:10.1007/978-3-032-06014-3_8 · Cited by 1 · see citing works

The Four Critical Priority Fungi According to the World Health Organization and the Hope for New Therapies: A Focus on Cell Wall Antifungal Targets

Marena, G. D., Carvalho, G. C., Magalhães, M. H. C., Figueiredo, J., Ramos, D. H., Nosanchuk, J. D., & Taborda, C. P. (2026) · Journal of Fungi · doi:10.3390/jof12030162 · Cited by 1 · see citing works

Antifungal Activity of Cisatracurium Against Fluconazole-Resistant Candida Isolates and its Antibiofilm Effects

do Nascimento, F. B. S. A., Sá, L. G. D. A. V., Neto, J. B. D. A., Cabral, V. P. D. F., Rodrigues, D. S., Barbosa, A. D., Moreira, L. E. A., de Oliveira, L. C., da Silva, A. S., Lima, I. S. P., et al. (2023) · Future Microbiology · doi:10.2217/fmb-2022-0224

Ekstrak Akar Purwoceng sebagai neuroprotektan Terhadap Model Stroke pada Tikus: Memori Spasial, Jumlah Sel Piramidal, Ekspresi SOD1 dan SOD2

Munawaroh, F., Efiyanti, C., Utami, P., Dewi, T., & Batubara, I. (2024) · Jurnal Tumbuhan Obat Indonesia · doi:10.31002/jtoi.v17i2.2236

Controllable Engineered Probiotic Hydrogel Coatings Prevent Drainage Tube‐Associated Infections by Disrupting Pathogen Oxidative Stress Responses

Wei, Y., Liu, J., Zhang, M., Chen, Y., Ma, J., & Mao, X. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.202505654

Proteomic and Secretomic Response of an African Armillaria Species to Iron

Mensah, D. L. N., Wingfield, B. D., & Coetzee, M. P. A. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00979

Copper-only Superoxide dismutase 6 contributes to reactive oxygen species regulation, genotoxic stress tolerance, and virulence in Candida albicans

Liu, Z., Li, M., Wang, J. X., & Chen, B. (2026) · Medical Mycology · doi:10.1093/mmy/myag063

Organ-specific phenotypes of Candida albicans: implications for immunity and pathogenesis.

Morris, E., Sheriff, L., & Drummond, R. A. (2026) · Current Opinion in Microbiology · doi:10.1016/j.mib.2026.102817

Oxidative stress responses in human fungal pathogens: a review of molecular mechanisms

Pereira, M. D., Costa, L. D. R., Mattos, L. M. M., Pires, D. C., Fonseca, F. L., Santos, A. L. S., & Riger, C. J. (2026) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2026.2706136

Beyond antifungal susceptibility: molecular mechanisms, detection, and clinical implications of fungal heteroresistance

Taş, E., Çetin, B., Yılmazer, A. N., & Işık, T. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12737-3

From confrontation to co-adaptation: the dynamic dialogue of Candida albicans and macrophages

Miramón, P., Wilson, H. B., & Lorenz, M. C. (2026) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00191-22

The Irony of Cu-only Superoxide Dismutases in Fungal Pathogens

Schatzman, S. S., Teka, M., Peterson, R. L., Cabelli, D. E., & Culotta, V. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.040 · Cited by 1 · see citing works

Two classes of extracellular Cu-only SODs for fungal pathogens

Schatzman, S. S., Teka, M., Cabelli, D. E., Cormack, B. P., & Culotta, V. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.264 · Cited by 1 · see citing works

Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense

Gleason, J. E., Galaleldeen, A., Peterson, R. L., Taylor, A. B., Holloway, S. P., Waninger‐Saroni, J., Cormack, B. P., Cabelli, D. E., Hart, P. J., & Culotta, V. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400137111 · Cited by 127 · see citing works

The cryo-EM structure of the S-layer deinoxanthin-binding complex of Deinococcus radiodurans informs properties of its environmental interactions

Farci, D., Haniewicz, P., de Sanctis, D., Iesu, L., Kereı̈che, S., Winterhalter, M., & Piano, D. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148720

The Phylogeny and Active Site Design of Eukaryotic Copper-only Superoxide Dismutases

Peterson, R. L., Galaleldeen, A., Villarreal, J., Taylor, A. B., Cabelli, D. E., Hart, P. J., & Culotta, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.748251 · Cited by 38 · see citing works