{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T23:40:47Z","timestamp":1776296447687,"version":"3.50.1"},"reference-count":142,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,9,2]],"date-time":"2022-09-02T00:00:00Z","timestamp":1662076800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"RMIT research grants"},{"name":"Biodiem Ltd."}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antibiotics"],"abstract":"<jats:p>Phylogenetically diverse fungal species are an increasing cause of severe disease and mortality. Identification of new targets and development of new fungicidal drugs are required to augment the effectiveness of current chemotherapy and counter increasing resistance in pathogens. Nitroalkenyl benzene derivatives are thiol oxidants and inhibitors of cysteine-based molecules, which show broad biological activity against microorganisms. Nitropropenyl benzodioxole (NPBD), one of the most active antimicrobial derivatives, shows high activity in MIC assays for phylogenetically diverse saprophytic, commensal and parasitic fungi. NPBD was fungicidal to all species except the dermatophytic fungi, with an activity profile comparable to that of Amphotericin B and Miconazole. NPBD showed differing patterns of dynamic kill rates under different growth conditions for Candida albicans and Aspergillus fumigatus and was rapidly fungicidal for non-replicating vegetative forms and microconidia. It did not induce resistant or drug tolerant strains in major pathogens on long term exposure. A literature review highlights the complexity and interactivity of fungal tyrosine phosphate and redox signaling pathways, their differing metabolic effects in fungal species and identifies some targets for inhibition. A comparison of the metabolic activities of Amphotericin B, Miconazole and NPBD highlights the multiple cellular functions of these agents and the complementarity of many mechanisms. The activity profile of NPBD illustrates the functional diversity of fungal tyrosine phosphatases and thiol-based redox active molecules and contributes to the validation of tyrosine phosphatases and redox thiol molecules as related and complementary selective targets for antimicrobial drug development. NPBD is a selective antifungal agent with low oral toxicity which would be suitable for local treatment of skin and mucosal infections.<\/jats:p>","DOI":"10.3390\/antibiotics11091188","type":"journal-article","created":{"date-parts":[[2022,9,5]],"date-time":"2022-09-05T20:48:25Z","timestamp":1662410905000},"page":"1188","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["The Anti-Fungal Activity of Nitropropenyl Benzodioxole (NPBD), a Redox-Thiol Oxidant and Tyrosine Phosphatase Inhibitor"],"prefix":"10.3390","volume":"11","author":[{"given":"Gina","family":"Nicoletti","sequence":"first","affiliation":[{"name":"STEM College, RMIT University, Melbourne, VIC 3001, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1963-6140","authenticated-orcid":false,"given":"Kylie","family":"White","sequence":"additional","affiliation":[{"name":"STEM College, RMIT University, Melbourne, VIC 3001, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,9,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2732","DOI":"10.1016\/j.febslet.2012.05.008","article-title":"The human phosphatase interactome: An intricate family portrait","volume":"586","author":"Sacco","year":"2012","journal-title":"FEBS Lett."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1111\/febs.12077","article-title":"Protein tyrosine phosphatases\u2014From housekeeping enzymes to master regulators of signal transduction","volume":"280","author":"Tonks","year":"2013","journal-title":"FEBS J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1944","DOI":"10.1111\/febs.12224","article-title":"Redox regulation of protein kinases","volume":"280","author":"Corcoran","year":"2013","journal-title":"FEBS J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1093\/jb\/mvz085","article-title":"Redox regulation of tyrosine kinase signalling: More than meets the eye","volume":"167","author":"Dustin","year":"2020","journal-title":"J. Biochem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.copbio.2016.06.005","article-title":"Cell signaling regulation by protein phosphorylation: A multivariate, heterogeneous, and context-dependent process","volume":"40","author":"Day","year":"2016","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1002\/msb.201304521","article-title":"Evolution and functional cross-talk of protein post-translational modifications","volume":"9","author":"Beltrao","year":"2013","journal-title":"Mol. Syst. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1093\/mmy\/myv098","article-title":"Regulatory roles of phosphorylation in model and pathogenic fungi","volume":"54","author":"Albataineh","year":"2015","journal-title":"Med. Mycol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/nrmicro1578","article-title":"Sensing the environment: Lessons from fungi","volume":"5","author":"Bahn","year":"2007","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1126\/science.aaf2144","article-title":"Evolution of protein phosphorylation across 18 fungal species","volume":"354","author":"Studer","year":"2016","journal-title":"Science"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1111\/nph.13374","article-title":"Functional analysis of the Fusarium graminearum phosphatome","volume":"207","author":"Yun","year":"2015","journal-title":"New Phytol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4212","DOI":"10.1038\/s41467-020-18028-0","article-title":"Genome-wide functional analysis of phosphatases in the pathogenic fungus Cryptococcus neoformans","volume":"11","author":"Jin","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1534\/g3.115.016766","article-title":"Systematic Global Analysis of Genes Encoding Protein Phosphatases in Aspergillus fumigatus","volume":"5","author":"Dolan","year":"2015","journal-title":"G3 Genes Genomes Genet."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1128\/EC.00011-15","article-title":"Analysis of the Candida albicans Phosphoproteome","volume":"14","author":"Willger","year":"2015","journal-title":"Eukaryot. Cell"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Zhao, Z., Jin, Q., Xu, J.-R., and Liu, H. (2014). Identification of a Fungi-Specific Lineage of Protein Kinases Closely Related to Tyrosine Kinases. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0089813"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Gonz\u00e1lez-Rubio, G., Fern\u00e1ndez-Acero, T., Mart\u00edn, H., and Molina, M. (2019). Mitogen-Activated Protein Kinase Phosphatases (MKPs) in Fungal Signaling: Conservation, Function, and Regulation. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20071709"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.mib.2010.09.001","article-title":"Regulation of cross-talk in yeast MAPK signaling pathways","volume":"13","author":"Saito","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1128\/MMBR.00031-10","article-title":"Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases","volume":"75","author":"Cargnello","year":"2011","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.idc.2015.10.014","article-title":"Update from the Laboratory: Clinical Identification and Susceptibility Testing of Fungi and Trends in Antifungal Resistance","volume":"30","author":"Albataineh","year":"2016","journal-title":"Infect. Dis. Clin. N. Am."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Mohanta, T.K., Mohanta, N., Parida, P., Panda, S.K., Ponpandian, L.N., and Bae, H. (2016). Genome-Wide Identification of Mitogen-Activated Protein Kinase Gene Family across Fungal Lineage Shows Presence of Novel and Diverse Activation Loop Motifs. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0149861"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1089\/ars.2010.3611","article-title":"Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects","volume":"15","author":"Tanner","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.freeradbiomed.2015.03.022","article-title":"The cysteine proteome","volume":"84","author":"Go","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1146\/annurev-biochem-061516-045037","article-title":"Oxidative Stress","volume":"86","author":"Sies","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.freeradbiomed.2019.05.035","article-title":"The role of thiols in antioxidant systems","volume":"140","author":"Ulrich","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1089\/ars.2010.3376","article-title":"Cysteine-Based Redox Switches in Enzymes","volume":"14","author":"Klomsiri","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1021\/cr300163e","article-title":"Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery","volume":"113","author":"Paulsen","year":"2013","journal-title":"Chem. Rev."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3344","DOI":"10.1016\/j.csbj.2020.10.024","article-title":"Reactive oxygen species: A generalist in regulating development and pathogenicity of phytopathogenic fungi","volume":"18","author":"Zhang","year":"2020","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"318","DOI":"10.3390\/biom5020318","article-title":"Oxidative Stress in Fungi: Its Function in Signal Transduction, Interaction with Plant Hosts, and Lignocellulose Degradation","volume":"5","author":"Breitenbach","year":"2015","journal-title":"Biomolecules"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"4995","DOI":"10.1007\/s00253-018-9033-2","article-title":"Antioxidant enzymes and their contributions to biological control potential of fungal insect pathogens","volume":"102","author":"Zhang","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"567","DOI":"10.3389\/fmicb.2019.00567","article-title":"Oxidant-Sensing Pathways in the Responses of Fungal Pathogens to Chemical Stress Signals","volume":"10","author":"Simaan","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1134\/S0003683807050031","article-title":"Reactive oxygen species and the strategy of antioxidant defense in fungi: A review","volume":"43","author":"Belozerskaya","year":"2007","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2021.03.040","article-title":"Kinetic assessment of Michael addition reactions of alpha, beta-unsaturated carbonyl compounds to amino acid and protein thiols","volume":"169","author":"Sauerland","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1021\/acs.jmedchem.6b00788","article-title":"Covalent Modifiers: A Chemical Perspective on the Reactivity of \u03b1,\u03b2-Unsaturated Carbonyls with Thiols via Hetero-Michael Addition Reactions","volume":"60","author":"Jackson","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2365","DOI":"10.1021\/jo00034a032","article-title":"Kinetics of reversible thiolate ion addition to substituted b-nitrostyrenes in water. Radicaloid transition state or principle of nonperfect synchronization?","volume":"57","author":"Bernasconi","year":"1992","journal-title":"J. Org. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1038\/aps.2014.80","article-title":"Protein tyrosine phosphatases as potential therapeutic targets","volume":"35","author":"He","year":"2014","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.2174\/138161210791209027","article-title":"Targeting Protein Tyrosine Phosphatases for Anticancer Drug Discovery","volume":"16","author":"Scott","year":"2010","journal-title":"Curr. Pharm. Des."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1080\/14789450.2020.1704260","article-title":"The clinical potential of thiol redox proteomics","volume":"17","author":"Sheehan","year":"2020","journal-title":"Expert Rev. Proteom."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.cbpa.2010.10.016","article-title":"Redox platforms in cancer drug discovery and development","volume":"15","author":"Tew","year":"2011","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"179","DOI":"10.2174\/2211352511311020012","article-title":"Synthesis and antimicrobial activity of nitroalkenyl arenes","volume":"11","author":"Nicoletti","year":"2013","journal-title":"Anti-Infect. Agents"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"White, K., Nicoletti, G., and Cornell, H. (2021). Antibacterial Profile of a Microbicidal Agent Targeting Tyrosine Phosphatases and Redox Thiols, Novel Drug Targets. Antibiotics, 10.","DOI":"10.3390\/antibiotics10111310"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1124\/mol.63.5.1117","article-title":"Potent Inhibition of Human Telomerase by Nitrostyrene Derivatives","volume":"63","author":"Kim","year":"2003","journal-title":"Mol. Pharmacol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.bcp.2007.06.001","article-title":"Synthesis and pharmacological evaluation of novel \u03b2-nitrostyrene derivatives as tyrosine kinase inhibitors with potent antiplatelet activity","volume":"74","author":"Wang","year":"2007","journal-title":"Biochem. Pharmacol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/S0006-2952(02)01618-0","article-title":"Structure activity analysis of the pro-apoptotic, antitumor effect of nitrostyrene adducts and related compounds","volume":"65","author":"Kaap","year":"2003","journal-title":"Biochem. Pharmacol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"6606","DOI":"10.1016\/j.bmc.2009.07.076","article-title":"E-Combretastatin and E-resveratrol structural modifications: Antimicrobial and cancer cell growth inhibitory \u03b2-E-nitrostyrenes","volume":"17","author":"Pettit","year":"2009","journal-title":"Bioorganic Med. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Alfarisi, S., Santoso, M., Kristanti, A.N., Siswanto, I., and Puspaningsih, N.N.T. (2020). Synthesis, Antimicrobial Study, and Molecular Docking Simulation of 3,4-Dimethoxy-\u03b2-Nitrostyrene Derivatives as Candidate PTP1B Inhibitor. Sci. Pharm., 88.","DOI":"10.3390\/scipharm88030037"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"15014","DOI":"10.1021\/bi0486233","article-title":"trans-\u03b2-nitrostyrene derivatives as slow-binding inhibitors of protein tyrosine phosphatases","volume":"43","author":"Park","year":"2004","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2174\/1874104501408010001","article-title":"Nitropropenyl benzodioxole, an anti-infective agent with action as a protein tyrosine phosphatase inhibitor","volume":"8","author":"White","year":"2014","journal-title":"Open Med. Chem. J."},{"key":"ref_47","unstructured":"Nicoletti, A., and White, K. (2008). Protein Tyrosine Phosphatase Modulators. (WO\/2008\/061308), Patent."},{"key":"ref_48","unstructured":"White, K.S. (2008). The Antimicrobial Mechanism of Action of 3,4-methylenedioxy-b-nitropropene. [Ph.D. Thesis, RMIT University]."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4078","DOI":"10.1016\/j.bmc.2006.02.006","article-title":"\u03b2-Nitrostyrene derivatives as potential antibacterial agents: A structure\u2013property\u2013activity relationship study","volume":"14","author":"Milhazes","year":"2006","journal-title":"Bioorganic Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"380","DOI":"10.3390\/app4030380","article-title":"Comparisons of halogenated \u03b2-nitrostyrenes as antimicrobial agents","volume":"4","author":"Cornell","year":"2014","journal-title":"Appl. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Boysen, J.M., Saeed, N., Wolf, T., Panagiotou, G., and Hillmann, F. (2021). The Peroxiredoxin Asp f3 Acts as Redox Sensor in Aspergillus fumigatus. Genes, 12.","DOI":"10.3390\/genes12050668"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"648894","DOI":"10.3389\/fmicb.2021.648894","article-title":"The Redox Proteome of Thiol Proteins in the Rice Blast Fungus Magnaporthe oryzae","volume":"12","author":"Zhang","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"a019273","DOI":"10.1101\/cshperspect.a019273","article-title":"The Spectrum of Fungi That Infects Humans","volume":"5","author":"Casadevall","year":"2015","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3389\/fmicb.2017.00036","article-title":"Antifungal Therapy: New Advances in the Understanding and Treatment of Mycosis","volume":"8","author":"Scorzoni","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1128\/AAC.45.1.124-128.2001","article-title":"Studies of In Vitro Activities of Voriconazole and Itraconazole against Aspergillus Hyphae Using Viability Staining","volume":"45","author":"Nagl","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2760","DOI":"10.1128\/AAC.41.12.2760","article-title":"Comparison of in vitro antifungal susceptibilities of conidia and hyphae of filamentous fungi","volume":"41","author":"Guarro","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_57","unstructured":"(2017). Performance Standards for Antifungal Susceptibility Testing of Filamentous Fungi (Standard No. CLSI Standard M61)."},{"key":"ref_58","unstructured":"(2008). Reference Method for Broth Dilution Antifungal Susceptibility Testing of Filamentous Fungi (Standard No. CLSI Standard M38)."},{"key":"ref_59","unstructured":"(2008). Reference Method for Broth Dilution Antifungal Susceptibility Testing of Yeasts (Standard No. CLSI Standard M27)."},{"key":"ref_60","unstructured":"Fothergill, A.W., Cushion, M.T., Collins, M.S., Kirkpatrick, W.R., Najvar, L.K., Patterson, T.F., and Wiederhold, N.P. (2013, January 10\u201313). Antifungal and Antipneumocystis Activity of the Investigational Antimicrobial BDM-I. Proceedings of the 53rd Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC), Denver, Colorado."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Yag\u00fce, P., Gonzalez-Qui\u00f1onez, N., Fern\u00e1nez-Garc\u00eda, G., Alonso-Fern\u00e1ndez, S., and Manteca, A. (2019). Goals and Challenges in Bacterial Phosphoproteomics. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20225678"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2160","DOI":"10.1089\/ars.2013.5731","article-title":"Cellular Biochemistry Methods for Investigating Protein Tyrosine Phosphatases","volume":"20","author":"Stanford","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Moura, M., and Conde, C. (2019). Phosphatases in Mitosis: Roles and Regulation. Biomolecules, 9.","DOI":"10.3390\/biom9020055"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1186\/s12935-020-01304-w","article-title":"The role of CDC25C in cell cycle regulation and clinical cancer therapy: A systematic review","volume":"20","author":"Liu","year":"2020","journal-title":"Cancer Cell Int."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"10060","DOI":"10.1021\/bi0345081","article-title":"Catalytic and Chemical Competence of Regulation of Cdc25 Phosphatase by Oxidation\/Reduction","volume":"42","author":"Sohn","year":"2003","journal-title":"Biochemistry"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2673","DOI":"10.1242\/jcs.201012","article-title":"Re-examining the role of Cdc14 phosphatase in reversal of Cdk phosphorylation during mitotic exit","volume":"130","author":"Powers","year":"2017","journal-title":"J. Cell Sci."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1038\/s41598-019-38579-7","article-title":"Pharmacophore-guided discovery of CDC25 inhibitors causing cell cycle arrest and tumor regression","volume":"9","author":"Kabakci","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1242\/jcs.02820","article-title":"The Cdc14p phosphatase affects late cell-cycle events and morphogenesis in Candida albicans","volume":"119","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Manzano-L\u00f3pez, J., and Monje-Casas, F. (2020). The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21030709"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"2867","DOI":"10.1242\/jcs.074815","article-title":"Cdc14: A highly conserved family of phosphatases with non-conserved functions?","volume":"123","author":"Mocciaro","year":"2010","journal-title":"J. Cell Sci."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"12073","DOI":"10.1038\/s41598-020-68921-3","article-title":"Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: Implications for antifungal development","volume":"10","author":"DeMarco","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"141","DOI":"10.3389\/fcimb.2018.00141","article-title":"The Aspergillus flavus Phosphatase CDC14 Regulates Development, Aflatoxin Biosynthesis and Pathogenicity","volume":"8","author":"Yang","year":"2018","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Altwasser, R., Baldin, C., Weber, J., Guthke, R., Kniemeyer, O., Brakhage, A.A., Linde, J., and Valiante, V. (2015). Network Modeling Reveals Cross Talk of MAP Kinases during Adaptation to Caspofungin Stress in Aspergillus fumigatus. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0136932"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1128\/EC.00193-09","article-title":"Our Paths Might Cross: The Role of the Fungal Cell Wall Integrity Pathway in Stress Response and Cross Talk with Other Stress Response Pathways","volume":"8","author":"Fuchs","year":"2009","journal-title":"Eukaryot. Cell"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.fgb.2018.12.006","article-title":"Differential roles, crosstalk and response to the Antifungal Protein AfpB in the three Mitogen-Activated Protein Kinases (MAPK) pathways of the citrus postharvest pathogen Penicillium digitatum","volume":"124","author":"Garrigues","year":"2019","journal-title":"Fungal Genet. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3389\/fcimb.2019.00261","article-title":"Stress-Activated Protein Kinases in Human Fungal Pathogens","volume":"9","author":"Day","year":"2019","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3389\/fmicb.2015.00325","article-title":"The Aspergillus fumigatus cell wall integrity signaling pathway: Drug target, compensatory pathways, and virulence","volume":"6","author":"Valiante","year":"2015","journal-title":"Front. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1469-0691.2008.02690.x","article-title":"Fungi sensing environmental stress","volume":"15","author":"Arana","year":"2009","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1128\/EC.00069-14","article-title":"Distinct and Redundant Roles of Protein Tyrosine Phosphatases Ptp1 and Ptp2 in Governing the Differentiation and Pathogenicity of Cryptococcus neoformans","volume":"13","author":"Lee","year":"2014","journal-title":"Eukaryot. Cell"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1128\/EC.5.2.347-358.2006","article-title":"The Cek1 and Hog1 Mitogen-Activated Protein Kinases Play Complementary Roles in Cell Wall Biogenesis and Chlamydospore Formation in the Fungal Pathogen Candida albicans","volume":"5","author":"Eisman","year":"2006","journal-title":"Eukaryot. Cell"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"re7","DOI":"10.1126\/scisignal.2005458","article-title":"Hog1: 20 years of discovery and impact","volume":"7","author":"Brewster","year":"2014","journal-title":"Sci. Signal."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Jiang, C., Zhang, X., Liu, H., and Xu, J.-R. (2018). Mitogen-activated protein kinase signaling in plant pathogenic fungi. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006875"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1093\/mmy\/myx027","article-title":"Cpp1 phosphatase mediated signaling crosstalk between Hog1 and Cek1 mitogen-activated protein kinases is involved in the phenotypic transition in Candida albicans","volume":"56","author":"Deng","year":"2018","journal-title":"Med. Mycol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1128\/EC.00218-13","article-title":"Stress Signaling Pathways for the Pathogenicity of Cryptococcus","volume":"12","author":"Bahn","year":"2013","journal-title":"Eukaryot. Cell"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Zheng, D., Zhang, S., Zhou, X., Wang, C., Xiang, P., Zheng, Q., and Xu, J.-R. (2012). The FgHOG1 Pathway Regulates Hyphal Growth, Stress Responses, and Plant Infection in Fusarium graminearum. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0049495"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1099\/mic.0.28571-0","article-title":"Calcineurin, Mpk1 and Hog1 MAPK pathways independently control fludioxonil antifungal sensitivity in Cryptococcus neoformans","volume":"152","author":"Kojima","year":"2006","journal-title":"Microbiology"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1111\/mmi.14179","article-title":"Fungicide resistance toward fludioxonil conferred by overexpression of the phosphatase gene MoPTP2 in Magnaporthe oryzae","volume":"111","author":"Bohnert","year":"2019","journal-title":"Mol. Microbiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.celrep.2012.12.021","article-title":"Fungicidal Drugs Induce a Common Oxidative-Damage Cellular Death Pathway","volume":"3","author":"Belenky","year":"2013","journal-title":"Cell Rep."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1111\/j.1574-6968.2012.02575.x","article-title":"Identification of novel genes conferring altered azole susceptibility in Aspergillus fumigatus","volume":"332","author":"Bowyer","year":"2012","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1093\/jac\/dkt114","article-title":"The role of oxidative and nitrosative bursts caused by azoles and amphotericin B against the fungal pathogen Cryptococcus gattii","volume":"68","author":"Ferreira","year":"2013","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Kim, J.H., Tam, C.C., Chan, K.L., Cheng, L.W., Land, K.M., Friedman, M., and Chang, P.-K. (2021). Antifungal Efficacy of Redox-Active Natamycin against Some Foodborne Fungi\u2014Comparison with Aspergillus fumigatus. Foods, 10.","DOI":"10.3390\/foods10092073"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"6627","DOI":"10.1128\/AAC.03570-14","article-title":"The Production of Reactive Oxygen Species Is a Universal Action Mechanism of Amphotericin B against Pathogenic Yeasts and Contributes to the Fungicidal Effect of This Drug","volume":"58","author":"Casas","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"e00978-00917","DOI":"10.1128\/AAC.00978-17","article-title":"Induction of Mitochondrial Reactive Oxygen Species Production by Itraconazole, Terbinafine, and Amphotericin B as a Mode of Action against Aspergillus fumigatus","volume":"61","author":"Shekhova","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/s41579-019-0322-2","article-title":"Drug resistance and tolerance in fungi","volume":"18","author":"Berman","year":"2020","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1128\/CMR.17.2.268-280.2004","article-title":"Determination of Fungicidal Activities against Yeasts and Molds: Lessons Learned from Bactericidal Testing and the Need for Standardization","volume":"17","author":"Pfaller","year":"2004","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1128\/AAC.48.7.2477-2482.2004","article-title":"Patterns of Amphotericin B Killing Kinetics against Seven Candida Species","volume":"48","author":"Gobernado","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1128\/AAC.42.5.1207","article-title":"Influence of Test Conditions on Antifungal Time-Kill Curve Results: Proposal for Standardized Methods","volume":"42","author":"Klepser","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1128\/AAC.47.4.1200-1206.2003","article-title":"Sublethal Injury and Resuscitation of Candida albicans after Amphotericin B Treatment","volume":"47","author":"Liao","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_99","first-page":"594","article-title":"The evaluation of in vitro pharmacodynamic properties of amphotericin B, voriconazole and caspofungin against A. fumigatus isolates by the conventional and colorimetric time-kill assays","volume":"49","author":"Kiraz","year":"2011","journal-title":"Med. Mycol."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"McDonagh, A., Fedorova, N.D., Crabtree, J., Yu, Y., Kim, S., Chen, D., Loss, O., Cairns, T., Goldman, G., and Armstrong-James, D. (2008). Sub-Telomere Directed Gene Expression during Initiation of Invasive Aspergillosis. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000154"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Kwon-Chung, K.J., and Sugui, J.A. (2013). Aspergillus fumigatus\u2014What Makes the Species a Ubiquitous Human Fungal Pathogen?. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003743"},{"key":"ref_102","first-page":"9870679","article-title":"Antifungal Resistance, Metabolic Routes as Drug Targets, and New Antifungal Agents: An Overview about Endemic Dimorphic Fungi","volume":"2017","author":"Amaral","year":"2017","journal-title":"Mediat. Inflamm."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Vincent, B.M., Lancaster, A.K., Scherz-Shouval, R., Whitesell, L., and Lindquist, S. (2013). Fitness Trade-offs Restrict the Evolution of Resistance to Amphotericin B. PLoS Biol., 11.","DOI":"10.1371\/journal.pbio.1001692"},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Wuyts, J., Van Dijck, P., and Holtappels, M. (2018). Fungal persister cells: The basis for recalcitrant infections?. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1007301"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e00670-00617","DOI":"10.1128\/AAC.00670-17","article-title":"Oxidative Stress Response Tips the Balance in Aspergillus terreus Amphotericin B Resistance","volume":"61","author":"Jukic","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1128\/AAC.39.8.1779","article-title":"Antagonistic interactions between azoles and amphotericin B with yeasts depend on azole lipophilia for special test conditions in vitro","volume":"39","author":"Scheven","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1093\/jac\/dkl384","article-title":"In vitro activity and synergism of amphotericin B, azoles and cationic antimicrobials against the emerging pathogen Trichoderma spp.","volume":"58","author":"Kratzer","year":"2006","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1093\/mmy\/myy009","article-title":"In vitro activity of amphotericin B-azole combinations against Malassezia pachydermatis strains","volume":"57","author":"Blanco","year":"2019","journal-title":"Med. Mycol."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Chudzik, B., Bonio, K., Dabrowski, W., Pietrzak, D., Niewiadomy, A., Olender, A., Pawlikowska-Pawl\u0119ga, B., and Gago\u015b, M. (2019). Antifungal effects of a 1,3,4-thiadiazole derivative determined by cytochemical and vibrational spectroscopic studies. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0222775"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1093\/femsre\/fuw003","article-title":"Exploring the diversity of protein modifications: Special bacterial phosphorylation systems","volume":"40","author":"Mijakovic","year":"2016","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1111\/myc.12620","article-title":"New insights on the antibacterial efficacy of miconazole in vitro","volume":"60","author":"Nenoff","year":"2017","journal-title":"Mycoses"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1820","DOI":"10.1017\/S0031182018000562","article-title":"CYP51 as drug targets for fungi and protozoan parasites: Past, present and future","volume":"145","author":"Lepesheva","year":"2018","journal-title":"Parasitology"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.micinf.2011.01.015","article-title":"Amphotericin B mediates killing in Cryptococcus neoformans through the induction of a strong oxidative burst","volume":"13","author":"Scorzoni","year":"2011","journal-title":"Microbes Infect."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3113","DOI":"10.1128\/AAC.46.10.3113-3117.2002","article-title":"Endogenous Reactive Oxygen Species Is an Important Mediator of Miconazole Antifungal Effect","volume":"46","author":"Kobayashi","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s12154-017-0172-1","article-title":"Amphotericin B potentiates the anticancer activity of doxorubicin on the MCF-7 breast cancer cells","volume":"10","author":"Tavangar","year":"2017","journal-title":"J. Chem. Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1006\/taap.2002.9352","article-title":"Antitumor Effects of Miconazole on Human Colon Carcinoma Xenografts in Nude Mice through Induction of Apoptosis and G0\/G1 Cell Cycle Arrest","volume":"180","author":"Wu","year":"2002","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_117","first-page":"290","article-title":"Miconazole triggers various forms of cell death in human breast cancer MDA-MB-231 cells","volume":"74","author":"Chengzhu","year":"2019","journal-title":"Die Pharm.-Int. J. Pharm. Sci."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1093\/jnci\/82.13.1107","article-title":"New Colorimetric Cytotoxicity Assay for Anticancer-Drug Screening","volume":"82","author":"Skehan","year":"1990","journal-title":"JNCI J. Natl. Cancer Inst."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"479712","DOI":"10.1155\/2012\/479712","article-title":"Osteosarcoma Phenotype Is Inhibited by 3,4-Methylenedioxy-\u03b2-nitrostyrene","volume":"2012","author":"Messerschmitt","year":"2012","journal-title":"Sarcoma"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.canlet.2015.11.035","article-title":"The synthetic \u03b2-nitrostyrene derivative CYT-Rx20 induces breast cancer cell death and autophagy via ROS-mediated MEK\/ERK pathway","volume":"371","author":"Hung","year":"2016","journal-title":"Cancer Lett."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.lfs.2016.12.009","article-title":"3\u2032-Hydroxy-4\u2032-methoxy-\u03b2-methyl-\u03b2-nitrostyrene inhibits tumor growth through ROS generation and GSH depletion in lung cancer cells","volume":"172","author":"Tsai","year":"2017","journal-title":"Life Sci."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Chiu, W.-C., Lee, Y.-C., Su, Y.-H., Wang, Y.-Y., Tsai, C.-H., Hou, Y.-A., Wang, C.-H., Huang, Y.-F., Huang, C.-J., and Chou, S.-H. (2016). The Synthetic \u03b2-Nitrostyrene Derivative CYT-Rx20 Inhibits Esophageal Tumor Growth and Metastasis via PI3K\/AKT and STAT3 Pathways. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0166453"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"10964","DOI":"10.1021\/acscatal.8b03401","article-title":"Mechanisms of Cytochrome P450-Catalyzed Oxidations","volume":"8","author":"Guengerich","year":"2018","journal-title":"ACS Catal."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/s10059-011-0276-3","article-title":"Regulation of reactive oxygen species generation in cell signaling","volume":"32","author":"Bae","year":"2011","journal-title":"Mol. Cells"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.bbapap.2010.06.020","article-title":"Cytochrome P450 enzymes in the fungal kingdom","volume":"1814","year":"2011","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1093\/gbe\/evu132","article-title":"Fungal Cytochrome P450 Monooxygenases: Their Distribution, Structure, Functions, Family Expansion, and Evolutionary Origin","volume":"6","author":"Chen","year":"2014","journal-title":"Genome Biol. Evol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1248\/bpb.28.1805","article-title":"Effect of Antifungal Drugs on Cytochrome P450 (CYP) 2C9, CYP2C19, and CYP3A4 Activities in Human Liver Microsomes","volume":"28","author":"Niwa","year":"2005","journal-title":"Biol. Pharm. Bull."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1248\/bpb.28.1813","article-title":"Effect of Antifungal Drugs on Cytochrome P450 (CYP) 1A2, CYP2D6, and CYP2E1 Activities in Human Liver Microsomes","volume":"28","author":"Niwa","year":"2005","journal-title":"Biol. Pharm. Bull."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1124\/dmd.106.012633","article-title":"Mechanism-Based Inactivation of Human Cytochrome P450 Enzymes and the Prediction of Drug-Drug Interactions","volume":"35","author":"Obach","year":"2007","journal-title":"Drug Metab. Dispos."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1124\/dmd.32.6.647","article-title":"Validated assays for human cytochrome P450 activities","volume":"32","author":"Walsky","year":"2004","journal-title":"Drug Metab. Dispos."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1007\/s40265-013-0069-4","article-title":"Amphotericin B Formulations: A Comparative Review of Efficacy and Toxicity","volume":"73","author":"Hamill","year":"2013","journal-title":"Drugs"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"265","DOI":"10.2217\/17460913.3.3.265","article-title":"Miconazole revisited: New evidence of antifungal efficacy from laboratory and clinical trials","volume":"3","author":"Barasch","year":"2008","journal-title":"Future Microbiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/ja.2010.80","article-title":"A newly identified derivative of amphotericin B: Isolation, structure determination and primary evaluation of the activity and toxicity","volume":"63","author":"Wang","year":"2010","journal-title":"J. Antibiot."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1093\/toxsci\/kfr347","article-title":"Antifungal Miconazole Induces Cardiotoxicity Via Inhibition of APE\/Ref-1-Related Pathway in Rat Neonatal Cardiomyocytes","volume":"126","author":"Won","year":"2012","journal-title":"Toxicol. Sci."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1038\/sj.bjp.0706095","article-title":"Blockade of HERG cardiac K+ current by antifungal drug miconazole","volume":"144","author":"Kikuchi","year":"2005","journal-title":"Br. J. Pharmacol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1128\/AAC.35.4.615","article-title":"Amphotericin B lipid complex therapy of experimental fungal infections in mice","volume":"35","author":"Clark","year":"1991","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Bahn, Y.-S. (2015). Exploiting Fungal Virulence-Regulating Transcription Factors As Novel Antifungal Drug Targets. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004936"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"S474","DOI":"10.1093\/infdis\/jix130","article-title":"Novel Agents and Drug Targets to Meet the Challenges of Resistant Fungi","volume":"216","author":"McCarthy","year":"2017","journal-title":"J. Infect. Dis."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"e02281-18","DOI":"10.1128\/AAC.02281-18","article-title":"Structure, mechanism, and inhibition of Aspergillus fumigatus thioredoxin reductase","volume":"63","author":"Marshall","year":"2019","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_140","first-page":"e01719-20","article-title":"The Future of Antifungal Drug Therapy: Novel Compounds and Targets","volume":"20","author":"Dasilva","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"3013","DOI":"10.1089\/ars.2009.2541","article-title":"Redox-Directed Cancer Therapeutics: Molecular Mechanisms and Opportunities","volume":"11","author":"Wondrak","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Narayanan, D., Ma, S., and \u00d6zcelik, D. (2020). Targeting the Redox Landscape in Cancer Therapy. Cancers, 12.","DOI":"10.3390\/cancers12071706"}],"container-title":["Antibiotics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-6382\/11\/9\/1188\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:22:21Z","timestamp":1760142141000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-6382\/11\/9\/1188"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,2]]},"references-count":142,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["antibiotics11091188"],"URL":"https:\/\/doi.org\/10.3390\/antibiotics11091188","relation":{},"ISSN":["2079-6382"],"issn-type":[{"value":"2079-6382","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,2]]}}}