{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,2]],"date-time":"2026-11-02T21:58:19Z","timestamp":1793656699208,"version":"4.5.1"},"reference-count":92,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["Z01-ES050159"],"award-info":[{"award-number":["Z01-ES050159"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["DNA Repair"],"published-print":{"date-parts":[[2021,9]]},"DOI":"10.1016\/j.dnarep.2021.103134","type":"journal-article","created":{"date-parts":[[2021,5,11]],"date-time":"2021-05-11T13:21:25Z","timestamp":1620739285000},"page":"103134","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"special_numbering":"C","title":["Perspectives on formaldehyde dysregulation: Mitochondrial DNA damage and repair in mammalian cells"],"prefix":"10.1016","volume":"105","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4721-6904","authenticated-orcid":false,"given":"Cristina A.","family":"Nadalutti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajendra","family":"Prasad","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel H.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.dnarep.2021.103134_bib0005","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/0092-8674(92)90611-F","article-title":"Targeted mutation of the DNA methyltransferase gene results in embryonic lethality","volume":"69","author":"Li","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0010","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0092-8674(00)81656-6","article-title":"DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development","volume":"99","author":"Okano","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0015","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.cbi.2011.01.017","article-title":"Metabolic mechanisms of methanol\/formaldehyde in isolated rat hepatocytes: carbonyl-metabolizing enzymes versus oxidative stress","volume":"191","author":"MacAllister","year":"2011","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.dnarep.2021.103134_bib0020","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1152\/physrev.00034.2014","article-title":"Metabolic methanol: molecular pathways and physiological roles","volume":"95","author":"Dorokhov","year":"2015","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.dnarep.2021.103134_bib0025","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1111\/j.1471-4159.1976.tb07001.x","article-title":"Regional and subcellular distribution of protein carboxymethylase in brain and other tissues","volume":"26","author":"Diliberto","year":"1976","journal-title":"J. Neurochem."},{"key":"10.1016\/j.dnarep.2021.103134_bib0030","first-page":"315","article-title":"Kinetics and mechanism of methanol and formaldehyde interconversion and formaldehyde oxidation catalyzed by liver alcohol dehydrogenase","author":"Pocker","year":"1991","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0035","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/S0021-9258(18)81367-9","article-title":"Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase","volume":"237","author":"Frisell","year":"1962","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.dnarep.2021.103134_bib0040","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1093\/carcin\/9.1.65","article-title":"Role of formaldehyde hydrazone and catalase in hydrazine-induced methylation of DNA guanine","volume":"9","author":"Lambert","year":"1988","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.dnarep.2021.103134_bib0045","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1016\/0024-3205(91)90504-5","article-title":"The toxicity of methanol","volume":"48","author":"Tephly","year":"1991","journal-title":"Life Sci."},{"key":"10.1016\/j.dnarep.2021.103134_bib0050","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1080\/713857189","article-title":"Toxicological and metabolic consequences of methanol poisoning","volume":"13","author":"Skrzydlewska","year":"2003","journal-title":"Toxicol. Mech. Methods"},{"key":"10.1016\/j.dnarep.2021.103134_bib0055","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.reprotox.2010.09.014","article-title":"Species- and strain-dependent teratogenicity of methanol in rabbits and mice","volume":"31","author":"Sweeting","year":"2011","journal-title":"Reprod. Toxicol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0060","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.jinsphys.2009.10.010","article-title":"Methanol metabolism in the Asian corn borer, Ostrinia furnacalis (Guenee) (Lepidoptera: Pyralidae)","volume":"56","author":"Guo","year":"2010","journal-title":"J. Insect Physiol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0065","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1002\/arch.21021","article-title":"The involvement of cytochrome P450 monooxygenases in methanol elimination in Drosophila melanogaster larvae","volume":"79","author":"Wang","year":"2012","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0070","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/6525474","article-title":"The effects of formaldehyde on cytochrome P450 isoform activity in rats","author":"Xu","year":"2017","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.dnarep.2021.103134_bib0075","first-page":"393","article-title":"Formaldehyde-mediated chronic damage may be related to sporadic neurodegeneration","volume":"35","author":"Li","year":"2008","journal-title":"Prog. Biochem. Biophys."},{"key":"10.1016\/j.dnarep.2021.103134_bib0080","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-11289-8","article-title":"Evidence that endogenous formaldehyde produces immunogenic and atherogenic adduct epitopes","volume":"7","author":"Nakamura","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.dnarep.2021.103134_bib0085","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0300-483X(92)90067-O","article-title":"Methylamine metabolism to formaldehyde by vascular semicarbazide-sensitive amine oxidase","volume":"73","author":"Boor","year":"1992","journal-title":"Toxicology"},{"key":"10.1016\/j.dnarep.2021.103134_bib0090","doi-asserted-by":"crossref","first-page":"594","DOI":"10.2337\/diab.42.4.594","article-title":"Oxidative deamination of methylamine by semicarbazide-sensitive amine oxidase leads to cytotoxic damage in endothelial-cells - possible consequences for diabetes","volume":"42","author":"Yu","year":"1993","journal-title":"Diabetes"},{"key":"10.1016\/j.dnarep.2021.103134_bib0095","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.lfs.2006.01.017","article-title":"Diabetes and semicarbazide-sensitive amine oxidase (SSAO) activity: a review","volume":"79","author":"Obata","year":"2006","journal-title":"Life Sci."},{"key":"10.1016\/j.dnarep.2021.103134_bib0100","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1054\/mehy.2001.1329","article-title":"Involvement of cerebrovascular semicarbazide-sensitive amine oxidase in the pathogenesis of Alzheimer\u2019s disease and vascular dementia","volume":"57","author":"Yu","year":"2001","journal-title":"Med. Hypotheses"},{"key":"10.1016\/j.dnarep.2021.103134_bib0105","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S1570-9639(03)00101-8","article-title":"Physiological and pathological implications of semicarbazide-sensitive amine oxidase","volume":"1647","author":"Yu","year":"2003","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"10.1016\/j.dnarep.2021.103134_bib0110","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/S0161-813X(03)00117-7","article-title":"Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do","volume":"25","author":"O\u2019Sullivan","year":"2004","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.dnarep.2021.103134_bib0115","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S1570-0232(04)00655-5","article-title":"Assay of plasma semicarbazide-sensitive amine oxidase and determination of its endogenous substrate methylamine by liquid chromatography","volume":"810","author":"Li","year":"2004","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"10.1016\/j.dnarep.2021.103134_bib0120","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1161\/ATVBAHA.107.153130","article-title":"VAP-1 and CD73, endothelial cell surface enzymes in leukocyte extravasation","volume":"28","author":"Jalkanen","year":"2008","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0125","doi-asserted-by":"crossref","first-page":"309","DOI":"10.33549\/physiolres.931982","article-title":"Monoamine oxidase and semicarbazide-sensitive amine oxidase kinetic analysis in mesenteric arteries of patients with type 2 diabetes","volume":"60","author":"Nunes","year":"2011","journal-title":"Physiol. Res."},{"key":"10.1016\/j.dnarep.2021.103134_bib0130","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1124\/jpet.107.124123","article-title":"Evidence for in vivo scavenging by aminoguanidine of formaldehyde produced via semicarbazide-sensitive amine oxidase-mediated deamination","volume":"322","author":"Kazachkov","year":"2007","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.dnarep.2021.103134_bib0135","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1172\/JCI119176","volume":"99","author":"Anderson","year":"1997","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.dnarep.2021.103134_bib0140","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.dnarep.2021.103134_bib0145","doi-asserted-by":"crossref","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.dnarep.2021.103134_bib0150","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/s00775-004-0622-4","article-title":"The intrinsic axial ligand effect on propene oxidation by horseradish peroxidase versus cytochrome P450 enzymes","volume":"10","author":"Kumar","year":"2005","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.dnarep.2021.103134_bib0155","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.pharmthera.2012.12.007","article-title":"Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation","volume":"138","author":"Zanger","year":"2013","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.dnarep.2021.103134_bib0160","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.neubiorev.2014.05.011","article-title":"Consequences of psychophysiological stress on cytochrome P450-catalyzed drug metabolism","volume":"45","author":"Konstandi","year":"2014","journal-title":"Neurosci. Biobehav. Rev."},{"key":"10.1016\/j.dnarep.2021.103134_bib0165","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1007\/PL00000897","article-title":"Cytochromes P450 and metabolism of xenobiotics","volume":"58","author":"Anzenbacher","year":"2001","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.dnarep.2021.103134_bib0170","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1016\/j.redox.2014.09.007","article-title":"Methodology to assay CYP2E1 mixed function oxidase catalytic activity and its induction","volume":"2","author":"Cederbaum","year":"2014","journal-title":"Redox Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0175","doi-asserted-by":"crossref","first-page":"20818","DOI":"10.1074\/jbc.RA117.000220","article-title":"Structural and functional effects of cytochrome b(5) interactions with human cytochrome P450 enzymes","volume":"292","author":"Bart","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.dnarep.2021.103134_bib0180","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.00089","article-title":"The role of cytochromes P450 in infection","volume":"9","author":"Stavropoulou","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0185","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.dnarep.2021.103134_bib0190","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.dnarep.2021.103134_bib0195","doi-asserted-by":"crossref","first-page":"3276","DOI":"10.1021\/bi00634a002","article-title":"Formaldehyde as a probe of DNA structure. 4. Mechanism of the initial reaction of formaldehyde with DNA","volume":"16","author":"McGhee","year":"1977","journal-title":"Biochemistry"},{"key":"10.1016\/j.dnarep.2021.103134_bib0200","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1021\/ja808048c","article-title":"Formation of S-[1-(N2-deoxyguanosinyl)methyl]glutathione between glutathione and DNA induced by formaldehyde","volume":"131","author":"Lu","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.dnarep.2021.103134_bib0205","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1586\/erv.12.38","article-title":"Inactivated virus vaccines from chemistry to prophylaxis: merits, risks and challenges","volume":"11","author":"Delrue","year":"2012","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.dnarep.2021.103134_bib0210","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1126\/science.6828890","article-title":"Formaldehyde damage to DNA and inhibition of DNA-repair in human bronchial cells","volume":"220","author":"Grafstrom","year":"1983","journal-title":"Science"},{"key":"10.1016\/j.dnarep.2021.103134_bib0215","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.dnarep.2015.02.010","article-title":"BLM protein mitigates formaldehyde-induced genomic instability","volume":"28","author":"Kumari","year":"2015","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0220","doi-asserted-by":"crossref","first-page":"65","DOI":"10.3103\/S0095452717010078","article-title":"Formaldehyde induces DNA strand breaks on spermatozoa and lymphocytes of wistar rats","volume":"51","author":"J.V. J","year":"2017","journal-title":"Cytol. Genet."},{"key":"10.1016\/j.dnarep.2021.103134_bib0225","doi-asserted-by":"crossref","first-page":"5575","DOI":"10.1038\/s41598-020-61477-2","article-title":"Mitochondrial dysfunction and DNA damage accompany enhanced levels of formaldehyde in cultured primary human fibroblasts","volume":"10","author":"Nadalutti","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.dnarep.2021.103134_bib0230","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1038\/s41586-018-0448-9","article-title":"Parkin and PINK1 mitigate STING-induced inflammation","volume":"561","author":"Sliter","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.dnarep.2021.103134_bib0235","doi-asserted-by":"crossref","first-page":"3053","DOI":"10.1093\/nar\/gkh634","article-title":"Twinkle and POLG defects enhance age-dependent accumulation of mutations in the control region of mtDNA","volume":"32","author":"Wanrooij","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.dnarep.2021.103134_bib0240","doi-asserted-by":"crossref","first-page":"2539","DOI":"10.1093\/nar\/gkp100","article-title":"Oxidative stress induces degradation of mitochondrial DNA","volume":"37","author":"Shokolenko","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.dnarep.2021.103134_bib0245","doi-asserted-by":"crossref","first-page":"3034","DOI":"10.1093\/nar\/gky094","article-title":"Structural rearrangements in the mitochondrial genome of Drosophila melanogaster induced by elevated levels of the replicative DNA helicase","volume":"46","author":"Nadalutti","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.dnarep.2021.103134_bib0250","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.freeradbiomed.2016.11.025","article-title":"Risky repair: DNA-protein crosslinks formed by mitochondrial base excision DNA repair enzymes acting on free radical lesions","volume":"107","author":"Caston","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.dnarep.2021.103134_bib0255","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/j.bbagrm.2012.06.002","article-title":"Mitochondrial DNA damage and its consequences for mitochondrial gene expression","volume":"1819","author":"Cline","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.dnarep.2021.103134_bib0260","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.mrfmmm.2010.12.007","article-title":"Repair and biochemical effects of DNA-protein crosslinks","volume":"711","author":"Ide","year":"2011","journal-title":"Mutat. Res."},{"key":"10.1016\/j.dnarep.2021.103134_bib0265","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.cell.2014.09.024","article-title":"Repair of a DNA-protein crosslink by replication-coupled proteolysis","volume":"159","author":"Duxin","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0270","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.cell.2018.10.053","article-title":"The CMG helicase bypasses DNA-protein cross-links to facilitate their repair","volume":"176","author":"Sparks","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0275","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.cell.2014.04.053","article-title":"A DNA-dependent protease involved in DNA-protein crosslink repair","volume":"158","author":"Stingele","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0280","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.21491","article-title":"SPRTN is a mammalian DNA-binding metalloprotease that resolves DNA-protein crosslinks","volume":"5","author":"Lopez-Mosqueda","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.dnarep.2021.103134_bib0285","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.dnarep.2021.103134_bib0290","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/nrm.2017.56","article-title":"Mechanisms of DNA-protein crosslink repair","volume":"18","author":"Stingele","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0295","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.bbrc.2010.11.094","article-title":"Repair pathways independent of the Fanconi anemia nuclear core complex play a predominant role in mitigating formaldehyde-induced DNA damage","volume":"404","author":"Noda","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.dnarep.2021.103134_bib0300","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.dnarep.2021.103134_bib0305","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1007\/s00294-020-01057-z","article-title":"Genetic investigation of formaldehyde-induced DNA damage response in Schizosaccharomyces pombe","volume":"66","author":"Anandarajan","year":"2020","journal-title":"Curr. Genet."},{"key":"10.1016\/j.dnarep.2021.103134_bib0310","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0003-9861(69)90344-0","article-title":"Inhibition by formaldehyde of energy transfer and related processes in rat liver mitochondria. II. Effects on energy-linked reactions in intact mitochondria and phosphorylating particles","volume":"132","author":"Van Buskirk","year":"1969","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.dnarep.2021.103134_bib0315","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/s10565-015-9309-6","article-title":"Effects of formaldehyde on mitochondrial dysfunction and apoptosis in SK-N-SH neuroblastoma cells","volume":"31","author":"Zerin","year":"2015","journal-title":"Cell Biol. Toxicol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0320","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2020.102824","article-title":"Requirements for PARP-1 covalent crosslinking to DNA (PARP-1 DPC)","volume":"89","author":"Prasad","year":"2020","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0325","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2020.102822","article-title":"Function and evolution of the DNA-protein crosslink proteases Wss1 and SPRTN","volume":"88","author":"Reinking","year":"2020","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0330","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2020.102837","article-title":"Excision repair of topoisomerase DNA-protein crosslinks (TOP-DPC)","volume":"89","author":"Sun","year":"2020","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0335","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2019.102773","article-title":"Oxidative DNA-protein crosslinks formed in mammalian cells by abasic site lyases involved in DNA repair","volume":"87","author":"Qui\u00f1ones","year":"2020","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0340","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2016.12.014","article-title":"Single-molecule analysis of mtDNA replication uncovers the basis of the common deletion","volume":"65","author":"Phillips","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0345","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0176795","article-title":"Selective mitochondrial DNA degradation following double-strand breaks","volume":"12","author":"Moretton","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.dnarep.2021.103134_bib0350","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/bs.enz.2019.08.004","article-title":"Mitochondrial DNA degradation: a quality control measure for mitochondrial genome maintenance and stress response","volume":"45","author":"Zhao","year":"2019","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0355","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1189\/jlb.0703328","article-title":"Endogenously oxidized mitochondrial DNA induces in vivo and in vitro inflammatory responses","volume":"75","author":"Collins","year":"2004","journal-title":"J. Leukoc. Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0360","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.4049\/jimmunol.1203162","article-title":"Molecular basis of DNA recognition in the immune system","volume":"190","author":"Atianand","year":"2013","journal-title":"J. Immunol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0365","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1042\/ETLS20170063","article-title":"TREX1 is a checkpoint for innate immune sensing of DNA damage that fosters cancer immune resistance","volume":"1","author":"Demaria","year":"2017","journal-title":"Emerg. Top. Life Sci."},{"key":"10.1016\/j.dnarep.2021.103134_bib0370","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.2005653","article-title":"Structural basis for overhang excision and terminal unwinding of DNA duplexes by TREX1","volume":"16","author":"Huang","year":"2018","journal-title":"PLoS Biol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0375","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/bs.apcsb.2018.11.004","article-title":"Mechanistic link between DNA damage sensing, repairing and signaling factors and immune signaling","volume":"115","author":"Mukherjee","year":"2019","journal-title":"DNA Repair"},{"key":"10.1016\/j.dnarep.2021.103134_bib0380","doi-asserted-by":"crossref","first-page":"5117","DOI":"10.1073\/pnas.1423804112","article-title":"Exonuclease TREX1 degrades double-stranded DNA to prevent spontaneous lupus-like inflammatory disease","volume":"112","author":"Grieves","year":"2015","journal-title":"PNAS"},{"key":"10.1016\/j.dnarep.2021.103134_bib0385","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.mad.2006.12.005","article-title":"WRN exonuclease activity is blocked by DNA termini harboring 3\u2019 obstructive groups","volume":"128","author":"Harrigan","year":"2007","journal-title":"Mech. Ageing Dev."},{"key":"10.1016\/j.dnarep.2021.103134_bib0390","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev-immunol-042718-041257","article-title":"Self-awareness: nucleic acid\u2013driven inflammation and the type I interferonopathies","volume":"37","author":"Uggenti","year":"2019","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0395","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1084\/jem.20180783","article-title":"N-glycanase NGLY1 regulates mitochondrial homeostasis and inflammation through NRF1","volume":"215","author":"Yang","year":"2018","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.dnarep.2021.103134_bib0400","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1038\/s42255-019-0150-8","article-title":"Mitochondrial DNA stress signalling protects the nuclear genome","volume":"1","author":"Wu","year":"2019","journal-title":"Nat. Metab."},{"key":"10.1016\/j.dnarep.2021.103134_bib0405","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/nature14156","article-title":"Mitochondrial DNA stress primes the antiviral innate immune response","volume":"520","author":"West","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.dnarep.2021.103134_bib0410","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1038\/s41586-018-0372-z","article-title":"New mitochondrial DNA synthesis enables NLRP3 inflammasome activation","volume":"560","author":"Zhong","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.dnarep.2021.103134_bib0415","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nri2975","article-title":"Mitochondria in innate immune responses","volume":"11","author":"West","year":"2011","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0420","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s10048-020-00609-2","article-title":"Loss of mitochondrial ClpP, Lonp1, and Tfam triggers transcriptional induction of Rnf213, a susceptibility factor for moyamoya disease","volume":"21","author":"Key","year":"2020","journal-title":"Neurogenetics"},{"key":"10.1016\/j.dnarep.2021.103134_bib0425","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201949799","article-title":"Mitochondrial DNA in inflammation and immunity","volume":"21","author":"Riley","year":"2020","journal-title":"EMBO Rep."},{"key":"10.1016\/j.dnarep.2021.103134_bib0430","doi-asserted-by":"crossref","DOI":"10.1021\/acs.chemrestox.0c00083","article-title":"Mitochondrial DNA damage: prevalence, biological consequence, and emerging pathways","author":"Zhao","year":"2020","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.dnarep.2021.103134_bib0435","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/jnc.12356","article-title":"Formaldehyde in brain: an overlooked player in neurodegeneration?","volume":"127","author":"Tulpule","year":"2013","journal-title":"J. Neurochem."},{"key":"10.1016\/j.dnarep.2021.103134_bib0440","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1111\/acel.12345","article-title":"Aging-associated formaldehyde-induced norepinephrine deficiency contributes to age-related memory decline","volume":"14","author":"Mei","year":"2015","journal-title":"Aging Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0445","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.molcel.2014.07.010","article-title":"Maternal aldehyde elimination during pregnancy preserves the fetal genome","volume":"55","author":"Oberbeck","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.dnarep.2021.103134_bib0450","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s41021-020-00160-4","article-title":"The failure of two major formaldehyde catabolism enzymes (ADH5 and ALDH2) leads to partial synthetic lethality in C57BL\/6 mice","volume":"42","author":"Nakamura","year":"2020","journal-title":"Genes Environ."},{"key":"10.1016\/j.dnarep.2021.103134_bib0455","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abd7197","article-title":"Digenic mutations in ALDH2 and ADH5 impair formaldehyde clearance and cause a multisystem disorder, AMeD syndrome","volume":"6","author":"Oka","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.dnarep.2021.103134_bib0460","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/j.molcel.2020.11.040","article-title":"A surge of DNA damage links transcriptional reprogramming and hematopoietic deficit in fanconi Anemia","volume":"80","author":"Shen","year":"2020","journal-title":"Mol. Cell"}],"container-title":["DNA Repair"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1568786421000902?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1568786421000902?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T20:51:45Z","timestamp":1761598305000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1568786421000902"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9]]},"references-count":92,"alternative-id":["S1568786421000902"],"URL":"https:\/\/doi.org\/10.1016\/j.dnarep.2021.103134","relation":{},"ISSN":["1568-7864"],"issn-type":[{"value":"1568-7864","type":"print"}],"subject":[],"published":{"date-parts":[[2021,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Perspectives on formaldehyde dysregulation: Mitochondrial DNA damage and repair in mammalian cells","name":"articletitle","label":"Article Title"},{"value":"DNA Repair","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.dnarep.2021.103134","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"103134"}}