{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T13:06:22Z","timestamp":1790255182884,"version":"4.1.0"},"reference-count":71,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T00:00:00Z","timestamp":1785024000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100013076","name":"National Major Science and Technology Projects of China","doi-asserted-by":"publisher","award":["2026ZD1218801"],"award-info":[{"award-number":["2026ZD1218801"]}],"id":[{"id":"10.13039\/501100013076","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Therapy Oncology"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.omton.2026.201310","type":"journal-article","created":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T23:35:21Z","timestamp":1785195321000},"page":"201310","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Engineered indoleamine 2,3-dioxygenase variant: Oxidative activation of prodrug indole-3-acetic acid against cancer cells for targeted therapy"],"prefix":"10.1016","volume":"34","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-5786-8077","authenticated-orcid":false,"given":"Liru","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanfang","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1097-7283","authenticated-orcid":false,"given":"Sheng","family":"Ye","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.omton.2026.201310_bib1","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.jconrel.2015.09.067","article-title":"Novel delivery approaches for cancer therapeutics","volume":"219","author":"Mitra","year":"2015","journal-title":"J. Control. Release"},{"key":"10.1016\/j.omton.2026.201310_bib2","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.ejmech.2016.10.061","article-title":"Prodrug approach: An overview of recent cases","volume":"127","author":"Abet","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib3","doi-asserted-by":"crossref","first-page":"342","DOI":"10.2174\/187231309787158271","article-title":"Reactive oxygen species, cancer and anti-cancer therapies","volume":"3","author":"Manda","year":"2009","journal-title":"Curr. Chem. Biol."},{"key":"10.1016\/j.omton.2026.201310_bib4","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/nrd2803","article-title":"Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?","volume":"8","author":"Trachootham","year":"2009","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.omton.2026.201310_bib5","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.2174\/1381612023394610","article-title":"Indole-3-acetic acids and horseradish peroxidase: a new prodrug\/enzyme combination for targeted cancer therapy","volume":"8","author":"Wardman","year":"2002","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.omton.2026.201310_bib6","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1007\/s00253-014-6346-7","article-title":"An updated view on horseradish peroxidases: recombinant production and biotechnological applications","volume":"99","author":"Krainer","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.omton.2026.201310_bib7","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1038\/sj.cgt.7700258","article-title":"Development of a novel enzyme\/prodrug combination for gene therapy of cancer: horseradish peroxidase\/indole-3-acetic acid","volume":"7","author":"Greco","year":"2000","journal-title":"Cancer Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib8","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0898-6568(03)00091-3","article-title":"Oxidation of indole-3-acetic acid by horseradish peroxidase induces apoptosis in G361 human melanoma cells","volume":"16","author":"Kim","year":"2004","journal-title":"Cell. Signal."},{"key":"10.1016\/j.omton.2026.201310_bib9","doi-asserted-by":"crossref","first-page":"4519","DOI":"10.3748\/wjg.v11.i29.4519","article-title":"Apoptosis of pancreatic cancer BXPC-3 cells induced by indole-3-acetic acid in combination with horseradish peroxidase","volume":"11","author":"Huang","year":"2005","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.omton.2026.201310_bib10","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/cgt.2009.86","article-title":"In vivo characterization of horseradish peroxidase with indole-3-acetic acid and 5-bromoindole-3-acetic acid for gene therapy of cancer","volume":"17","author":"Tupper","year":"2010","journal-title":"Cancer Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib11","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/s10529-014-1664-5","article-title":"Horseradish peroxidase-encapsulated chitosan nanoparticles for enzyme-prodrug cancer therapy","volume":"37","author":"Cao","year":"2015","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.omton.2026.201310_bib12","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1002\/cam4.668","article-title":"Recombinant horseradish peroxidase variants for targeted cancer treatment","volume":"5","author":"Bonifert","year":"2016","journal-title":"Cancer Med."},{"key":"10.1016\/j.omton.2026.201310_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2021.112037","article-title":"Potential of unglycosylated horseradish peroxidase variants for enzyme prodrug cancer therapy","volume":"142","author":"Humer","year":"2021","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.omton.2026.201310_bib14","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1007\/s00706-021-02848-x","article-title":"Enzyme prodrug therapy: cytotoxic potential of paracetamol turnover with recombinant horseradish peroxidase","volume":"152","author":"Humer","year":"2021","journal-title":"Monatsh. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib15","article-title":"In-vitro and in-vivo efficacy of hollow gold nanoparticles encapsulating horseradish peroxidase: Oxidative stress-mediated tumor cell killing","volume":"79","author":"Gupta","year":"2023","journal-title":"J. Drug Deliv. Sci. Technol."},{"key":"10.1016\/j.omton.2026.201310_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.enzmictec.2021.109889","article-title":"Hyaluronic acid-coated chitosan nanoparticles as carrier for the enzyme\/prodrug complex based on horseradish peroxidase\/indole-3-acetic acid: Characterization and potential therapeutic for bladder cancer cells","volume":"150","author":"Pereira","year":"2021","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.omton.2026.201310_bib17","doi-asserted-by":"crossref","first-page":"409","DOI":"10.2147\/IJN.S323802","article-title":"Horseradish peroxidase-functionalized gold nanoconjugates for breast cancer treatment based on enzyme prodrug therapy","volume":"17","author":"Vivo-Llorca","year":"2022","journal-title":"Int. J. Nanomed."},{"key":"10.1016\/j.omton.2026.201310_bib18","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/cgt.2011.65","article-title":"Tumor-targeted gene therapy using Adv-AFP-HRPC\/IAA prodrug system suppresses growth of hepatoma xenografted in mice","volume":"19","author":"Dai","year":"2012","journal-title":"Cancer Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib19","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1016\/j.leukres.2010.11.025","article-title":"Antibody-targeted horseradish peroxidase associated with indole-3-acetic acid induces apoptosis in vitro in hematological malignancies","volume":"35","author":"Dalmazzo","year":"2011","journal-title":"Leuk. Res."},{"key":"10.1016\/j.omton.2026.201310_bib20","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1038\/sj.cgt.7700713","article-title":"Analysis of the horseradish peroxidase\/indole-3-acetic acid combination in a three-dimensional tumor model","volume":"11","author":"Tupper","year":"2004","journal-title":"Cancer Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib21","doi-asserted-by":"crossref","first-page":"122","DOI":"10.31083\/ph.2010.9715","article-title":"Indole-3-acetic acid\/horseradish peroxidase induces apoptosis in TCCSUP human urinary bladder carcinoma cells","volume":"65","author":"Jeong","year":"2010","journal-title":"Pharmazie"},{"key":"10.1016\/j.omton.2026.201310_bib22","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1093\/clinchem\/29.7.1354","article-title":"Liquid-chromatographic determination of indole-3-acetic acid and 5-hydroxyindole-3-acetic acid in human plasma","volume":"29","author":"Mart\u00ednez","year":"1983","journal-title":"Clin. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib23","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1002\/jcb.10292","article-title":"Mechanisms of cytotoxicity induced by horseradish peroxidase\/indole-3-acetic acid gene therapy","volume":"87","author":"Greco","year":"2002","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.omton.2026.201310_bib24","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.febslet.2006.01.073","article-title":"Hydrogen peroxide is a mediator of indole-3-acetic acid\/horseradish peroxidase-induced apoptosis","volume":"580","author":"Kim","year":"2006","journal-title":"FEBS Lett."},{"key":"10.1016\/j.omton.2026.201310_bib25","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1248\/bpb.29.1625","article-title":"Indole-3-acetic acid\/horseradish peroxidase-induced apoptosis involves cell surface CD95 (Fas\/APO-1) expression","volume":"29","author":"Kim","year":"2006","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.omton.2026.201310_bib26","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0014-5793(76)80804-6","article-title":"Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11. 1.7)","volume":"72","author":"Welinder","year":"1976","journal-title":"FEBS Lett."},{"key":"10.1016\/j.omton.2026.201310_bib27","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/0006-291X(78)91350-5","article-title":"Calcium-related properties of horseradish peroxidase","volume":"80","author":"Haschke","year":"1978","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.omton.2026.201310_bib28","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.3389\/fimmu.2020.01185","article-title":"Immunosuppressive IDO in cancer: mechanisms of action, animal models, and targeting strategies","volume":"11","author":"Zhai","year":"2020","journal-title":"Front. Immunol."},{"key":"10.1016\/j.omton.2026.201310_bib29","doi-asserted-by":"crossref","first-page":"2771","DOI":"10.7150\/jca.31727","article-title":"Role of IDO and TDO in cancers and related diseases and the therapeutic implications","volume":"10","author":"Ye","year":"2019","journal-title":"J. Cancer"},{"key":"10.1016\/j.omton.2026.201310_bib30","doi-asserted-by":"crossref","first-page":"4700","DOI":"10.1016\/S0021-9258(17)30447-7","article-title":"Indoleamine 2, 3-dioxygenase. Purification and some properties","volume":"253","author":"Shimizu","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib31","doi-asserted-by":"crossref","first-page":"13966","DOI":"10.1073\/pnas.1207191109","article-title":"Indole peroxygenase activity of indoleamine 2, 3-dioxygenase","volume":"109","author":"Kuo","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.omton.2026.201310_bib32","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1074\/jbc.M112.410993","article-title":"Human indoleamine 2, 3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide","volume":"288","author":"Freewan","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib33","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.omton.2026.201310_bib34","first-page":"702","article-title":"The choice of prodrugs for gene directed enzyme prodrug therapy of cancer","volume":"2","author":"Connors","year":"1995","journal-title":"Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib35","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1172\/JCI10001","article-title":"Prodrug-activating systems in suicide gene therapy","volume":"105","author":"Springer","year":"2000","journal-title":"J. Clin. Investig."},{"key":"10.1016\/j.omton.2026.201310_bib36","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1080\/00224561.2000.12436384","article-title":"Adoption of conservation production systems in three Midwest watersheds","volume":"55","author":"Napier","year":"2000","journal-title":"J. Soil Water Conserv."},{"key":"10.1016\/j.omton.2026.201310_bib37","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1002\/1097-4652(2001)9999:9999<::AID-JCP1060>3.0.CO;2-H","article-title":"Gene directed enzyme\/prodrug therapy of cancer: historical appraisal and future prospectives","volume":"187","author":"Greco","year":"2001","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.omton.2026.201310_bib38","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.it.2012.10.001","article-title":"Indoleamine 2, 3 dioxygenase and metabolic control of immune responses","volume":"34","author":"Munn","year":"2013","journal-title":"Trends Immunol."},{"key":"10.1016\/j.omton.2026.201310_bib39","doi-asserted-by":"crossref","first-page":"3249","DOI":"10.1073\/pnas.1719190115","article-title":"Immune-modulating enzyme indoleamine 2, 3-dioxygenase is effectively inhibited by targeting its apo-form","volume":"115","author":"Nelp","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.omton.2026.201310_bib40","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1084\/jem.189.9.1363","article-title":"Inhibition of T cell proliferation by macrophage tryptophan catabolism","volume":"189","author":"Munn","year":"1999","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.omton.2026.201310_bib41","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/nm1196","article-title":"Inhibition of indoleamine 2, 3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy","volume":"11","author":"Muller","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.omton.2026.201310_bib42","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.it.2016.01.002","article-title":"IDO in the tumor microenvironment: inflammation, counter-regulation, and tolerance","volume":"37","author":"Munn","year":"2016","journal-title":"Trends Immunol."},{"key":"10.1016\/j.omton.2026.201310_bib43","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1038\/nm934","article-title":"Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2, 3-dioxygenase","volume":"9","author":"Uyttenhove","year":"2003","journal-title":"Nat. Med."},{"key":"10.1016\/j.omton.2026.201310_bib44","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1186\/s13045-018-0644-y","article-title":"Targeting the IDO1 pathway in cancer: from bench to bedside","volume":"11","author":"Liu","year":"2018","journal-title":"J. Hematol. Oncol."},{"key":"10.1016\/j.omton.2026.201310_bib45","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.addr.2011.02.002","article-title":"Prodrugs for improving tumor targetability and efficiency","volume":"63","author":"Mahato","year":"2011","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.omton.2026.201310_bib46","first-page":"151","article-title":"Horseradish peroxidase-mediated gene therapy: choice of prodrugs in oxic and anoxic tumor conditions","volume":"1","author":"Greco","year":"2001","journal-title":"Mol. Cancer Therapeut."},{"key":"10.1016\/j.omton.2026.201310_bib47","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0006-2952(00)00498-6","article-title":"Oxidative activation of indole-3-acetic acids to cytotoxic species\u2014a potential new role for plant auxins in cancer therapy","volume":"61","author":"Folkes","year":"2001","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.omton.2026.201310_bib48","doi-asserted-by":"crossref","first-page":"4517","DOI":"10.3390\/molecules14114517","article-title":"Bystander or no bystander for gene directed enzyme prodrug therapy","volume":"14","author":"Dachs","year":"2009","journal-title":"Molecules"},{"key":"10.1016\/j.omton.2026.201310_bib49","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.jconrel.2011.06.001","article-title":"Targeted drug delivery to tumors: myths, reality and possibility","volume":"153","author":"Bae","year":"2011","journal-title":"J. Control. Release"},{"key":"10.1016\/j.omton.2026.201310_bib50","series-title":"Targeted Drug Delivery","first-page":"155","article-title":"Gene-directed enzyme\u2013prodrug therapy (GDEPT) as a suicide gene therapy modality for cancer treatment","author":"Kharkar","year":"2022"},{"key":"10.1016\/j.omton.2026.201310_bib51","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1016\/S0959-8049(96)00483-2","article-title":"The role of the bystander effect in suicide gene therapy","volume":"33","author":"Pope","year":"1997","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/j.omton.2026.201310_bib52","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1089\/hum.1997.8.15-1807","article-title":"A \u201cdistant\u201d bystander effect of suicide gene therapy: regression of nontransduced tumors together with a distant transduced tumor","volume":"8","author":"Kianmanesh","year":"1997","journal-title":"Hum. Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib53","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1002\/cmdc.200700159","article-title":"Prodrug strategies in anticancer chemotherapy","volume":"3","author":"Kratz","year":"2008","journal-title":"ChemMedChem"},{"key":"10.1016\/j.omton.2026.201310_bib54","doi-asserted-by":"crossref","first-page":"111","DOI":"10.2174\/1874104501812010111","article-title":"Therapeutic potential of prodrugs towards targeted drug delivery","volume":"12","author":"Mishra","year":"2018","journal-title":"Open Med. Chem. J."},{"key":"10.1016\/j.omton.2026.201310_bib55","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1208\/ps020106","article-title":"Targeted prodrug design to optimize drug delivery","volume":"2","author":"Han","year":"2000","journal-title":"AAPS PharmSci"},{"key":"10.1016\/j.omton.2026.201310_bib56","doi-asserted-by":"crossref","first-page":"2977","DOI":"10.1016\/j.bbamcr.2016.09.012","article-title":"Activation of apoptosis signalling pathways by reactive oxygen species","volume":"1863","author":"Redza-Dutordoir","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.omton.2026.201310_bib57","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/s41419-017-0135-z","article-title":"Cellular death, reactive oxygen species (ROS) and diabetic complications","volume":"9","author":"Volpe","year":"2018","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.omton.2026.201310_bib58","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.toxlet.2003.12.067","article-title":"The mechanism of indole acetic acid cytotoxicity","volume":"148","author":"de Melo","year":"2004","journal-title":"Toxicol. Lett."},{"key":"10.1016\/j.omton.2026.201310_bib59","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1080\/09553000110097983","article-title":"Oxic and anoxic enhancement of radiation-mediated toxicity by horseradish peroxidase\/indole-3-acetic acid gene therapy","volume":"78","author":"Greco","year":"2002","journal-title":"Int. J. Radiat. Biol."},{"key":"10.1016\/j.omton.2026.201310_bib60","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0006-2952(01)00868-1","article-title":"5-Fluoroindole-3-acetic acid: a prodrug activated by a peroxidase with potential for use in targeted cancer therapy","volume":"63","author":"Folkes","year":"2002","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.omton.2026.201310_bib61","first-page":"204","article-title":"The triad indole-3-acetic acid ethyl ester\/esterase\/horseradish peroxidase as a new cytotoxic prodrug\/enzyme combination","volume":"30","author":"Pereira","year":"2010","journal-title":"Appl. Cancer. Res."},{"key":"10.1016\/j.omton.2026.201310_bib62","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/s11046-014-9807-8","article-title":"Induction of oxidative stress in Prototheca zopfii by indole-3-acetic acid\/HRP or 2, 4-pentanedione\/HRP systems and their oxidation products","volume":"179","author":"Cunha","year":"2015","journal-title":"Mycopathologia"},{"key":"10.1016\/j.omton.2026.201310_bib63","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1089\/hum.1998.9.6-855","article-title":"Double suicide gene (cytosine deaminase and herpes simplex virus thymidine kinase) but not single gene transfer allows reliable elimination of tumor cells in vivo","volume":"9","author":"Uckert","year":"1998","journal-title":"Hum. Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib64","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1089\/10430340050016166","article-title":"Double suicide gene therapy augments the antitumor activity of a replication-competent lytic adenovirus through enhanced cytotoxicity and radiosensitization","volume":"11","author":"Rogulski","year":"2000","journal-title":"Hum. Gene Ther."},{"key":"10.1016\/j.omton.2026.201310_bib65","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/S0140-6736(97)22001-5","article-title":"Immune system in suicide-gene therapy","volume":"349","author":"Freeman","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.omton.2026.201310_bib66","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.canlet.2009.03.021","article-title":"Radiation enhances suicide gene therapy in radioresistant laryngeal squamous cell carcinoma via activation of a tumor-specific promoter","volume":"283","author":"Liao","year":"2009","journal-title":"Cancer Lett."},{"key":"10.1016\/j.omton.2026.201310_bib67","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1186\/1479-5876-9-39","article-title":"Gene therapy with tumor-specific promoter mediated suicide gene plus IL-12 gene enhanced tumor inhibition and prolonged host survival in a murine model of Lewis lung carcinoma","volume":"9","author":"Xu","year":"2011","journal-title":"J. Transl. Med."},{"key":"10.1016\/j.omton.2026.201310_bib68","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1073\/pnas.0508996103","article-title":"Crystal structure of human indoleamine 2, 3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase","volume":"103","author":"Sugimoto","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.omton.2026.201310_bib69","doi-asserted-by":"crossref","first-page":"9617","DOI":"10.1021\/acs.jmedchem.7b00974","article-title":"Discovery of a novel and selective indoleamine 2, 3-dioxygenase (IDO-1) inhibitor 3-(5-fluoro-1 H-indol-3-yl) pyrrolidine-2, 5-dione (EOS200271\/PF-06840003) and its characterization as a potential clinical candidate","volume":"60","author":"Crosignani","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib70","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1016\/S0021-9258(19)77982-4","article-title":"Mechanism of interferon-gamma action. Characterization of indoleamine 2, 3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity","volume":"263","author":"Takikawa","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.omton.2026.201310_bib71","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1016\/S0360-3016(98)00297-1","article-title":"Toward targeted \u201coxidation therapy\u201d of cancer: peroxidase-catalysed cytotoxicity of indole-3-acetic acids","volume":"42","author":"Folkes","year":"1998","journal-title":"Int. J. Radiat. Oncol. Biol. Phys."}],"container-title":["Molecular Therapy Oncology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2950329926001864?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2950329926001864?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:38:54Z","timestamp":1790253534000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2950329926001864"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":71,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["S2950329926001864"],"URL":"https:\/\/doi.org\/10.1016\/j.omton.2026.201310","relation":{},"ISSN":["2950-3299"],"issn-type":[{"value":"2950-3299","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Engineered indoleamine 2,3-dioxygenase variant: Oxidative activation of prodrug indole-3-acetic acid against cancer cells for targeted therapy","name":"articletitle","label":"Article Title"},{"value":"Molecular Therapy Oncology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.omton.2026.201310","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Published by Elsevier Inc. on behalf of The American Society of Gene and Cell Therapy.","name":"copyright","label":"Copyright"}],"article-number":"201310"}}