{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T06:05:34Z","timestamp":1792821934693,"version":"4.5.0"},"reference-count":78,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,12,24]],"date-time":"2020-12-24T00:00:00Z","timestamp":1608768000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006668","name":"Fondo para la Investigaci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006668","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2021,4]]},"DOI":"10.1016\/j.redox.2020.101850","type":"journal-article","created":{"date-parts":[[2020,12,28]],"date-time":"2020-12-28T12:34:29Z","timestamp":1609158869000},"page":"101850","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":93,"special_numbering":"C","title":["The toxic side of one-carbon metabolism and epigenetics"],"prefix":"10.1016","volume":"40","author":[{"given":"Agust\u00edn E.","family":"Morellato","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carla","family":"Umansky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8384-3422","authenticated-orcid":false,"given":"Lucas B.","family":"Pontel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.redox.2020.101850_bib1","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1146\/annurev-physiol-020911-153251","article-title":"The intestinal absorption of folates","volume":"76","author":"Visentin","year":"2014","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.redox.2020.101850_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12929-014-0077-z","article-title":"Folic acid supplementation in pregnancy and implications in health and disease","volume":"21","author":"Barua","year":"2014","journal-title":"J. Biomed. Sci."},{"key":"10.1016\/j.redox.2020.101850_bib3","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0092-8674(74)90091-9","article-title":"Isolation and biochemical characterization of folate deficient mutants of Chinese hamster cells","volume":"2","author":"McBurney","year":"1974","journal-title":"Cell"},{"key":"10.1016\/j.redox.2020.101850_bib4","doi-asserted-by":"crossref","first-page":"11910","DOI":"10.1016\/S0021-9258(19)50286-1","article-title":"Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization","volume":"268","author":"Garrow","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib5","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1139\/o70-156","article-title":"Oxidative degradation of dihydrofolate and tetrahydrofolate","volume":"48","author":"Chippel","year":"1970","journal-title":"Can. J. Biochem."},{"key":"10.1016\/j.redox.2020.101850_bib6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0083-6729(08)00401-9","article-title":"Chapter 1 folate-mediated one-carbon metabolism","volume":"79","author":"Fox","year":"2008","journal-title":"Vitam. Horm."},{"key":"10.1016\/j.redox.2020.101850_bib7","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1038\/nature23481","article-title":"Mammals divert endogenous genotoxic formaldehyde into one-carbon metabolism","volume":"548","author":"Burgos-barragan","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.redox.2020.101850_bib8","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.molcel.2015.08.020","article-title":"Endogenous formaldehyde is a hematopoietic stem cell genotoxin and metabolic carcinogen","volume":"60","author":"Pontel","year":"2015","journal-title":"Mol. Cell."},{"key":"10.1016\/j.redox.2020.101850_bib9","series-title":"Endogenous Formaldehyde Scavenges Cellular Glutathione Resulting in Cytotoxic Redox Disruption","first-page":"2020","author":"Umansky","year":"2020"},{"key":"10.1016\/j.redox.2020.101850_bib10","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1016\/j.ajpath.2016.06.022","article-title":"Formaldehyde is a potent proteotoxic stressor causing rapid Heat Shock transcription factor 1 activation and lys48-linked polyubiquitination of proteins","volume":"186","author":"Ortega-Atienza","year":"2016","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.redox.2020.101850_bib11","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cmet.2016.08.009","article-title":"One-carbon metabolism in health and disease","volume":"25","author":"Ducker","year":"2017","journal-title":"Cell Metabol."},{"key":"10.1016\/j.redox.2020.101850_bib12","series-title":"Genotoxicity of Tetrahydrofolic Acid to Hematopoietic Stem and Progenitor Cells","author":"Jos\u00e9","year":"2018"},{"key":"10.1016\/j.redox.2020.101850_bib13","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1146\/annurev-nutr-071714-034441","article-title":"Nuclear folate metabolism","volume":"38","author":"Field","year":"2014","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.redox.2020.101850_bib14","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/0003-9861(85)90516-8","article-title":"Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver","volume":"243","author":"Porter","year":"1985","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2020.101850_bib15","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1038\/nature25460","article-title":"Mitochondrial translation requires folate-dependent tRNA methylation","volume":"554","author":"Morscher","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.redox.2020.101850_bib16","doi-asserted-by":"crossref","first-page":"15163","DOI":"10.1073\/pnas.1103623108","article-title":"Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria","volume":"108","author":"Andersona","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.redox.2020.101850_bib17","article-title":"Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase\/methenyltetrahydrofolate cyclohydrolase","volume":"5","author":"Shin","year":"2017","journal-title":"Canc. Metabol."},{"key":"10.1016\/j.redox.2020.101850_bib18","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.cmet.2011.07.010","article-title":"Mutations in MTFMT underlie a human disorder of formylation causing impaired mitochondrial translation","volume":"14","author":"Tucker","year":"2011","journal-title":"Cell Metabol."},{"key":"10.1016\/j.redox.2020.101850_bib19","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1146\/annurev.nutr.012809.104810","article-title":"Compartmentalization of mammalian folate-mediated one-carbon metabolism","volume":"30","author":"Tibbetts","year":"2010","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.redox.2020.101850_bib20","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1016\/j.cmet.2016.04.016","article-title":"Reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway article reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway","volume":"23","author":"Ducker","year":"2016","journal-title":"Cell Metabol."},{"key":"10.1016\/j.redox.2020.101850_bib21","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.molmet.2019.05.012","article-title":"Formate metabolism in health and disease","volume":"33","author":"Pietzke","year":"2020","journal-title":"Mol. Metab."},{"key":"10.1016\/j.redox.2020.101850_bib22","series-title":"Primary Structure of a Human Trifunctional Enzyme: Isolation of a cDNA Encoding Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase-Formyltetrahydrofolate Synthetase*","author":"Hum","year":"1988"},{"key":"10.1016\/j.redox.2020.101850_bib23","doi-asserted-by":"crossref","first-page":"38381","DOI":"10.1074\/jbc.M205000200","article-title":"Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses","volume":"277","author":"Herbig","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib24","first-page":"320","article-title":"Reversible compartmentalization of de novo purine biosynthetic complexes in living cells","volume":"80","author":"An","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.redox.2020.101850_bib25","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/s41568-019-0187-8","article-title":"Methionine metabolism in health and cancer: a nexus of diet and precision medicine","volume":"19","author":"Sanderson","year":"2019","journal-title":"Nat. Rev. Canc."},{"key":"10.1016\/j.redox.2020.101850_bib26","doi-asserted-by":"crossref","first-page":"4790","DOI":"10.1074\/jbc.M111.302174","article-title":"Competition between sumoylation and ubiquitination of serine hydroxymethyltransferase 1 determines its nuclear localization and its accumulation in the nucleus","volume":"287","author":"Anderson","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib27","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/B978-0-12-380866-0.60002-2","article-title":"DNA methylation and cancer","volume":"70","author":"Kulis","year":"2010","journal-title":"Adv. Genet."},{"key":"10.1016\/j.redox.2020.101850_bib28","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/npp.2012.112","article-title":"DNA methylation and its basic function","volume":"38","author":"Moore","year":"2013","journal-title":"Neuropsychopharmacology"},{"key":"10.1016\/j.redox.2020.101850_bib29","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1038\/s41580-019-0168-5","article-title":"Reading, writing and erasing mRNA methylation","volume":"20","author":"Zaccara","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.redox.2020.101850_bib30","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/nrm3327","article-title":"Post-translational modifications: molecular mechanisms and potential functions of histone demethylases","volume":"13","author":"Kooistra","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.redox.2020.101850_bib31","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2007.02.005","article-title":"Chromatin modifications and their function","volume":"128","author":"Kouzarides","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.redox.2020.101850_bib32","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/nrg3173","article-title":"Histone methylation: a dynamic mark in health, disease and inheritance","volume":"13","author":"Greer","year":"2012","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.redox.2020.101850_bib33","doi-asserted-by":"crossref","first-page":"10822","DOI":"10.1016\/S0021-9258(19)70381-0","article-title":"S-Adenosylmethionine and S-adenosylhomocystein metabolism in isolated rat liver. Effects of L-methionine, L-homocystein, and adenosine","volume":"255","author":"Hoffman","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib34","doi-asserted-by":"crossref","first-page":"3481","DOI":"10.3390\/nu5093481","article-title":"The metabolic burden of methyl donor deficiency with focus on the betaine homocysteine methyltransferase pathway","volume":"5","author":"Obeid","year":"2013","journal-title":"Nutrients"},{"key":"10.1016\/j.redox.2020.101850_bib35","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1016\/j.bbamcr.2017.03.004","article-title":"Betaine homocysteine S-methyltransferase emerges as a new player of the nuclear methionine cycle","volume":"1864","author":"P\u00e9rez-Miguelsanz","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"10.1016\/j.redox.2020.101850_bib36","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1096\/fasebj.4.5.2407589","article-title":"Cobalamin\u2010dependent methionine synthase","volume":"4","author":"Banerjee","year":"1990","journal-title":"Faseb. J."},{"key":"10.1016\/j.redox.2020.101850_bib37","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1007\/s00018-008-8516-1","article-title":"Structure-function relationships in methionine adenosyltransferases","volume":"66","author":"Markham","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.redox.2020.101850_bib38","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1152\/physrev.00047.2011","article-title":"S-adenosylmethionine in liver health, injury, and cancer","volume":"92","author":"Lu","year":"2012","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.redox.2020.101850_bib39","doi-asserted-by":"crossref","first-page":"13528","DOI":"10.1021\/bi0615644","article-title":"Human cystathionine beta-synthase is a target for sumoylation","volume":"45","author":"Kabil","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101850_bib40","doi-asserted-by":"crossref","first-page":"13005","DOI":"10.1021\/bi001088w","article-title":"The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes","volume":"39","author":"Mosharov","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101850_bib41","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/0003-9861(80)90009-0","article-title":"Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes","volume":"204","author":"Beatty","year":"1980","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2020.101850_bib42","doi-asserted-by":"crossref","first-page":"14784","DOI":"10.1038\/s41598-019-51377-5","article-title":"Glutathione deficiency induces epigenetic alterations of vitamin D metabolism genes in the livers of high-fat diet-fed obese mice","volume":"9","author":"Parsanathan","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.redox.2020.101850_bib43","doi-asserted-by":"crossref","first-page":"29318","DOI":"10.1074\/jbc.M002725200","article-title":"Increase in plasma homocysteine associated with parallel increases in plasma S-adenosylhomocysteine and lymphocyte DNA hypomethylation","volume":"275","author":"Yi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib44","first-page":"493","article-title":"The effect of S-adenosylhomocysteine on DNA methylation in isolated rat liver nuclei","volume":"474","author":"Cox","year":"1977","journal-title":"BBA Sect. Nucleic Acids Protein Synth."},{"key":"10.1016\/j.redox.2020.101850_bib45","doi-asserted-by":"crossref","first-page":"2895","DOI":"10.1021\/pr400195u","article-title":"Disruption of DNA methylation via S-adenosylhomocysteine is a key process in high incidence liver carcinogenesis in fish","volume":"12","author":"Mirbahai","year":"2013","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.redox.2020.101850_bib46","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0261-5614(98)80304-X","article-title":"Effect of folate supplementation on DNA methylation of rectal mucosa in patients with colonic adenomas: correlation with nutrient intake","volume":"17","author":"Cravo","year":"1998","journal-title":"Clin. Nutr."},{"key":"10.1016\/j.redox.2020.101850_bib47","doi-asserted-by":"crossref","first-page":"764","DOI":"10.3389\/fgene.2019.00764","article-title":"The impact of one carbon metabolism on histone methylation","volume":"10","author":"Serefidou","year":"2019","journal-title":"Front. Genet."},{"key":"10.1016\/j.redox.2020.101850_bib48","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1126\/science.1170116","article-title":"Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1","volume":"324","author":"Tahiliani","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.redox.2020.101850_bib49","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.freeradbiomed.2018.12.009","article-title":"Dynamic regulation of epigenetic demethylation by oxygen availability and cellular redox","volume":"131","author":"Lamadema","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2020.101850_bib50","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1101\/gad.191056.112","article-title":"Inhibition of \u03b1-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors","volume":"26","author":"Xiao","year":"2012","journal-title":"Genes Dev."},{"key":"10.1016\/j.redox.2020.101850_bib51","doi-asserted-by":"crossref","DOI":"10.1186\/gb-2001-2-3-research0007","article-title":"The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases","volume":"2","author":"Aravind","year":"2001","journal-title":"Genome Biol."},{"key":"10.1016\/j.redox.2020.101850_bib52","doi-asserted-by":"crossref","first-page":"20734","DOI":"10.1074\/jbc.R115.656462","article-title":"The AlkB family of Fe(II)\/\u03b1-ketoglutarate-dependent dioxygenases: repairing nucleic acid alkylation damage and beyond","volume":"290","author":"Fedeles","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib53","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.cell.2004.12.012","article-title":"Histone demethylation mediated by the nuclear amine oxidase homolog LSD1","volume":"119","author":"Shi","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.redox.2020.101850_bib54","doi-asserted-by":"crossref","first-page":"4750","DOI":"10.1021\/bi200247b","article-title":"Histone demethylase LSD1 is a folate-binding protein","volume":"50","author":"Luka","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101850_bib55","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1101\/gad.276568.115","article-title":"Role of TET enzymes in DNA methylation, development, and cancer","volume":"30","author":"Rasmussen","year":"2016","journal-title":"Genes Dev."},{"key":"10.1016\/j.redox.2020.101850_bib56","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.cell.2018.09.041","article-title":"Mitochondrial one-carbon pathway supports cytosolic folate integrity in cancer cells","volume":"175","author":"Zheng","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.redox.2020.101850_bib57","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1111\/j.1471-4159.1978.tb07059.x","article-title":"Dihydrofolate reductase is present in brain","volume":"30","author":"Pollock","year":"1978","journal-title":"J. Neurochem."},{"key":"10.1016\/j.redox.2020.101850_bib58","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1016\/j.bbadis.2011.12.001","article-title":"Role of peroxisomes in ROS\/RNS-metabolism: implications for human disease","volume":"1822","author":"Fransen","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.redox.2020.101850_bib59","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.freeradbiomed.2015.02.011","article-title":"A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1","volume":"83","author":"Ramming","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2020.101850_bib60","doi-asserted-by":"crossref","first-page":"2203","DOI":"10.1016\/j.febslet.2005.03.015","article-title":"Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process","volume":"579","author":"Forneris","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1016\/j.redox.2020.101850_bib61","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1042\/bj1280617","article-title":"The cellular production of hydrogen peroxide","volume":"128","author":"Boveris","year":"1972","journal-title":"Biochem. J."},{"key":"10.1016\/j.redox.2020.101850_bib62","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.cotox.2018.07.001","article-title":"Formaldehyde metabolism and its impact on human health","volume":"9","author":"Reingruber","year":"2018","journal-title":"Curr. Opin. Toxicol."},{"key":"10.1016\/j.redox.2020.101850_bib63","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S0378-4347(00)00552-1","article-title":"Determination of formaldehyde in blood plasma by high-performance liquid chromatography with fluorescence detection","volume":"753","author":"Luo","year":"2001","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"10.1016\/j.redox.2020.101850_bib64","first-page":"1","article-title":"IARC working group on the evaluation of carcinogenic risks to humans., formaldehyde, 2-butoxyethanol and 1-tert-Butoxypropan-2-ol","volume":"88","year":"2006","journal-title":"IARC Work. Gr. Eval. Carcinog. Risks to Humans"},{"key":"10.1016\/j.redox.2020.101850_bib65","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3389\/fenvs.2014.00036","article-title":"Genotoxicity of formaldehyde: molecular basis of DNA damage and mutation","volume":"2","author":"Kawanishi","year":"2014","journal-title":"Front. Environ. Sci. ."},{"key":"10.1016\/j.redox.2020.101850_bib66","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/s42004-020-0324-z","article-title":"Amino acid dependent formaldehyde metabolism in mammals","volume":"3","author":"Pietzke","year":"2020","journal-title":"Commun. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib67","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1038\/nsmb.2173","article-title":"Formaldehyde catabolism is essential in cells deficient for the Fanconi anemia DNA-repair pathway","volume":"18","author":"Rosado","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.redox.2020.101850_bib68","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1093\/toxsci\/kfq061","article-title":"Distribution of DNA adducts caused by inhaled formaldehyde is consistent with induction of nasal carcinoma but not leukemia","volume":"116","author":"Lu","year":"2010","journal-title":"Toxicol. Sci."},{"key":"10.1016\/j.redox.2020.101850_bib69","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.molcel.2016.09.031","article-title":"Mechanism and regulation of DNA-protein crosslink repair by the DNA-dependent metalloprotease SPRTN","volume":"64","author":"Stingele","year":"2016","journal-title":"Mol. Cell."},{"key":"10.1016\/j.redox.2020.101850_bib70","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1016\/j.cell.2017.05.010","article-title":"A class of environmental and endogenous toxins induces BRCA2 haploinsufficiency and genome instability","volume":"169","author":"Tan","year":"2017","journal-title":"Cell"},{"issue":"6","key":"10.1016\/j.redox.2020.101850_bib71","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1016\/j.molcel.2020.10.012","article-title":"Two aldehyde clearance systems are essential to prevent lethal formaldehyde accumulation in mice and humans","volume":"80","author":"Dingler","year":"2020","journal-title":"Mol. Cell."},{"key":"10.1016\/j.redox.2020.101850_bib72","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1016\/S0140-6736(81)91172-7","article-title":"Aldehyde ehydrogenase deficiency as cause of facial flushing reaction to alcohol in Japanese","volume":"318","author":"Harada","year":"1981","journal-title":"Lancet"},{"key":"10.1016\/j.redox.2020.101850_bib73","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1124\/dmd.30.1.69","article-title":"Effects of aldehyde dehydrogenase-2 genetic polymorphisms on metabolism of structurally different aldehydes in human liver","volume":"30","author":"Wang","year":"2002","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.redox.2020.101850_bib74","doi-asserted-by":"crossref","first-page":"5851","DOI":"10.1016\/S0021-9258(18)96350-7","article-title":"The mechanism of the condensation of formaldehyde with tetrahydrofolic acid","volume":"241","author":"Kallen","year":"1966","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101850_bib75","doi-asserted-by":"crossref","DOI":"10.3390\/metabo10020065","article-title":"Vivo rate of formaldehyde condensation with tetrahydrofolate","volume":"10","author":"He","year":"2020","journal-title":"Metabolites"},{"key":"10.1016\/j.redox.2020.101850_bib76","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/nchembio.1142","article-title":"Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis","volume":"9","author":"Morgan","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.redox.2020.101850_bib77","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1021\/bi201785u","article-title":"Mechanism of inhibition for N6022, a first-in-class drug targeting S-nitrosoglutathione reductase","volume":"51","author":"Green","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101850_bib78","doi-asserted-by":"crossref","first-page":"429","DOI":"10.3181\/00379727-97-23764","article-title":"Inhibition of dihydrofolic reductase by aminopterin and amethopterin","volume":"97","author":"Osborn","year":"1958","journal-title":"Proc. Soc. Exp. Biol. Med."}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231720310557?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231720310557?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T06:16:56Z","timestamp":1761977816000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231720310557"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4]]},"references-count":78,"alternative-id":["S2213231720310557"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2020.101850","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2021,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The toxic side of one-carbon metabolism and epigenetics","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2020.101850","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"101850"}}