{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T14:14:10Z","timestamp":1783606450006,"version":"3.55.0"},"reference-count":221,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Humanidades, Ciencias y Tecnolog\u00edas","doi-asserted-by":"publisher","award":["EM-R A1-S-10743"],"award-info":[{"award-number":["EM-R A1-S-10743"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Humanidades, Ciencias y Tecnolog\u00edas","doi-asserted-by":"publisher","award":["1007737"],"award-info":[{"award-number":["1007737"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Humanidades, Ciencias y Tecnolog\u00edas","doi-asserted-by":"publisher","award":["801406"],"award-info":[{"award-number":["801406"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2025,3]]},"DOI":"10.1016\/j.abb.2025.110321","type":"journal-article","created":{"date-parts":[[2025,1,25]],"date-time":"2025-01-25T23:08:09Z","timestamp":1737846489000},"page":"110321","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Ornithine decarboxylase and its role in cancer"],"prefix":"10.1016","volume":"765","author":[{"given":"Jessica Georgina","family":"Filisola-Villase\u00f1or","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beatriz Irene","family":"Arroyo-S\u00e1nchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Janiel","family":"Navarro-Gonz\u00e1lez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edgar","family":"Morales-R\u00edos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8049-807X","authenticated-orcid":false,"given":"Viridiana","family":"Olin-Sandoval","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2025.110321_bib1","first-page":"539","article-title":"Polyamines and related signaling pathways in cancer. Cancer Cell","volume":"20","author":"Li","year":"2020","journal-title":"Int."},{"key":"10.1016\/j.abb.2025.110321_bib2","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.canlet.2021.06.020","article-title":"Metabolism and function of polyamines in cancer progression","volume":"519","author":"Sari","year":"2021","journal-title":"Cancer Lett."},{"key":"10.1016\/j.abb.2025.110321_bib3","doi-asserted-by":"crossref","first-page":"14904","DOI":"10.1074\/jbc.R116.731661","article-title":"Functions of polyamines in mammals","volume":"291","author":"Pegg","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib4","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/j.bbagen.2018.06.004","article-title":"The old and new biochemistry of polyamines","volume":"1862","author":"Bae","year":"2018","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.abb.2025.110321_bib5","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.biocel.2018.12.012","article-title":"The functional role of polyamines in eukaryotic cells","volume":"107","author":"Igarashi","year":"2019","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib6","first-page":"44","article-title":"Polyamines: functions, metabolism, and role in human disease management","volume":"9","author":"Sagar","year":"2021","journal-title":"Med. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib7","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/nrc1454","article-title":"Polyamines and cancer: old molecules, new understanding","volume":"4","author":"Gerner","year":"2004","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib8","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/s00425-008-0772-7","article-title":"Polyamines: essential factors for growth and survival","volume":"228","author":"Kusano","year":"2008","journal-title":"Planta"},{"key":"10.1016\/j.abb.2025.110321_bib9","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1016\/j.jmb.2015.06.020","article-title":"Remaining mysteries of molecular biology: the role of polyamines in the cell","volume":"427","author":"Miller-Fleming","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib10","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1038\/s41586-019-1442-6","article-title":"Lysine harvesting is an antioxidant strategy and triggers underground polyamine metabolism","volume":"572","author":"Olin-Sandoval","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.abb.2025.110321_bib11","series-title":"Methods and Protocols","first-page":"493","author":"Blagbrough","year":"2011"},{"key":"10.1016\/j.abb.2025.110321_bib12","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1039\/b413742f","article-title":"Polyamine alkaloids","volume":"22","author":"Bienz","year":"2005","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib13","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.3390\/molecules23051216","article-title":"Improved synthesis of n-methylcadaverine","volume":"23","author":"Anderson","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.abb.2025.110321_bib14","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1111\/tpj.14454","article-title":"Metabolic diversification of nitrogen\u2010containing metabolites by the expression of a heterologous lysine decarboxylase gene in Arabidopsis","volume":"100","author":"Shimizu","year":"2019","journal-title":"Plant J."},{"key":"10.1016\/j.abb.2025.110321_bib15","doi-asserted-by":"crossref","first-page":"1394","DOI":"10.1007\/s00018-003-2332-4","article-title":"Polyamine-dependent gene expression","volume":"60","author":"Childs","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.abb.2025.110321_bib16","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1017\/S0967199417000120","article-title":"Physiological importance of polyamines","volume":"25","author":"Lenis","year":"2017","journal-title":"Zygote"},{"key":"10.1016\/j.abb.2025.110321_bib17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s12276-018-0149-3","article-title":"Spermidine restores dysregulated autophagy and polyamine synthesis in aged and osteoarthritic chondrocytes via EP300","volume":"50","author":"Sacitharan","year":"2018","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.abb.2025.110321_bib18","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1128\/JB.01777-08","article-title":"A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine","volume":"191","author":"Fonknechten","year":"2009","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.abb.2025.110321_bib19","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/S1357-2725(02)00305-9","article-title":"Transcriptional regulation of the ornithine decarboxylase gene by c-Myc\/Max\/Mad network and retinoblastoma protein interacting with c-Myc","volume":"35","author":"Auvinen","year":"2003","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib20","series-title":"Methods and Protocols. Polyamines.","first-page":"460","year":"2018"},{"key":"10.1016\/j.abb.2025.110321_bib21","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1038\/s41568-018-0050-3","article-title":"Polyamine metabolism and cancer: treatments, challenges and opportunities","volume":"18","author":"Casero","year":"2018","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib22","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1095\/biolreprod.113.114637","article-title":"Arginine decarboxylase and agmatinase: an alternative pathway for de novo biosynthesis of polyamines for development of mammalian conceptuses","volume":"90","author":"Wang","year":"2014","journal-title":"Biol. Reprod."},{"key":"10.1016\/j.abb.2025.110321_bib23","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/0005-2744(79)90310-3","article-title":"Decarboxylation of ornithine and lysine in rat tissues","volume":"568","author":"Pegg","year":"1979","journal-title":"Biochim. Biophys. Acta Enzymol."},{"key":"10.1016\/j.abb.2025.110321_bib24","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1266\/ggs.72.167","article-title":"The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme","volume":"72","author":"Yamamoto","year":"1997","journal-title":"Genes Genet. Syst."},{"key":"10.1016\/j.abb.2025.110321_bib25","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1111\/j.1365-2672.2007.03652.x","article-title":"Lysine decarboxylase of Vibrio parahaemolyticus: kinetics of transcription and role in acid resistance","volume":"104","author":"Tanaka","year":"2008","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.abb.2025.110321_bib26","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1128\/JB.02070-12","article-title":"Three-component lysine\/ornithine decarboxylation system in Lactobacillus saerimneri 30a","volume":"195","author":"Romano","year":"2013","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.abb.2025.110321_bib27","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.jsb.2018.02.002","article-title":"A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora","volume":"202","author":"Salomone-Stagni","year":"2018","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib28","doi-asserted-by":"crossref","DOI":"10.4161\/psb.25850","article-title":"Cadaverine: a lysine catabolite involved in plant growth and development","volume":"8","author":"Tomar","year":"2013","journal-title":"Plant Signal. Behav."},{"key":"10.1016\/j.abb.2025.110321_bib29","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.plaphy.2010.01.017","article-title":"Characteristics of cellular polyamine transport in prokaryotes and eukaryotes","volume":"48","author":"Igarashi","year":"2010","journal-title":"Plant Physiol. Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib30","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41568-022-00473-2","article-title":"Polyamines in cancer: integrating organismal metabolism and antitumour immunity","volume":"22","author":"Holbert","year":"2022","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib31","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1038\/nrd2243","article-title":"Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases","volume":"6","author":"Casero","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.abb.2025.110321_bib32","doi-asserted-by":"crossref","first-page":"G517","DOI":"10.1152\/ajpgi.00169.2010","article-title":"Polyamine transport is mediated by both endocytic and solute carrier transport mechanisms in the gastrointestinal tract","volume":"299","author":"Uemura","year":"2010","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.abb.2025.110321_bib33","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1021\/mp400024d","article-title":"Polyamine transport by the polyspecific organic cation transporters OCT1, OCT2, and OCT3","volume":"10","author":"Sala-Rabanal","year":"2013","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.abb.2025.110321_bib34","doi-asserted-by":"crossref","first-page":"4045","DOI":"10.1038\/s41598-022-07712-4","article-title":"ATP13A3 facilitates polyamine transport in human pancreatic cancer cells","volume":"12","author":"Sekhar","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib35","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/0968-0004(90)90216-X","article-title":"Molecular genetics of polyamine synthesis in eukaryotic cells","volume":"15","author":"Heby","year":"1990","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib36","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1042\/bst0260575","article-title":"Regulation of mammalian ornithine decarboxylase","volume":"26","author":"Persson","year":"1998","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.abb.2025.110321_bib37","doi-asserted-by":"crossref","first-page":"14529","DOI":"10.1074\/jbc.R500031200","article-title":"Regulation of ornithine decarboxylase","volume":"281","author":"Pegg","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib38","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1006\/excr.1995.1393","article-title":"Relationship between ornithine decarboxylase and cytoskeletal organization in cultured human keratinocytes: cellular responses to phorbol esters, cytochalasins, and \u03b1-difluoromethylornithine","volume":"221","author":"Pomidor","year":"1995","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.abb.2025.110321_bib39","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1177\/002215540405201002","article-title":"Intracellular localization of ornithine decarboxylase and its regulatory protein, antizyme-1","volume":"52","author":"Schipper","year":"2004","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.abb.2025.110321_bib40","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/BF00221849","article-title":"Immunocytochemical localization of ornithine decarboxylase in cultured murine cells","volume":"243","author":"Greenfield","year":"1986","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.abb.2025.110321_bib41","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1093\/emboj\/18.5.1214","article-title":"Translocation of ornithine decarboxylase to the surface membrane during cell activation and transformation","volume":"18","author":"Heiskala","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.abb.2025.110321_bib42","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1002\/jcp.1041620209","article-title":"Regulation of human ornithine decarboxylase expression following prolonged quiescence: role for the c\u2010Myc\/Max protein complex","volume":"162","author":"Pe\u00f1a","year":"1995","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.abb.2025.110321_bib43","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S1357-2725(98)00135-6","article-title":"Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway","volume":"31","author":"Shantz","year":"1999","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib44","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1016\/j.biocel.2009.04.021","article-title":"Identification of proteins whose synthesis is preferentially enhanced by polyamines at the level of translation in mammalian cells","volume":"41","author":"Nishimura","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib45","first-page":"2239","article-title":"Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells","volume":"50","author":"Hsieh","year":"1990","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib46","first-page":"6146","article-title":"Two chromosomal locations for human ornithine decarboxylase gene sequences and elevated expression in colorectal neoplasia","volume":"50","author":"Radford","year":"1990","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib47","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1089\/dna.1.1989.8.623","article-title":"Characterization and sequence analysis of the human ornithine decarboxylase gene","volume":"8","author":"Fitzgerald","year":"1989","journal-title":"DNA"},{"key":"10.1016\/j.abb.2025.110321_bib48","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0378-1119(89)90410-1","article-title":"Human ornithine decarboxylase (ODC)-encoding gene; cloning and expression in ODC-deficient CHO cells","volume":"83","author":"H\u00f6ltt\u00e4","year":"1989","journal-title":"Gene"},{"key":"10.1016\/j.abb.2025.110321_bib49","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0378-1119(90)90233-H","article-title":"Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene","volume":"93","author":"Hickok","year":"1990","journal-title":"Gene"},{"key":"10.1016\/j.abb.2025.110321_bib50","first-page":"129","article-title":"The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes","volume":"74","author":"Mehta","year":"2000","journal-title":"Adv. Enzymol. Relat. Area Mol. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib51","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/S1570-9639(03)00050-5","article-title":"Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes. Biochimica et Biophysica","volume":"1647","author":"Paiardini","year":"2003","journal-title":"Acta Proteins and Proteomics"},{"key":"10.1016\/j.abb.2025.110321_bib52","doi-asserted-by":"crossref","unstructured":"H. Kidron, S. Repo, M.S. Johnson, T.A. Salminen. Functional classification of amino acid decarboxylases from the alanine racemase structural family by phylogenetic studies. Mol. Biol. Evol., 24, 79-89.","DOI":"10.1093\/molbev\/msl133"},{"key":"10.1016\/j.abb.2025.110321_bib53","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0014-5793(85)81311-9","article-title":"Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L-ornithine and salts","volume":"190","author":"Solano","year":"1985","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2025.110321_bib54","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1006\/jmbi.1999.3331","article-title":"Crystal structure of human ornithine decarboxylase at 2.1 \u00c5 resolution: structural insights to antizyme binding","volume":"295","author":"Almrud","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib55","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1042\/BJ20070188","article-title":"A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane","volume":"405","author":"Dufe","year":"2007","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib56","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1042\/BCJ20210647","article-title":"Structural basis of binding and inhibition of ornithine decarboxylase by 1-amino-oxy-3-aminopropane","volume":"478","author":"Zhou","year":"2021","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib57","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/S0969-2126(99)80073-2","article-title":"Structure of mammalian ornithine decarboxylase at 1.6 \u00c5 resolution: stereochemical implications of PLP-dependent amino acid decarboxylases","volume":"7","author":"Kern","year":"1999","journal-title":"Struct"},{"key":"10.1016\/j.abb.2025.110321_bib58","doi-asserted-by":"crossref","first-page":"34665","DOI":"10.1021\/acsomega.2c04702","article-title":"Structure and enzymatic activity of an intellectual disability-associated ornithine decarboxylase variant, G84R","volume":"7","author":"Zhou","year":"2022","journal-title":"ACS Omega"},{"key":"10.1016\/j.abb.2025.110321_bib59","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/S0021-9258(18)48472-4","article-title":"Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites","volume":"267","author":"Poulin","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib60","doi-asserted-by":"crossref","first-page":"11814","DOI":"10.1021\/bi9906221","article-title":"Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps","volume":"38","author":"Osterman","year":"1999","journal-title":"Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib61","doi-asserted-by":"crossref","first-page":"11247","DOI":"10.1021\/bi001209s","article-title":"Altering the reaction specificity of eukaryotic ornithine decarboxylase","volume":"39","author":"Jackson","year":"2000","journal-title":"Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib62","doi-asserted-by":"crossref","first-page":"5157","DOI":"10.1016\/j.bbagen.2013.07.003","article-title":"Mutational analysis of the antizyme-binding element reveals critical residues for the function of ornithine decarboxylase","volume":"1830","author":"Ramos-Molina","year":"2013","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.abb.2025.110321_bib63","doi-asserted-by":"crossref","first-page":"29651","DOI":"10.1074\/jbc.M100578200","article-title":"The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase, enables a well-balanced polyamine synthesis without domain-domain interaction","volume":"276","author":"Wrenger","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib64","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s40265-018-1023-2","article-title":"Pharmacokinetic and pharmacodynamic properties of L-ornithine L-aspartate (LOLA) in hepatic encephalopathy","volume":"79","author":"Kircheis","year":"2019","journal-title":"Drugs"},{"key":"10.1016\/j.abb.2025.110321_bib65","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s00726-011-1036-6","article-title":"Regulation of polyamine metabolism by translational control","volume":"42","author":"Perez-Leal","year":"2012","journal-title":"Amino acids"},{"key":"10.1016\/j.abb.2025.110321_bib66","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1002\/mc.20030","article-title":"Estrogen\u2010dependent regulation of ornithine decarboxylase in breast cancer cells through activation of nongenomic cAMP\u2010dependent pathways","volume":"40","author":"Qin","year":"2004","journal-title":"Mol. Carcinog."},{"key":"10.1016\/j.abb.2025.110321_bib67","doi-asserted-by":"crossref","first-page":"7859","DOI":"10.1073\/pnas.1332465100","article-title":"Pronounced reduction in adenoma recurrence associated with aspirin use and a polymorphism in the ornithine decarboxylase gene","volume":"100","author":"Mart\u00ednez","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.abb.2025.110321_bib68","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/j.1939-4640.1998.tb01981.x","article-title":"Androgen regulation of the human ornithine decarboxylase promoter in prostate cancer cells","volume":"19","author":"Bai","year":"1998","journal-title":"J. Androl."},{"key":"10.1016\/j.abb.2025.110321_bib69","doi-asserted-by":"crossref","first-page":"E1010","DOI":"10.1152\/ajpendo.00316.2006","article-title":"Sexual dimorphism of ornithine decarboxylase in the mouse adrenal: influence of polyamine deprivation on catecholamine and corticoid levels","volume":"292","author":"Bastida","year":"2007","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.abb.2025.110321_bib70","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.1093\/nar\/25.10.2012","article-title":"Transcription factor Sp3 antagonizes activation of the ornithine decarboxylase promoter by Sp1","volume":"25","author":"Kumar","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110321_bib71","doi-asserted-by":"crossref","first-page":"19955","DOI":"10.1074\/jbc.273.32.19955","article-title":"Transcription factor ZBP-89 regulates the activity of the ornithine decarboxylase promoter","volume":"273","author":"Law","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib72","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1002\/jcp.1111","article-title":"Sp1 and kr\u00fcppel\u2010like factor family of transcription factors in cell growth regulation and cancer","volume":"188","author":"Black","year":"2001","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.abb.2025.110321_bib73","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1093\/nar\/24.6.1149","article-title":"Regulation of ornithine decarboxylase gene expression by the Wilms' tumor suppressor WT1","volume":"24","author":"Moshier","year":"1996","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110321_bib74","doi-asserted-by":"crossref","first-page":"18866","DOI":"10.1016\/S0021-9258(19)37041-3","article-title":"Multiple DNA elements responsible for transcriptional regulation of the ornithine decarboxylase gene by protein kinase A","volume":"267","author":"Abrahamsen","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib75","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1042\/bj3160993","article-title":"Characterization of cell-specific modulatory element in the murine ornithine decarboxylase promoter","volume":"316","author":"Palvimo","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib76","doi-asserted-by":"crossref","first-page":"18757","DOI":"10.1074\/jbc.TM118.003336","article-title":"Polyamine synthesis as a target of MYC oncogenes","volume":"293","author":"Bachmann","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib77","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/BF00665680","article-title":"Estradiol control of ornithine decarboxylase mRNA, enzyme activity, and polyamine levels in MCF-7 breast cancer cells: therapeutic implications","volume":"29","author":"Thomas","year":"1994","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.abb.2025.110321_bib78","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1007\/s00726-016-2300-6","article-title":"Tamoxifen metabolite endoxifen interferes with the polyamine pathway in breast cancer","volume":"48","author":"Thomas","year":"2016","journal-title":"Amino Acids"},{"key":"10.1016\/j.abb.2025.110321_bib79","doi-asserted-by":"crossref","first-page":"7855","DOI":"10.1158\/0008-5472.CAN-07-5875","article-title":"Regulation of estrogenic effects by beclin 1 in breast cancer cells","volume":"68","author":"John","year":"2008","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib80","doi-asserted-by":"crossref","first-page":"E172","DOI":"10.1152\/ajpendo.00094.2011","article-title":"Ornithine decarboxylase is upregulated by the androgen receptor in skeletal muscle and regulates myoblast proliferation","volume":"301","author":"Lee","year":"2011","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.abb.2025.110321_bib81","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1111\/acel.12174","article-title":"Combined administration of testosterone plus an ornithine decarboxylase inhibitor as a selective prostate\u2010sparing anabolic therapy","volume":"13","author":"Jasuja","year":"2014","journal-title":"Aging Cell"},{"key":"10.1016\/j.abb.2025.110321_bib82","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/PL00010322","article-title":"Effects of testosterone and 17, \u03b2\u2013estradiol on the polyamine metabolism in cultivated normal rat kidney epithelial cells","volume":"18","author":"Jotova","year":"2000","journal-title":"Amino Acids"},{"key":"10.1016\/j.abb.2025.110321_bib83","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/0304-4165(74)90347-X","article-title":"Changes in polyamine metabolism during wound healing in rat skin","volume":"338","author":"Mizutani","year":"1974","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.abb.2025.110321_bib84","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/0006-2952(75)90136-7","article-title":"Effect of thyroxine and cortisol on brain ornithine decarboxylase activity and swimming behavior in developing rat","volume":"24","author":"Anderson","year":"1975","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib85","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/1523-1747.ep12547095","article-title":"Glucocorticoid inhibits elevated polyamine biosynthesis in psoriasis","volume":"71","author":"Russell","year":"1978","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.abb.2025.110321_bib86","doi-asserted-by":"crossref","first-page":"4341","DOI":"10.1074\/jbc.270.9.4341","article-title":"Regulation of rat ornithine decarboxylase promoter activity by binding of transcription factor Sp1","volume":"270","author":"Kumar","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib87","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/bbrc.1995.2291","article-title":"Sp1 affinity for GC-rich elements correlates with ornithine decarboxylase promoter activity","volume":"214","author":"Al-Asadi","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib88","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1006\/excr.1998.4361","article-title":"Ornithine decarboxylase is a transcriptional target of tumor suppressor WT1","volume":"247","author":"Li","year":"1999","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.abb.2025.110321_bib89","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1096\/fasebj.7.10.8393820","article-title":"The WT1 Wilms tumor gene product: a developmentally regulated transcription factor in the kidney that functions as a tumor suppressor","volume":"7","author":"Rauscher","year":"1993","journal-title":"Faseb. J."},{"key":"10.1016\/j.abb.2025.110321_bib90","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/0014-5793(93)81487-K","article-title":"A point mutation found in the WT1 gene in a sporadic Wilms' tumor without genitourinary abnormalities is identical with the most frequent point mutation in Denys-Drash syndrome","volume":"317","author":"Akasaka","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2025.110321_bib91","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1002\/jcp.1041350317","article-title":"Involvement of cAMP and calcium in the induction of ornithine decarboxylase activity in an osteoblast cell line","volume":"135","author":"Van Leeuwen","year":"1988","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.abb.2025.110321_bib92","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1038\/334494a0","article-title":"Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB","volume":"334","author":"Yamamoto","year":"1988","journal-title":"Nature"},{"key":"10.1016\/j.abb.2025.110321_bib93","doi-asserted-by":"crossref","first-page":"5761","DOI":"10.1073\/pnas.82.17.5761","article-title":"Nerve growth factor rapidly induces ornithine decarboxylase mRNA in PC12 rat pheochromocytoma cells","volume":"82","author":"Feinstein","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.abb.2025.110321_bib94","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1002\/jnr.490340307","article-title":"Molecular analysis of the nerve growth factor inducible ornithine decarboxylase gene in PC12 cells","volume":"34","author":"Muller","year":"1993","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2025.110321_bib95","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0079-6123(08)61297-2","article-title":"Mechanism of action and possible sites of synthesis of nerve growth factor","volume":"51","author":"Thoenen","year":"1979","journal-title":"Prog. Brain Res."},{"key":"10.1016\/j.abb.2025.110321_bib96","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1038\/nrm.2017.103","article-title":"Functional 5\u2032 UTR mRNA structures in eukaryotic translation regulation and how to find them","volume":"19","author":"Leppek","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib97","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1007\/s00018-005-5020-8","article-title":"Alternative splicing facilitates internal ribosome entry on the ornithine decarboxylase mRNA","volume":"62","author":"Pyronnet","year":"2005","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.abb.2025.110321_bib98","first-page":"1742","article-title":"Relief of ornithine decarboxylase messenger RNA translational repression induced by alternative splicing of its 5' untranslated region","volume":"56","author":"Pyronnet","year":"1996","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib99","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1042\/bj3560627","article-title":"Importance of the 3\u2032 untranslated region of ornithine decarboxylase mRNA in the translational regulation of the enzyme","volume":"356","author":"L\u00f6vkvist Wallstr\u00f6m","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib100","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1042\/bj3260361","article-title":"Co-operation of the 5\u2032 and 3\u2032 untranslated regions of ornithine decarboxylase mRNA and inhibitory role of its 3\u2032 untranslated region in regulating the translational efficiency of hybrid RNA species via cellular factor","volume":"326","author":"Lorenzini","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib101","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1042\/bj20030778","article-title":"Transcriptional and translational control of ornithine decarboxylase during Ras transformation","volume":"377","author":"Shantz","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib102","doi-asserted-by":"crossref","first-page":"4834","DOI":"10.1158\/0008-5472.CAN-06-4627","article-title":"Ras transformation of RIE-1 cells activates cap-independent translation of ornithine decarboxylase: regulation by the Raf\/MEK\/ERK and phosphatidylinositol 3-kinase pathways","volume":"67","author":"Origanti","year":"2007","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib103","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1517\/14728222.2013.764990","article-title":"Targeting the RAS oncogene","volume":"17","author":"Takashima","year":"2013","journal-title":"Expert Opin. Ther. Targets"},{"key":"10.1016\/j.abb.2025.110321_bib104","doi-asserted-by":"crossref","first-page":"3528","DOI":"10.1016\/S0021-9258(18)69102-1","article-title":"Regulation of ornithine decarboxylase mRNA translation by polyamines. Studies using a cell-free system and a cell line with an amplified ornithine decarboxylase gene","volume":"263","author":"Persson","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib105","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1111\/j.1432-1033.1991.tb15927.x","article-title":"Mouse ornithine decarboxylase is phosphorylated by casein kinase\u2010II at a predominant single location (serine 303)","volume":"197","author":"Rosenberg\u2010Hasson","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib106","doi-asserted-by":"crossref","first-page":"34458","DOI":"10.1074\/jbc.M105219200","article-title":"Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme","volume":"276","author":"Bauer","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib107","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S0300-9084(01)01252-4","article-title":"Antizyme, a mediator of ubiquitin-independent proteasomal degradation","volume":"83","author":"Coffino","year":"2001","journal-title":"Biochimie"},{"key":"10.1016\/j.abb.2025.110321_bib108","doi-asserted-by":"crossref","first-page":"18730","DOI":"10.1074\/jbc.TM118.003339","article-title":"The antizyme family for regulating polyamines","volume":"293","author":"Kahana","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib109","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.4161\/cc.4.11.2115","article-title":"Mechanisms of protein degradation: an odyssey with ODC","volume":"4","author":"Kahana","year":"2005","journal-title":"Cell Cycle"},{"key":"10.1016\/j.abb.2025.110321_bib110","doi-asserted-by":"crossref","first-page":"4857","DOI":"10.1038\/sj.emboj.7600473","article-title":"Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme","volume":"23","author":"Palanimurugan","year":"2004","journal-title":"EMBO J."},{"key":"10.1016\/j.abb.2025.110321_bib111","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1042\/BCJ20160519C","article-title":"Protein degradation, the main hub in the regulation of cellular polyamines","volume":"473","author":"Kahana","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib112","article-title":"Structural basis of Ornithine Decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1","volume":"5","author":"Wu","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib113","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/BJ20040547","article-title":"Regulation of all members of the antizyme family by antizyme inhibitor","volume":"385","author":"Mangold","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib114","doi-asserted-by":"crossref","first-page":"54097","DOI":"10.1074\/jbc.M410234200","article-title":"Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme","volume":"279","author":"Bercovich","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib115","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/cas.13122","article-title":"Antizyme inhibitor 1: a potential carcinogenic molecule","volume":"108","author":"Qiu","year":"2017","journal-title":"Cancer Sci."},{"key":"10.1016\/j.abb.2025.110321_bib116","first-page":"89","article-title":"Antizyme inhibitors in polyamine metabolism and beyond: physiopathological implications","volume":"6","author":"Ramos-Molina","year":"2018","journal-title":"Med. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib117","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/s12964-023-01445-1","article-title":"Antizyme inhibitor family: biological and translational research implications","volume":"22","author":"Feng","year":"2024","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.abb.2025.110321_bib118","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.molcel.2005.01.020","article-title":"20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1","volume":"17","author":"Asher","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/j.abb.2025.110321_bib119","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1021\/acs.jnatprod.3c00661","article-title":"Syrosingopine enhances 20S proteasome activity and degradation of \u03b1-synuclein","volume":"87","author":"Sadahiro","year":"2024","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.abb.2025.110321_bib120","doi-asserted-by":"crossref","first-page":"2948","DOI":"10.1016\/j.bbagen.2018.09.009","article-title":"The physiological role of the free 20S proteasome in protein degradation: a critical review","volume":"1862","author":"Demasi","year":"2018","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.abb.2025.110321_bib121","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1042\/bj1080533","article-title":"Biosynthesis of putrescine in the prostate gland of the rat","volume":"108","author":"Pegg","year":"1968","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib122","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1016\/j.bbapap.2011.05.014","article-title":"Analysis of catalytic determinants of diaminopimelate and ornithine decarboxylases using alternate substrates","volume":"1814","author":"Fogle","year":"2011","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.abb.2025.110321_bib123","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/0005-2744(72)90067-8","article-title":"Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats. Purification and some properties","volume":"284","author":"Ono","year":"1972","journal-title":"Biochim. Biophys. Acta Enzymol."},{"key":"10.1016\/j.abb.2025.110321_bib124","doi-asserted-by":"crossref","first-page":"6721","DOI":"10.1021\/bi00526a030","article-title":"Ornithine decarboxylase from calf liver. Purification and properties","volume":"20","author":"Haddox","year":"1981","journal-title":"Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib125","doi-asserted-by":"crossref","first-page":"361","DOI":"10.3177\/jnsv.55.361","article-title":"Long-term oral polyamine intake increases blood polyamine concentrations","volume":"55","author":"Soda","year":"2009","journal-title":"J. Nutr. Sci. Vitaminol."},{"key":"10.1016\/j.abb.2025.110321_bib126","doi-asserted-by":"crossref","first-page":"2423","DOI":"10.1007\/s00726-016-2246-8","article-title":"Polyamine\u2013DNA interactions and development of gene delivery vehicles","volume":"48","author":"Thomas","year":"2016","journal-title":"Amino Acids"},{"key":"10.1016\/j.abb.2025.110321_bib127","unstructured":"J. Ferlay, M. Ervik, F. Lam, M. Laversanne, M. Colombet, L. Mery, M. Pi\u00f1eros, A. Znaor, I. Soerjomataram, F. Bray, in Global Cancer Observatory: Cancer Today. Estimated number of deaths in 2020, worldwide, both sexes, all ages. Lyon, France: International Agency for Research on Cancer. https:\/\/gco.iarc.who.int\/today Accessed 10 June 2024."},{"key":"10.1016\/j.abb.2025.110321_bib128","doi-asserted-by":"crossref","first-page":"209","DOI":"10.3322\/caac.21660","article-title":"Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries","volume":"71","author":"Sung","year":"2021","journal-title":"CA A Cancer J. Clin."},{"key":"10.1016\/j.abb.2025.110321_bib129","doi-asserted-by":"crossref","first-page":"8392","DOI":"10.1038\/sj.onc.1208217","article-title":"RNAi and HTS: exploring cancer by systematic loss-of-function","volume":"23","author":"Willingham","year":"2004","journal-title":"Oncogene"},{"key":"10.1016\/j.abb.2025.110321_bib130","doi-asserted-by":"crossref","first-page":"1438","DOI":"10.1038\/nm.3336","article-title":"The epigenetics of epithelial-mesenchymal plasticity in cancer","volume":"19","author":"Tam","year":"2013","journal-title":"Nat. Med."},{"key":"10.1016\/j.abb.2025.110321_bib131","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1146\/annurev.ge.18.120184.003005","article-title":"The molecular genetics of cellular oncogenes","volume":"18","author":"Varmus","year":"1984","journal-title":"Annu. Rev. Genet."},{"key":"10.1016\/j.abb.2025.110321_bib132","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1038\/sj.onc.1201273","article-title":"Induction of ornithine decarboxylase by IL-3 is mediated by sequential c-Myc-independent and c-Myc-dependent pathways","volume":"15","author":"Packham","year":"1997","journal-title":"Oncogene"},{"key":"10.1016\/j.abb.2025.110321_bib133","first-page":"3016","article-title":"Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice","volume":"57","author":"Auvinen","year":"1997","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib134","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1093\/nar\/25.8.1493","article-title":"c-Myc\/Max heterodimers bind cooperatively to the E-box sequences located in the first intron of the rat ornithine decarboxylase (ODC) gene","volume":"25","author":"Walhout","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110321_bib135","first-page":"249","article-title":"hnRNP U interacts with the c-Myc-Max complex on the E-box promoter region inducing the ornithine decarboxylase gene","volume":"22","author":"Matsuoka","year":"2009","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib136","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/mc.20047","article-title":"Differences in ornithine decarboxylase and androgen receptor allele frequencies among ethnic groups","volume":"41","author":"O'Brien","year":"2004","journal-title":"Mol. Carcinog."},{"key":"10.1016\/j.abb.2025.110321_bib137","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrc969","article-title":"Targeting RAS signalling pathways in cancer therapy","volume":"3","author":"Downward","year":"2003","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib138","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1007\/s00726-007-0531-2","article-title":"Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential","volume":"33","author":"Shantz","year":"2007","journal-title":"Amino acids"},{"key":"10.1016\/j.abb.2025.110321_bib139","doi-asserted-by":"crossref","first-page":"5546","DOI":"10.1158\/1078-0432.CCR-12-0977","article-title":"c-Myc and cancer metabolism","volume":"18","author":"Miller","year":"2012","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib140","series-title":"Encyclopedia of Cancer","first-page":"947","author":"M\u00e4dge","year":"2008"},{"key":"10.1016\/j.abb.2025.110321_bib141","doi-asserted-by":"crossref","first-page":"142","DOI":"10.3390\/genes8050142","article-title":"MYC\u2014master regulator of the cancer epigenome and transcriptome","volume":"8","author":"Poole","year":"2017","journal-title":"Genes"},{"key":"10.1016\/j.abb.2025.110321_bib142","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/MCB.19.1.1","article-title":"c-Myc target genes involved in cell growth, apoptosis, and metabolism","volume":"19","author":"Dang","year":"1999","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib143","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1124\/mol.62.6.1400","article-title":"c-Myc exerts a protective function through ornithine decarboxylase against cellular insults","volume":"62","author":"Park","year":"2002","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib144","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s12943-020-01291-6","article-title":"Taking the Myc out of cancer: toward therapeutic strategies to directly inhibit c-Myc","volume":"20","author":"Madden","year":"2021","journal-title":"Mol. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib145","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1038\/nrm1703","article-title":"Transcriptional regulation and transformation by Myc proteins","volume":"6","author":"Adhikary","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib146","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/s41392-018-0008-7","article-title":"Targeting oncogenic Myc as a strategy for cancer treatment","volume":"3","author":"Chen","year":"2018","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.abb.2025.110321_bib147","doi-asserted-by":"crossref","first-page":"883","DOI":"10.3390\/cells9040883","article-title":"Blocking Myc to treat cancer: reflecting on two decades of omomyc","volume":"9","author":"Mass\u00f3-Vall\u00e9s","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.abb.2025.110321_bib148","doi-asserted-by":"crossref","first-page":"9735","DOI":"10.1158\/0008-5472.CAN-07-6866","article-title":"ODC1 is a critical determinant of MYCN oncogenesis and a therapeutic target in neuroblastoma","volume":"68","author":"Hogarty","year":"2008","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib149","series-title":"Drug Targeting and Stimuli Sensitive Drug Delivery Systems","first-page":"1","author":"Yildizhan","year":"2018"},{"key":"10.1016\/j.abb.2025.110321_bib150","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.drup.2016.07.001","article-title":"Old drugs, novel ways out: drug resistance toward cytotoxic chemotherapeutics","volume":"28","author":"Wijdeven","year":"2016","journal-title":"Drug Resist. Updates"},{"key":"10.1016\/j.abb.2025.110321_bib151","first-page":"215","article-title":"Principles of cancer treatment by chemotherapy","volume":"39","author":"Dickens","year":"2021","journal-title":"Surg"},{"key":"10.1016\/j.abb.2025.110321_bib152","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbcan.2019.188310","article-title":"Mechanisms of acquired tumor drug resistance","volume":"1872","author":"Aleksakhina","year":"2019","journal-title":"Biochim. Biophys. Acta, Rev. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib153","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0189044","article-title":"Ornithine decarboxylase as a therapeutic target for endometrial cancer","volume":"12","author":"Kim","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.abb.2025.110321_bib154","doi-asserted-by":"crossref","first-page":"659","DOI":"10.3390\/cells10030659","article-title":"Signaling pathways in cancer: therapeutic targets, combinatorial treatments, and new developments","volume":"10","author":"Yip","year":"2021","journal-title":"Cells"},{"key":"10.1016\/j.abb.2025.110321_bib155","first-page":"226","article-title":"Translational development of difluoromethylornithine (DFMO) for the treatment of neuroblastoma","volume":"4","author":"Bassiri","year":"2015","journal-title":"Transl. Pediatr."},{"key":"10.1016\/j.abb.2025.110321_bib156","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/s41392-020-00235-2","article-title":"Regulation of cancer cell metabolism: oncogenic MYC in the driver's seat","volume":"5","author":"Dong","year":"2020","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.abb.2025.110321_bib157","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1073\/pnas.73.5.1626","article-title":"Alpha-methyl ornithine, a potent competitive inhibitor of ornithine decarboxylase, blocks proliferation of rat hepatoma cells in culture","volume":"73","author":"Mamont","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.abb.2025.110321_bib158","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/0006-291X(77)91585-6","article-title":"Effect of alpha-methyl ornithine on ornithine decarboxylase activity of rat hepatoma cells in culture","volume":"76","author":"McCann","year":"1977","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib159","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/0005-2744(73)90433-6","article-title":"Ornithine decarboxylase: inhibition by alpha-hydrazinoornithine","volume":"327","author":"Harik","year":"1973","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2025.110321_bib160","doi-asserted-by":"crossref","first-page":"537","DOI":"10.2174\/1389450033490885","article-title":"Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect. Part 1. Selective enzyme inhibitors","volume":"4","author":"Seiler","year":"2003","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.abb.2025.110321_bib161","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/0012-1606(78)90204-X","article-title":"Inhibitory effect of alpha-hydrazinoornithine on egg cleavage in sea urchin eggs","volume":"67","author":"Kusunoki","year":"1978","journal-title":"Dev. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib162","first-page":"569","article-title":"Effect of DL-alpha-hydrazino-delta-aminovaleric acid, an inhibitor of ornithine decarboxylase, on polyamine metabolism and growth of mouse sarcoma-180","volume":"67","author":"Kato","year":"1976","journal-title":"Gan"},{"key":"10.1016\/j.abb.2025.110321_bib163","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1093\/oxfordjournals.jbchem.a134359","article-title":"Inhibition of polyamine synthesis and proliferation in mouse L cells by DL-alpha-hydrazino-delta-aminovaleric acid, an inhibitor of ornithine decarboxylase","volume":"94","author":"Gohda","year":"1983","journal-title":"J. Biochem."},{"key":"10.1016\/j.abb.2025.110321_bib164","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/0304-4165(81)90149-5","article-title":"Several inhibitors of ornithine and adenosylmethionine decarboxylases may also have antiproliferative effects unrelated to polyamine depletion","volume":"677","author":"H\u00f6ltt\u00e4","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2025.110321_bib165","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0006-291X(83)90406-0","article-title":"(2R,5R)-6-heptyne-2,5-diamine, an extremely potent inhibitor of mammalian ornithine decarboxylase","volume":"116","author":"Danzin","year":"1983","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib166","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2022.912279","article-title":"The role of polyamine metabolism in remodeling immune responses and blocking therapy within the tumor immune microenvironment","volume":"13","author":"Lian","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.abb.2025.110321_bib167","first-page":"4972","article-title":"Antitumor properties of (2R,5R)-6-heptyne-2,5-diamine, a new potent enzyme-activated irreversible inhibitor of ornithine decarboxylase, in rodents","volume":"44","author":"Bartholeyns","year":"1984","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib168","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1007\/BF00435834","article-title":"Phase I study of methylacetylenic putrescine, an inhibitor of polyamine biosynthesis","volume":"23","author":"Cornbleet","year":"1989","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib169","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/BF02940297","article-title":"Assessment of renal toxicity by urinary enzymes in patients receiving chemotherapy with 8-methyl-8-acetylenic-putrescine","volume":"26","author":"Carmichael","year":"1990","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib170","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/0006-291X(85)90458-9","article-title":"1-Aminooxy-3-aminopropane, a new and potent inhibitor of polyamine biosynthesis that inhibits ornithine decarboxylase, adenosylmethionine decarboxylase and spermidine synthase","volume":"130","author":"Khomutov","year":"1985","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib171","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1042\/bj2630215","article-title":"Effect of 1-amino-oxy-3-aminopropane on polyamine metabolism and growth of L1210 cells","volume":"263","author":"Poulin","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib172","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1042\/bj2570929","article-title":"Feedback regulation of S-adenosylmethionine decarboxylase synthesis","volume":"257","author":"Persson","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib173","doi-asserted-by":"crossref","first-page":"262","DOI":"10.2174\/13816128113199990037","article-title":"Charge deficient analogues of the natural polyamines","volume":"20","author":"Weisell","year":"2014","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.abb.2025.110321_bib174","doi-asserted-by":"crossref","first-page":"345","DOI":"10.3109\/14756366.2014.926342","article-title":"N-\u03c9-chloroacetyl-l-ornithine, a new competitive inhibitor of ornithine decarboxylase, induces selective growth inhibition and cytotoxicity on human cancer cells versus normal cells","volume":"30","author":"Medina-Enr\u00edquez","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.abb.2025.110321_bib175","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1097\/CAD.0000000000000353","article-title":"N-\u03c9-chloroacetyl-L-ornithine has in vitro activity against cancer cell lines and in vivo activity against ascitic and solid tumors","volume":"27","author":"Vargas-Ram\u00edrez","year":"2016","journal-title":"Anti Cancer Drugs"},{"key":"10.1016\/j.abb.2025.110321_bib176","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1007\/s00044-008-9103-6","article-title":"Computational and experimental evaluation of ornithine derivatives as ornithine decarboxylase inhibitors","volume":"18","author":"Correa-Basurto","year":"2009","journal-title":"Med. Chem. Res."},{"key":"10.1016\/j.abb.2025.110321_bib177","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2022.106118","article-title":"Anticancer potential of allicin: a review","volume":"177","author":"Catanzaro","year":"2022","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.abb.2025.110321_bib178","doi-asserted-by":"crossref","first-page":"5452","DOI":"10.3390\/molecules27175452","article-title":"Combination anticancer therapies using selected phytochemicals","volume":"27","author":"Talib","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.abb.2025.110321_bib179","doi-asserted-by":"crossref","first-page":"2518","DOI":"10.1021\/acs.jnatprod.0c00613","article-title":"Allicin, a potent new ornithine decarboxylase inhibitor in neuroblastoma cells","volume":"83","author":"Schultz","year":"2020","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.abb.2025.110321_bib180","doi-asserted-by":"crossref","first-page":"3867","DOI":"10.3390\/nu12123867","article-title":"Baicalein, 7, 8-Dihydroxyflavone and myricetin as potent inhibitors of human ornithine decarboxylase","volume":"12","author":"Liu","year":"2020","journal-title":"Nutrients"},{"key":"10.1016\/j.abb.2025.110321_bib181","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.3390\/ijms17101681","article-title":"The fascinating effects of baicalein on cancer: a review","volume":"17","author":"Liu","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib182","doi-asserted-by":"crossref","first-page":"3095","DOI":"10.1016\/S0960-894X(01)00617-5","article-title":"Flavonoids: structural requirements for antiproliferative activity on breast cancer cells","volume":"11","author":"Pouget","year":"2001","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.abb.2025.110321_bib183","doi-asserted-by":"crossref","first-page":"631","DOI":"10.3892\/or.2014.3632","article-title":"Apoptotic effects of 7, 8-dihydroxyflavone in human oral squamous cancer cells through suppression of Sp1","volume":"33","author":"Lee","year":"2015","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib184","doi-asserted-by":"crossref","first-page":"528","DOI":"10.3892\/or.2016.4825","article-title":"Anticancer activity of 7, 8-dihydroxyflavone in melanoma cells via downregulation of \u03b1-MSH\/cAMP\/MITF pathway","volume":"36","author":"Sim","year":"2016","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib185","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.mrgentox.2012.12.002","article-title":"Apoptosis induction of human leukemia U937 cells by 7, 8-dihydroxyflavone hydrate through modulation of the Bcl-2 family of proteins and the MAPKs signaling pathway","volume":"751","author":"Park","year":"2013","journal-title":"Mutat. Res. Genet. Toxicol. Environ. Mutagen"},{"key":"10.1016\/j.abb.2025.110321_bib186","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-015-0048-7","article-title":"7, 8-dihydroxyflavone, a small molecular TrkB agonist, is useful for treating various BDNF-implicated human disorders","volume":"5","author":"Liu","year":"2016","journal-title":"Transl. Neurodegener."},{"key":"10.1016\/j.abb.2025.110321_bib187","doi-asserted-by":"crossref","first-page":"90","DOI":"10.3390\/nu8020090","article-title":"Myricetin: a dietary molecule with diverse biological activities","volume":"8","author":"Semwal","year":"2016","journal-title":"Nutrients"},{"key":"10.1016\/j.abb.2025.110321_bib188","doi-asserted-by":"crossref","first-page":"4411","DOI":"10.3390\/ijms23084411","article-title":"Molecular pathways involved in the anti-cancer activity of flavonols: a focus on myricetin and kaempferol","volume":"23","author":"Felice","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib189","first-page":"19","article-title":"Preformulation studies of myricetin: a natural antioxidant flavonoid","volume":"69","author":"Yao","year":"2014","journal-title":"Pharmazie"},{"key":"10.1016\/j.abb.2025.110321_bib190","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1093\/carcin\/bgx082","article-title":"Herbacetin suppresses cutaneous squamous cell carcinoma and melanoma cell growth by targeting AKT and ODC","volume":"38","author":"Kim","year":"2017","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.abb.2025.110321_bib191","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1158\/0008-5472.CAN-15-0442","article-title":"Herbacetin is a novel allosteric inhibitor of ornithine decarboxylase with antitumor activity","volume":"76","author":"Kim","year":"2016","journal-title":"Cancer Res."},{"key":"10.1016\/j.abb.2025.110321_bib192","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.fct.2012.09.036","article-title":"Herbacetin induces apoptosis in HepG2 cells: involvements of ROS and PI3K\/Akt pathway","volume":"51","author":"Qiao","year":"2013","journal-title":"Food Chem. Toxicol."},{"key":"10.1016\/j.abb.2025.110321_bib193","doi-asserted-by":"crossref","DOI":"10.1016\/j.jep.2021.114356","article-title":"A comprehensive review of herbacetin: from chemistry to pharmacological activities","volume":"279","author":"Wei","year":"2021","journal-title":"J. Ethnopharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib194","doi-asserted-by":"crossref","first-page":"2551","DOI":"10.1021\/ja00476a050","article-title":"Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C.4.1.1.17) by substrate and product analogs","volume":"100","author":"Metcalf","year":"1978","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.abb.2025.110321_bib195","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0053397","article-title":"Structural insight into DFMO resistant ornithine decarboxylase from Entamoeba histolytica: an inkling to adaptive evolution","volume":"8","author":"Preeti","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.abb.2025.110321_bib196","doi-asserted-by":"crossref","first-page":"809","DOI":"10.2217\/fon-2016-0266","article-title":"Difluoromethylornithine in cancer: new advances","volume":"13","author":"Alexiou","year":"2017","journal-title":"Future Oncol."},{"key":"10.1016\/j.abb.2025.110321_bib197","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001204","article-title":"A molecular mechanism for eflornithine resistance in African trypanosomes","volume":"6","author":"Vincent","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.abb.2025.110321_bib198","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.bpg.2011.09.007","article-title":"DFMO: targeted risk reduction therapy for colorectal neoplasia","volume":"25","author":"Laukaitis","year":"2011","journal-title":"Best Pract. Res. Clin. Gastroenterol."},{"key":"10.1016\/j.abb.2025.110321_bib199","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/0006-291X(78)91630-3","article-title":"Anti-proliferative properties of DL-alpha-difluoromethyl ornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylase","volume":"81","author":"Mamont","year":"1978","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib200","first-page":"458","article-title":"An approach to the use of polyamine inhibitors for cancer therapy","volume":"59","author":"Marton","year":"1981","journal-title":"Med. Biol."},{"key":"10.1016\/j.abb.2025.110321_bib201","first-page":"261","article-title":"Clinical relevance of polyamines","volume":"18","author":"Russell","year":"1983","journal-title":"Crit. Rev. Clin. Lab Sci."},{"key":"10.1016\/j.abb.2025.110321_bib202","first-page":"543","article-title":"Treatment of hamster pancreatic cancer with alpha-difluoromethylornithine, an inhibitor of polyamine biosynthesis","volume":"79","author":"Marx","year":"1987","journal-title":"J. Natl. Cancer Inst."},{"key":"10.1016\/j.abb.2025.110321_bib203","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1023\/A:1016375705487","article-title":"Polyamine-DNA interactions: possible site of new cancer chemotherapeutic intervention","volume":"3","author":"Marton","year":"1986","journal-title":"Pharm. Res. (N. Y.)"},{"key":"10.1016\/j.abb.2025.110321_bib204","article-title":"Targeting metabolic vulnerabilities of cancer: small molecule inhibitors in clinic","volume":"2","author":"Tripathi","year":"2019","journal-title":"Cancer Rep"},{"key":"10.1016\/j.abb.2025.110321_bib205","doi-asserted-by":"crossref","first-page":"4001","DOI":"10.3390\/cancers15154001","article-title":"Chemoprevention of colon cancer by DFMO, sulindac, and NO-sulindac administered individually or in combinations in F344 rats","volume":"15","author":"Madka","year":"2023","journal-title":"Cancers"},{"key":"10.1016\/j.abb.2025.110321_bib206","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.3892\/ijo.2013.1835","article-title":"DFMO\/eflornithine inhibits migration and invasion downstream of MYCN and involves p27Kip1 activity in neuroblastoma","volume":"4","author":"Koomoa","year":"2013","journal-title":"Int. J. Oncol."},{"key":"10.1016\/j.abb.2025.110321_bib207","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1007\/s00280-021-04309-y","article-title":"Probenecid increases renal retention and antitumor activity of DFMO in neuroblastoma","volume":"88","author":"Schultz","year":"2021","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.abb.2025.110321_bib208","article-title":"A phase I trial of DFMO targeting polyamine addiction in patients with relapsed\/refractory neuroblastoma","volume":"5","author":"Saulnier Sholler","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.abb.2025.110321_bib209","unstructured":"G. Mauro, in Oncology Nursing News. FDA Approves Eflornithine for Children, Adults with High-Risk Neuroblastoma. Gale Academic OneFile. Intellisphere, LLC. https:\/\/link.gale.com\/apps\/doc\/A776635045\/AONE?u=ano\u00f17b7ee7ae&sid=googleScholar&xid=5d6955db Accessed 3 April 2024."},{"key":"10.1016\/j.abb.2025.110321_bib210","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1200\/JCO.22.02875","article-title":"Eflornithine as postimmunotherapy maintenance in high-risk neuroblastoma: externally controlled, propensity score-matched survival outcome comparisons","volume":"42","author":"Oesterheld","year":"2024","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.abb.2025.110321_bib212","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj20031327","article-title":"A perspective of polyamine metabolism","volume":"376","author":"Wallace","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2025.110321_bib213","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1021\/acsmedchemlett.1c00557","article-title":"Development of polyamine lassos as polyamine transport inhibitors","volume":"13","author":"Dobrovolskaite","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.abb.2025.110321_bib214","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-16007-7","article-title":"Difluoromethylornithine (DFMO) and AMXT 1501 inhibit capsule biosynthesis in pneumococci","volume":"12","author":"Ayoola","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2025.110321_bib215","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/s41467-021-20896-z","article-title":"Dual targeting of polyamine synthesis and uptake in diffuse intrinsic pontine gliomas","volume":"12","author":"Khan","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2025.110321_bib216","doi-asserted-by":"crossref","DOI":"10.1016\/j.biocel.2021.106038","article-title":"The discovery of indolone GW5074 during a comprehensive search for non-polyamine-based polyamine transport inhibitors","volume":"138","author":"Dobrovolskaite","year":"2021","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110321_bib217","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1158\/1940-6207.CAPR-08-0042","article-title":"Difluoromethylornithine plus sulindac for the prevention of sporadic colorectal adenomas: a randomized placebo-controlled, double-blind trial","volume":"1","author":"Meyskens","year":"2008","journal-title":"Cancer Prev. Res."},{"key":"10.1016\/j.abb.2025.110321_bib218","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1038\/s41416-023-02525-2","article-title":"Phase 1 study of high-dose DFMO, celecoxib, cyclophosphamide and topotecan for patients with relapsed neuroblastoma: a New Approaches to Neuroblastoma Therapy trial","volume":"130","author":"Hogarty","year":"2024","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.abb.2025.110321_bib219","doi-asserted-by":"crossref","first-page":"8173","DOI":"10.3390\/ijms25158173","article-title":"The synergistic benefit of combination strategies targeting tumor cell polyamine homeostasis","volume":"25","author":"Liu","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib220","doi-asserted-by":"crossref","first-page":"84140","DOI":"10.18632\/oncotarget.20493","article-title":"A novel polyamine blockade therapy activates an anti-tumor immune response","volume":"8","author":"Alexander","year":"2017","journal-title":"Oncotarget"},{"key":"10.1016\/j.abb.2025.110321_bib221","first-page":"44","article-title":"Polyamine-based nanostructures share polyamine transport mechanisms with native polyamines and their analogues: significance for polyamine-targeted therapy","volume":"10","author":"Holbert","year":"2022","journal-title":"Med. Sci."},{"key":"10.1016\/j.abb.2025.110321_bib222","first-page":"65","article-title":"Polyamine biosynthetic pathway as a drug target for osteosarcoma therapy","volume":"6","author":"Weicht","year":"2018","journal-title":"Med. Sci."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125000347?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125000347?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,4,30]],"date-time":"2025-04-30T08:10:21Z","timestamp":1746000621000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986125000347"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3]]},"references-count":221,"alternative-id":["S0003986125000347"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2025.110321","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2025,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Ornithine decarboxylase and its role in cancer","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2025.110321","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"110321"}}