{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T05:26:34Z","timestamp":1778304394051,"version":"3.51.4"},"reference-count":73,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.abb.2025.110636","type":"journal-article","created":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T00:31:33Z","timestamp":1759797093000},"page":"110636","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Mitochondrial redox imbalance and CoQ10 deficiency in Rett syndrome: Insights from patient-derived fibroblasts"],"prefix":"10.1016","volume":"774","author":[{"given":"Francesco","family":"Mengarelli","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valeria","family":"Cordone","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessandra","family":"Pecorelli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mascia","family":"Benedusi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giuseppe","family":"Valacchi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Camilla","family":"Morresi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tiziana","family":"Bacchetti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patrick","family":"Orlando","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luca","family":"Tiano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sonia","family":"Silvestri","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"Pt 2","key":"10.1016\/j.abb.2025.110636_bib1","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.neubiorev.2014.01.012","article-title":"Mitochondrial dysfunction as a central actor in intellectual disability-related diseases: An overview of Down syndrome, autism, Fragile X and Rett syndrome","volume":"46","author":"Valenti","year":"2014","journal-title":"Neurosci. Biobehav. Rev."},{"issue":"5","key":"10.1016\/j.abb.2025.110636_bib2","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1002\/humu.10194","article-title":"RettBASE: The IRSA MECP2 variation database-a new mutation database in evolution","volume":"21","author":"Christodoulou","year":"2003","journal-title":"Hum. Mutat."},{"issue":"Pt A","key":"10.1016\/j.abb.2025.110636_bib3","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.freeradbiomed.2015.04.019","article-title":"Exploring the possible link between MeCP2 and oxidative stress in Rett syndrome","volume":"88","author":"Filosa","year":"2015","journal-title":"Free Radic. Biol. Med."},{"issue":"34","key":"10.1016\/j.abb.2025.110636_bib4","first-page":"32181","article-title":"Chromatin compaction by human MeCP2. Assembly of novel secondary chromatin structures in the absence of DNA methylation","volume":"278","author":"T Georgel","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"49","key":"10.1016\/j.abb.2025.110636_bib5","doi-asserted-by":"crossref","first-page":"17551","DOI":"10.1073\/pnas.0507856102","article-title":"Regulation of RNA splicing by the methylation-dependent transcriptional repressor methyl-CpG binding protein 2","volume":"102","author":"Young","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"5880","key":"10.1016\/j.abb.2025.110636_bib6","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1126\/science.1153252","article-title":"MeCP2, a key contributor to neurological disease, activates and represses transcription","volume":"320","author":"Chahrour","year":"2008","journal-title":"Science"},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib7","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.molcel.2010.01.030","article-title":"Neuronal MeCP2 is expressed at near histone-octamer levels and globally alters the chromatin state","volume":"37","author":"Skene","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.abb.2025.110636_bib8","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/5694058","article-title":"Lactonase activity and lipoprotein-phospholipase A2 as possible novel serum biomarkers for the differential diagnosis of autism spectrum disorders and Rett syndrome: results from a pilot study","volume":"2017","author":"Hayek","year":"2017","journal-title":"Oxid. Med. Cell. Longev."},{"issue":"8","key":"10.1016\/j.abb.2025.110636_bib9","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1097\/00005072-199708000-00001","article-title":"Review of Rett syndrome","volume":"56","author":"Armstrong","year":"1997","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib10","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.autrev.2016.01.011","article-title":"Rett syndrome: An autoimmune disease?","volume":"15","author":"De Felice","year":"2016","journal-title":"Autoimmun. Rev."},{"issue":"Pt B","key":"10.1016\/j.abb.2025.110636_bib11","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.biocel.2016.07.015","article-title":"OxInflammation in Rett syndrome","volume":"81","author":"Pecorelli","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.abb.2025.110636_bib12","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.freeradbiomed.2020.02.023","article-title":"Compromised immune\/inflammatory responses in Rett syndrome","volume":"152","author":"Pecorelli","year":"2020","journal-title":"Free Radic. Biol. Med."},{"issue":"5","key":"10.1016\/j.abb.2025.110636_bib13","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S0387-7604(87)80079-7","article-title":"Reduced concentrations of ascorbic acid and glutathione in a single case of Rett syndrome: A postmortem brain study","volume":"9","author":"Sofi\u0107","year":"1987","journal-title":"Brain Dev."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib14","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.bbagen.2011.12.002","article-title":"Morphological changes and oxidative damage in Rett Syndrome erythrocytes","volume":"1820","author":"Ciccoli","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.abb.2025.110636_bib15","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0022-510X(98)00035-5","article-title":"Vitamin E serum levels in Rett syndrome","volume":"156","author":"Formichi","year":"1998","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.abb.2025.110636_bib16","first-page":"236","article-title":"Oxidative stress in Rett syndrome","volume":"23","author":"Sierra","year":"2001","journal-title":"B & D (Brain & Dev.)"},{"issue":"100","key":"10.1016\/j.abb.2025.110636_bib17","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.nbd.2014.04.006","article-title":"Oxidative brain damage in Mecp2-mutant murine models of Rett syndrome","volume":"68","author":"De Felice","year":"2014","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.abb.2025.110636_bib18","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/195935","article-title":"Redox imbalance and morphological changes in skin fibroblasts in typical Rett syndrome","volume":"2014","author":"Signorini","year":"2014","journal-title":"Oxid. Med. Cell. Longev."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib19","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/j.freeradbiomed.2009.05.016","article-title":"Systemic oxidative stress in classic Rett syndrome","volume":"47","author":"De Felice","year":"2009","journal-title":"Free Radic. Biol. Med."},{"issue":"12","key":"10.1016\/j.abb.2025.110636_bib20","doi-asserted-by":"crossref","first-page":"2287","DOI":"10.1194\/jlr.P017798","article-title":"F2-dihomo-isoprostanes as potential early biomarkers of lipid oxidative damage in Rett syndrome","volume":"52","author":"De Felice","year":"2011","journal-title":"J. Lipid Res."},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib21","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1007\/s12263-012-0285-7","article-title":"Partial rescue of Rett syndrome by \u03c9-3 polyunsaturated fatty acids (PUFAs) oil","volume":"7","author":"De Felice","year":"2012","journal-title":"Gene Nutr."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib22","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1179\/1351000211Y.0000000004","article-title":"Oxidative stress in Rett syndrome: natural history, genotype, and variants","volume":"16","author":"Leoncini","year":"2011","journal-title":"Redox Rep."},{"issue":"5\u20136","key":"10.1016\/j.abb.2025.110636_bib23","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.clinbiochem.2011.01.007","article-title":"Increased levels of 4HNE-protein plasma adducts in Rett syndrome","volume":"44","author":"Pecorelli","year":"2011","journal-title":"Clin. Biochem."},{"issue":"15\u201316","key":"10.1016\/j.abb.2025.110636_bib24","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1016\/j.cca.2011.04.016","article-title":"F4-neuroprostanes mediate neurological severity in Rett syndrome","volume":"412","author":"Signorini","year":"2011","journal-title":"Clin. Chim. Acta"},{"issue":"14","key":"10.1016\/j.abb.2025.110636_bib25","doi-asserted-by":"crossref","first-page":"2199","DOI":"10.1016\/j.febslet.2013.05.042","article-title":"Scavenger receptor B1 post-translational modifications in Rett syndrome","volume":"587","author":"Sticozzi","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2025.110636_bib26","doi-asserted-by":"crossref","first-page":"E1","DOI":"10.1111\/j.1749-6632.2011.06205.x","article-title":"Scavenger receptor class B type I: a multifunctional receptor","volume":"1229","author":"Valacchi","year":"2011","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"9","key":"10.1016\/j.abb.2025.110636_bib27","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/ng.2714","article-title":"A suppressor screen in Mecp2 mutant mice implicates cholesterol metabolism in Rett syndrome","volume":"45","author":"Buchovecky","year":"2013","journal-title":"Nat. Genet."},{"issue":"8","key":"10.1016\/j.abb.2025.110636_bib28","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0104834","article-title":"Cholesterol metabolism is altered in Rett syndrome: a study on plasma and primary cultured fibroblasts derived from patients","volume":"9","author":"Segatto","year":"2014","journal-title":"PLoS One"},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib29","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/S0387-7604(88)80010-X","article-title":"Abnormal mitochondria in the Rett syndrome","volume":"10","author":"Eeg-Olofsson","year":"1988","journal-title":"Brain Dev."},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib30","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1177\/088307389000500311","article-title":"Rett syndrome: a mitochondrial disease?","volume":"5","author":"Eeg-Olofsson","year":"1990","journal-title":"J. Child Neurol."},{"issue":"5","key":"10.1016\/j.abb.2025.110636_bib31","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/0887-8994(89)90027-1","article-title":"Mitochondrial alterations in Rett syndrome","volume":"5","author":"Ruch","year":"1989","journal-title":"Pediatr. Neurol."},{"issue":"5","key":"10.1016\/j.abb.2025.110636_bib32","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0887-8994(90)90028-Y","article-title":"Rett syndrome: findings suggesting axonopathy and mitochondrial abnormalities","volume":"6","author":"Wakai","year":"1990","journal-title":"Pediatr. Neurol."},{"issue":"1","key":"10.1016\/j.abb.2025.110636_bib33","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.nbd.2012.06.007","article-title":"Oxidative burden and mitochondrial dysfunction in a mouse model of Rett syndrome","volume":"48","author":"Grosser","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.abb.2025.110636_bib34","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.mito.2014.02.012","article-title":"Mitochondrial dysfunction in the skeletal muscle of a mouse model of Rett syndrome (RTT): implications for the disease phenotype","volume":"15","author":"Gold","year":"2014","journal-title":"Mitochondrion"},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib35","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1002\/cne.22009","article-title":"Widespread changes in dendritic and axonal morphology in Mecp2-mutant mouse models of Rett syndrome: evidence for disruption of neuronal networks","volume":"514","author":"Belichenko","year":"2009","journal-title":"J. Comp. Neurol."},{"key":"10.1016\/j.abb.2025.110636_bib36","doi-asserted-by":"crossref","first-page":"56","DOI":"10.3389\/fncel.2014.00056","article-title":"The free radical scavenger Trolox dampens neuronal hyperexcitability, reinstates synaptic plasticity, and improves hypoxia tolerance in a mouse model of Rett syndrome","volume":"8","author":"Janc","year":"2014","journal-title":"Front. Cell. Neurosci."},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib37","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.nut.2009.08.008","article-title":"Clinical aspects of coenzyme Q10: an update","volume":"26","author":"Littarru","year":"2010","journal-title":"Nutrition"},{"issue":"8","key":"10.1016\/j.abb.2025.110636_bib38","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.3390\/antiox10081325","article-title":"Role of coenzyme Q10 in health and disease: an update on the last 10 Years (2010-2020)","volume":"10","author":"Cirilli","year":"2021","journal-title":"Antioxidants"},{"issue":"10","key":"10.1016\/j.abb.2025.110636_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0109223","article-title":"Coenzyme Q10 protects human endothelial cells from \u03b2-amyloid uptake and oxidative stress-induced injury","volume":"9","author":"Dur\u00e1n-Prado","year":"2014","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.abb.2025.110636_bib40","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1007\/s12031-009-9297-1","article-title":"Coenzyme Q10 reduces beta-amyloid plaque in an APP\/PS1 transgenic mouse model of Alzheimer's disease","volume":"41","author":"Yang","year":"2010","journal-title":"J. Mol. Neurosci."},{"issue":"7","key":"10.1016\/j.abb.2025.110636_bib41","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1001\/archneurol.2012.85","article-title":"Antioxidants for Alzheimer disease: a randomized clinical trial with cerebrospinal fluid biomarker measures","volume":"69","author":"Galasko","year":"2012","journal-title":"Arch. Neurol."},{"issue":"1","key":"10.1016\/j.abb.2025.110636_bib42","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.jped.2016.04.012","article-title":"Coenzyme Q10 and pro-inflammatory markers in children with Down syndrome: clinical and biochemical aspects","volume":"93","author":"Zaki","year":"2017","journal-title":"J. Pediatr."},{"issue":"13","key":"10.1016\/j.abb.2025.110636_bib43","doi-asserted-by":"crossref","first-page":"3317","DOI":"10.3390\/ijms20133317","article-title":"Loss of mevalonate\/cholesterol homeostasis in the brain: A focus on autism spectrum disorder and Rett syndrome","volume":"20","author":"Segatto","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"1\u20132","key":"10.1016\/j.abb.2025.110636_bib44","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s11010-019-03633-5","article-title":"Effects of oral administration of common antioxidant supplements on the energy metabolism of red blood cells. Attenuation of oxidative stress-induced changes in Rett syndrome erythrocytes by CoQ10","volume":"463","author":"Di Pierro","year":"2020","journal-title":"Mol. Cell. Biochem."},{"issue":"2","key":"10.1016\/j.abb.2025.110636_bib45","doi-asserted-by":"crossref","first-page":"256","DOI":"10.3390\/antiox10020256","article-title":"Human paraoxonase-2 (PON2): protein functions and modulation","volume":"10","author":"Manco","year":"2021","journal-title":"Antioxidants"},{"issue":"15","key":"10.1016\/j.abb.2025.110636_bib46","doi-asserted-by":"crossref","first-page":"2055","DOI":"10.1161\/CIRCULATIONAHA.106.681700","article-title":"Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation","volume":"115","author":"Horke","year":"2007","journal-title":"Circulation"},{"issue":"2","key":"10.1016\/j.abb.2025.110636_bib47","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.freeradbiomed.2004.09.035","article-title":"The paraoxonase gene family and atherosclerosis","volume":"38","author":"Ng","year":"2005","journal-title":"Free Radic. Biol. Med."},{"issue":"6","key":"10.1016\/j.abb.2025.110636_bib48","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1194\/jlr.M400511-JLR200","article-title":"Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities","volume":"46","author":"Draganov","year":"2005","journal-title":"J. Lipid Res."},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib49","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1089\/ars.2010.3430","article-title":"Paraoxonase 2 deficiency alters mitochondrial function and exacerbates the development of atherosclerosis","volume":"14","author":"Devarajan","year":"2011","journal-title":"Antioxidants Redox Signal."},{"issue":"32","key":"10.1016\/j.abb.2025.110636_bib50","doi-asserted-by":"crossref","first-page":"24398","DOI":"10.1074\/jbc.M110.118604","article-title":"One enzyme, two functions","volume":"285","author":"Altenh\u00f6fer","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2025.110636_bib51","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2023.110839","article-title":"Signature of paraoxonases in the altered redox homeostasis in Alzheimer's disease","volume":"388","author":"Beggiato","year":"2024","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.abb.2025.110636_bib52","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/5694058","article-title":"Lactonase activity and lipoprotein-phospholipase A2 as possible novel serum biomarkers for the differential diagnosis of autism spectrum disorders and Rett syndrome: Results from a pilot study","volume":"2017","author":"Hayek","year":"2017","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2025.110636_bib53","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.freeradbiomed.2020.05.014","article-title":"Proteomic profiling reveals mitochondrial alterations in Rett syndrome","volume":"155","author":"Cicaloni","year":"2020","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2025.110636_bib54","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.freeradbiomed.2021.01.032","article-title":"Anti-ageing effects of ubiquinone and ubiquinol in a senescence model of human dermal fibroblasts","volume":"165","author":"Marcheggiani","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2025.110636_bib55","doi-asserted-by":"crossref","DOI":"10.1155\/2018\/8936251","article-title":"Combination of coenzyme Q10 intake and moderate physical activity counteracts mitochondrial dysfunctions in a SAMP8 mouse model","volume":"2018","author":"Andreani","year":"2018","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2025.110636_bib56","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.mito.2020.11.004","article-title":"Evaluation of anticancer role of a novel ruthenium(II)-based compound compared with NAMI-A and cisplatin in impairing mitochondrial functionality and promoting oxidative stress in triple negative breast cancer models","volume":"56","author":"Silvestri","year":"2021","journal-title":"Mitochondrion"},{"key":"10.1016\/j.abb.2025.110636_bib57","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2023.110702","article-title":"Modulation of paraoxonase-2 in human dermal fibroblasts by UVA-induced oxidative stress: a new potential marker of skin photodamage","volume":"384","author":"Morresi","year":"2023","journal-title":"Chem. Biol. Interact."},{"issue":"10","key":"10.1016\/j.abb.2025.110636_bib58","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1089\/ars.2010.3779","article-title":"The interplay between mitochondrial dynamics and mitophagy","volume":"14","author":"Twig","year":"2011","journal-title":"Antioxidants Redox Signal."},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib59","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.molcel.2015.01.002","article-title":"Erk2 phosphorylation of Drp1 promotes mitochondrial fission and MAPK-driven tumor growth","volume":"57","author":"Kashatus","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.abb.2025.110636_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2021.108790","article-title":"Impaired mitochondrial quality control in Rett Syndrome","volume":"700","author":"Crivellari","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.abb.2025.110636_bib61","doi-asserted-by":"crossref","first-page":"58","DOI":"10.3389\/fncel.2017.00058","article-title":"Mitochondrial dysfunction in the pathogenesis of Rett syndrome: Implications for mitochondria-targeted therapies","volume":"11","author":"Shulyakova","year":"2017","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.abb.2025.110636_bib62","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1111\/j.1749-6632.2012.06611.x","article-title":"The role of oxidative stress in Rett syndrome: an overview","volume":"1259","author":"De Felice","year":"2012","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"10 Pt A","key":"10.1016\/j.abb.2025.110636_bib63","doi-asserted-by":"crossref","first-page":"2066","DOI":"10.1016\/j.bbadis.2015.07.014","article-title":"Impaired enzymatic defensive activity, mitochondrial dysfunction and proteasome activation are involved in RTT cell oxidative damage","volume":"1852","author":"Cervellati","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"issue":"3","key":"10.1016\/j.abb.2025.110636_bib64","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0304-3940(03)00185-X","article-title":"Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease","volume":"341","author":"M\u00fcller","year":"2003","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.abb.2025.110636_bib65","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.psychres.2018.03.061","article-title":"Coenzyme Q10 supplementation reduces oxidative stress and decreases antioxidant enzyme activity in children with autism spectrum disorders","volume":"265","author":"Mousavinejad","year":"2018","journal-title":"Psychiatry Res."},{"issue":"6","key":"10.1016\/j.abb.2025.110636_bib66","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.pediatrneurol.2007.08.003","article-title":"Coenzyme Q10 (ubiquinol-10) supplementation improves oxidative imbalance in children with trisomy 21","volume":"37","author":"Miles","year":"2007","journal-title":"Pediatr. Neurol."},{"issue":"8","key":"10.1016\/j.abb.2025.110636_bib67","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.3390\/jcm14082748","article-title":"Coenzyme Q10 and the blood\u2013brain barrier: An overview","volume":"14","author":"Mantle","year":"2025","journal-title":"J. Clin. Med."},{"issue":"6","key":"10.1016\/j.abb.2025.110636_bib68","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.3390\/antiox12061163","article-title":"Mitochondrial fission as a therapeutic target for metabolic diseases: insights into antioxidant strategies","volume":"12","author":"Yu","year":"2023","journal-title":"Antioxidants"},{"key":"10.1016\/j.abb.2025.110636_bib69","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.3389\/fphar.2020.01034","article-title":"CoenzymeQ10-Induced activation of AMPK-YAP-OPA1 pathway alleviates atherosclerosis by improving mitochondrial function, inhibiting oxidative stress and promoting energy metabolism","volume":"11","author":"Xie","year":"2020","journal-title":"Front. Pharmacol."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib70","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1007\/s11064-016-2143-2","article-title":"Water-soluble coenzyme Q10 reduces rotenone-induced mitochondrial fission","volume":"42","author":"Li","year":"2017","journal-title":"Neurochem. Res."},{"issue":"4","key":"10.1016\/j.abb.2025.110636_bib71","doi-asserted-by":"crossref","first-page":"60","DOI":"10.14715\/cmb\/2023.69.4.9","article-title":"Effects of pyrroloquinoline quinone (PQQ) and coenzyme Q10 on mitochondrial genes, MitomiRs and cellular properties in HepG2 cell line","volume":"69","author":"Nalbant","year":"2023","journal-title":"Cell. Mol. Biol. (Noisy-Le-Grand)"},{"issue":"1","key":"10.1016\/j.abb.2025.110636_bib72","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-25802-1","article-title":"Paraoxonase-2 contributes to promoting lipid metabolism and mitochondrial function via autophagy activation","volume":"12","author":"Shin","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2025.110636_bib73","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.neuro.2013.08.011","article-title":"Paraoxonase-2 (PON2) in brain and its potential role in neuroprotection","volume":"43","author":"Costa","year":"2014","journal-title":"Neurotoxicology"}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125003509?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125003509?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,30]],"date-time":"2025-10-30T00:44:19Z","timestamp":1761785059000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986125003509"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":73,"alternative-id":["S0003986125003509"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2025.110636","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mitochondrial redox imbalance and CoQ10 deficiency in Rett syndrome: Insights from patient-derived fibroblasts","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2025.110636","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110636"}}