{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,10]],"date-time":"2026-01-10T08:24:19Z","timestamp":1768033459431,"version":"3.49.0"},"reference-count":72,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2019,2,15]],"date-time":"2019-02-15T00:00:00Z","timestamp":1550188800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Rett syndrome (RTT) is a human neurodevelopmental disorder, whose pathogenesis has been linked to both oxidative stress and subclinical inflammatory status (OxInflammation). Methylglyoxal (MG), a glycolytic by-product with cytotoxic and pro-oxidant power, is the major precursor in vivo of advanced glycation end products (AGEs), which are known to exert their detrimental effect via receptor- (e.g., RAGE) or non-receptor-mediated mechanisms in several neurological diseases. On this basis, we aimed to compare fibroblasts from healthy subjects (CTR) with fibroblasts from RTT patients (N = 6 per group), by evaluating gene\/protein expression patterns, and enzymatic activities of glyoxalases (GLOs), along with the levels of MG-dependent damage in both basal and MG-challenged conditions. Our results revealed that RTT is linked to an alteration of the GLOs system (specifically, increased GLO2 activity), that ensures unchanged MG-dependent damage levels. However, RTT cells underwent more pronounced cell death upon exogenous MG-treatment, as compared to CTR, and displayed lower RAGE levels than CTR, with no alterations following MG-treatment, thus suggesting that an adaptive response to dicarbonyl stress may occur. In conclusion, besides OxInflammation, RTT is associated with reshaping of the major defense systems against dicarbonyl stress, along with an altered cellular stress response towards pro-glycating insults.<\/jats:p>","DOI":"10.3390\/cells8020161","type":"journal-article","created":{"date-parts":[[2019,2,17]],"date-time":"2019-02-17T22:11:50Z","timestamp":1550441510000},"page":"161","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Antiglycative Activity and RAGE Expression in Rett Syndrome"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2791-8121","authenticated-orcid":false,"given":"Valeria","family":"Cordone","sequence":"first","affiliation":[{"name":"Department of Life, Health and Environmental Sciences, University of L\u2019Aquila, Via Vetoio, 67100 L\u2019Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessandra","family":"Pecorelli","sequence":"additional","affiliation":[{"name":"Plants for Human Health Institute, Animal Science Department, NC Research Campus, NC State University, 600 Laureate Way, Kannapolis, NC 28081, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mascia","family":"Benedusi","sequence":"additional","affiliation":[{"name":"Department of Life Sciences and Biotechnology, University of Ferrara, Via Luigi Borsari 46, 44121 Ferrara, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6577-5892","authenticated-orcid":false,"suffix":"Jr.","given":"Silvano","family":"Santini","sequence":"additional","affiliation":[{"name":"Department of Life, Health and Environmental Sciences, University of L\u2019Aquila, Via Vetoio, 67100 L\u2019Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5978-0545","authenticated-orcid":false,"given":"Stefano","family":"Falone","sequence":"additional","affiliation":[{"name":"Department of Life, Health and Environmental Sciences, University of L\u2019Aquila, Via Vetoio, 67100 L\u2019Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joussef","family":"Hayek","sequence":"additional","affiliation":[{"name":"Child Neuropsychiatry Unit, University General Hospital, Azienda Ospedaliera Universitaria Senese, Viale M. Bracci 16, 53100 Siena, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernanda","family":"Amicarelli","sequence":"additional","affiliation":[{"name":"Department of Life, Health and Environmental Sciences, University of L\u2019Aquila, Via Vetoio, 67100 L\u2019Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giuseppe","family":"Valacchi","sequence":"additional","affiliation":[{"name":"Plants for Human Health Institute, Animal Science Department, NC Research Campus, NC State University, 600 Laureate Way, Kannapolis, NC 28081, USA"},{"name":"Department of Life Sciences and Biotechnology, University of Ferrara, Via Luigi Borsari 46, 44121 Ferrara, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,2,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/BF01487267","article-title":"Rett syndrome in Sweden","volume":"17","author":"Gillberg","year":"1987","journal-title":"J. Autism. Dev. Disord."},{"key":"ref_2","first-page":"8","article-title":"The prevalence and incidence of Rett syndrome in Australia","volume":"6","author":"Leonard","year":"1997","journal-title":"Eur. Child Adolesc. Psychiatry"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.pediatrneurol.2005.10.013","article-title":"The incidence of Rett syndrome in France","volume":"34","author":"Bienvenu","year":"2006","journal-title":"Pediatr. Neurol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1002\/ana.22124","article-title":"RettSearch Consortium. Rett syndrome: Revised diagnostic criteria and nomenclature","volume":"68","author":"Neul","year":"2010","journal-title":"Ann. Neurol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/nrg3897","article-title":"Rett syndrome: A complex disorder with simple roots","volume":"16","author":"Lyst","year":"2015","journal-title":"Nat. Rev. Genet."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1016\/j.neuron.2007.10.001","article-title":"The story of Rett syndrome: From clinic to neurobiology","volume":"56","author":"Chahrour","year":"2007","journal-title":"Neuron"},{"key":"ref_7","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"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"480980","DOI":"10.1155\/2014\/480980","article-title":"Subclinical inflammatory status in Rett syndrome","volume":"2014","author":"Cortelazzo","year":"2014","journal-title":"Mediators Inflamm."},{"key":"ref_9","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":"ref_10","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."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"421624","DOI":"10.1155\/2015\/421624","article-title":"Cytokine Dysregulation in MECP2- and CDKL5-Related Rett Syndrome: Relationships with Aberrant Redox Homeostasis, Inflammation, and \u03c9-3 PUFAs","volume":"2015","author":"Leoncini","year":"2015","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"858","DOI":"10.3389\/fphys.2018.00858","article-title":"OxInflammation: From Subclinical Condition to Pathological Biomarker","volume":"9","author":"Valacchi","year":"2018","journal-title":"Front. Physiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"332","DOI":"10.3109\/10799893.2011.607171","article-title":"Cell signaling and receptors in toxicity of advanced glycation end products (AGEs): \u03b1-dicarbonyls, radicals, oxidative stress and antioxidants","volume":"31","author":"Kovacic","year":"2011","journal-title":"J. Recept. Signal Transduct. Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.jfda.2016.10.017","article-title":"Polyphenols with antiglycation activity and mechanisms of action: A review of recent findings","volume":"25","author":"Yeh","year":"2017","journal-title":"J. Food Drug Anal."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.bbrc.2015.01.140","article-title":"Dicarbonyl stress in cell and tissue dysfunction contributing to ageing and disease","volume":"458","author":"Rabbani","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.freeradbiomed.2018.01.017","article-title":"Nicotine induces apoptosis in human osteoblasts via a novel mechanism driven by H(2)O(2) and entailing Glyoxalase 1-dependent MG-H1 accumulation leading to TG2-mediated NF-kB desensitization: Implication for smokers-related osteoporosis","volume":"117","author":"Marinucci","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1016\/S0891-5849(03)00438-6","article-title":"Scavenging system efficiency is crucial for cell resistance to ROS-mediated methylglyoxal injury","volume":"35","author":"Amicarelli","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.cbi.2007.11.009","article-title":"The tandem of free radicals and methylglyoxal","volume":"171","author":"Kalapos","year":"2008","journal-title":"Chem. Biol. Interact."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1007\/s10495-013-0902-y","article-title":"Reactive oxygen species induce apoptosis in bronchial epithelial BEAS-2B cells by inhibiting the antiglycation glyoxalase I defence: Involvement of superoxide anion, hydrogen peroxide and NF-\u03baB","volume":"19","author":"Antognelli","year":"2014","journal-title":"Apoptosis"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.brainres.2004.01.066","article-title":"Methylglyoxal induces oxidative stress-dependent cell injury and up-regulation of interleukin-1beta and nerve growth factor in cultured hippocampal neuronal cells","volume":"1006","author":"Caracciolo","year":"2004","journal-title":"Brain Res."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3390\/biom5010194","article-title":"Advanced glycation end products and oxidative stress in type 2 diabetes mellitus","volume":"5","author":"Nowotny","year":"2015","journal-title":"Biomolecules"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1080\/1071576021000041005","article-title":"Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185","volume":"37","author":"Park","year":"2003","journal-title":"Free Radic. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1016\/j.bcp.2009.02.024","article-title":"Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells","volume":"77","author":"Wang","year":"2009","journal-title":"Biochem. Pharmacol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1111\/j.1474-9726.2008.00371.x","article-title":"Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans","volume":"7","author":"Morcos","year":"2008","journal-title":"Aging Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"193","DOI":"10.5487\/TR.2014.30.3.193","article-title":"Methylglyoxal induces mitochondrial dysfunction and cell death in liver","volume":"30","author":"Seo","year":"2014","journal-title":"Toxicol. Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1007\/s10719-016-9705-z","article-title":"Dicarbonyls and glyoxalase in disease mechanisms and clinical therapeutics","volume":"33","author":"Rabbani","year":"2016","journal-title":"Glycoconj. J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1016\/j.neurobiolaging.2011.02.003","article-title":"AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation","volume":"33","author":"Li","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"407","DOI":"10.2478\/s11658-014-0205-5","article-title":"The role of advanced glycation end products in various types of neurodegenerative disease: A therapeutic approach","volume":"19","author":"Salahuddin","year":"2014","journal-title":"Cell. Mol. Biol. Lett."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.mehy.2012.01.032","article-title":"Methylglyoxal, advanced glycation end products and autism: Is there a connection?","volume":"78","author":"Maher","year":"2012","journal-title":"Med. Hypotheses"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1002\/path.2682","article-title":"The sour side of neurodegenerative disorders: The effects of protein glycation","volume":"221","author":"Outeiro","year":"2010","journal-title":"J. Pathol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e673","DOI":"10.1038\/cddis.2013.180","article-title":"Glycation exacerbates the neuronal toxicity of \u03b2-amyloid","volume":"4","author":"Li","year":"2013","journal-title":"Cell Death Dis."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1021\/cn3001679","article-title":"Restoration of glyoxalase enzyme activity precludes cognitive dysfunction in a mouse model of Alzheimer\u2019s disease","volume":"4","author":"More","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1139\/Y10-001","article-title":"Oxidative stress and aging: Is methylglyoxal the hidden enemy?","volume":"88","author":"Desai","year":"2010","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"249","DOI":"10.2337\/db09-0801","article-title":"Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands","volume":"59","author":"Yao","year":"2010","journal-title":"Diabetes"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1096\/fj.09-139634","article-title":"RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning\/memory in a mouse model of Alzheimer\u2019s disease","volume":"24","author":"Fang","year":"2010","journal-title":"FASEB J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1111\/jnc.13087","article-title":"Neuroprotective effects of vildagliptin in rat rotenone Parkinson\u2019s disease model: Role of RAGE-NF\u03baB and Nrf2-antioxidant signaling pathways","volume":"133","author":"Abdelsalam","year":"2015","journal-title":"J. Neurochem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.neubiorev.2015.12.006","article-title":"RAGE axis in neuroinflammation, neurodegeneration and its emerging role in the pathogenesis of amyotrophic lateral sclerosis","volume":"62","author":"Ray","year":"2016","journal-title":"Neurosci. Biobehav. Rev."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1074\/jbc.M117.786756","article-title":"Receptor for advanced glycation end products mediates sepsis-triggered amyloid-\u00df accumulation, Tau phosphorylation, and cognitive impairment","volume":"293","author":"Gasparotto","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_39","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"},{"key":"ref_40","first-page":"1439","article-title":"Mecp2 regulates tnfa during zebrafish embryonic development and acute inflammation","volume":"10","author":"Svoboda","year":"2017","journal-title":"Dis. Model. Mech."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1007\/s12035-012-8245-1","article-title":"Primary skin fibroblasts as a model of Parkinson\u2019s disease","volume":"46","author":"Auburger","year":"2012","journal-title":"Mol. Neurobiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3588","DOI":"10.1016\/j.bbadis.2018.09.018","article-title":"Mitochondrial dysfunction in fibroblasts of Multiple System Atrophy","volume":"1864","author":"Kleiner","year":"2018","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_43","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":"ref_44","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/S0076-6879(81)77041-1","article-title":"Glyoxalase I (rat liver)","volume":"77","author":"Mannervik","year":"1981","journal-title":"Methods Enzymol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"8818","DOI":"10.1021\/bi00424a020","article-title":"Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes","volume":"27","author":"Guha","year":"1988","journal-title":"Biochemistry"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2014","DOI":"10.1002\/jcp.25310","article-title":"Improved Mitochondrial and Methylglyoxal-Related Metabolisms Support Hyperproliferation Induced by 50 Hz Magnetic Field in Neuroblastoma Cells","volume":"231","author":"Falone","year":"2016","journal-title":"J. Cell. Physiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4256519","DOI":"10.1155\/2017\/4256519","article-title":"Potassium Ascorbate with Ribose: Promising Therapeutic Approach for Melanoma Treatment","volume":"2017","author":"Cavicchio","year":"2017","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.3390\/nu5083311","article-title":"Dietary fructose feeding increases adipose methylglyoxal accumulation in rats in association with low expression and activity of glyoxalase-2","volume":"5","author":"Masterjohn","year":"2013","journal-title":"Nutrients"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20121743","article-title":"The glyoxalase pathway: The first hundred years... and beyond","volume":"453","author":"Gomes","year":"2013","journal-title":"Biochem. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"5287","DOI":"10.1167\/iovs.03-0573","article-title":"Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins","volume":"44","author":"Ahmed","year":"2003","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3327","DOI":"10.1021\/bi500046t","article-title":"The receptor for advanced glycation end products (RAGE) specifically recognizes methylglyoxal-derived AGEs","volume":"53","author":"Xue","year":"2014","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"195935","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."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1002\/cbf.3236","article-title":"A possible S-glutathionylation of specific proteins by glyoxalase II: An in vitro and in silico study","volume":"34","author":"Ercolani","year":"2016","journal-title":"Cell Biochem. Funct."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"26497","DOI":"10.1074\/jbc.R113.461368","article-title":"Causes and consequences of cysteine S-glutathionylation","volume":"288","author":"Grek","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Birkenmeier, G., Stegemann, C., Hoffmann, R., G\u00fcnther, R., Huse, K., and Birkemeyer, C. (2010). Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation. PLoS ONE., 5.","DOI":"10.1371\/journal.pone.0010399"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tem.2012.06.005","article-title":"The dynamic regulation of NAD metabolism in mitochondria","volume":"23","author":"Stein","year":"2012","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.biocel.2016.08.001","article-title":"Proteomic analysis of 4-hydroxynonenal and nitrotyrosine modified proteins in RTT fibroblasts","volume":"81","author":"Pecorelli","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/sj.bjp.0707395","article-title":"Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors","volume":"153","author":"Coatrieux","year":"2008","journal-title":"Br. J. Pharmacol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1042\/bj2080129","article-title":"Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2+ in rat liver microsomes","volume":"208","author":"Esterbauer","year":"1982","journal-title":"Biochem. J."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.1212\/WNL.56.11.1486","article-title":"MeCP2 mutations in children with and without the phenotype of Rett syndrome","volume":"56","author":"Hoffbuhr","year":"2001","journal-title":"Neurology"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1002\/mrdd.10026","article-title":"Associations between MeCP2 mutations, X-chromosome inactivation, and phenotype","volume":"8","author":"Hoffbuhr","year":"2002","journal-title":"Ment. Retard. Dev. Disabil. Res. Rev."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1093\/hmg\/ddh142","article-title":"X-Chromosome inactivation ratios affect wild-type MeCP2 expression within mosaic Rett syndrome and Mecp2-\/+ mouse brain","volume":"13","author":"Braunschweig","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"24","DOI":"10.3389\/fpsyt.2012.00024","article-title":"X-chromosome inactivation in rett syndrome human induced pluripotent stem cells","volume":"3","author":"Cheung","year":"2012","journal-title":"Front. Psychiatry"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"170216","DOI":"10.1098\/rsob.170216","article-title":"Rett syndrome: A neurological disorder with metabolic components","volume":"8","author":"Kyle","year":"2018","journal-title":"Open Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1055\/s-0037-1613678","article-title":"AGE-RAGE Stress, Stressors, and Antistressors in Health and Disease","volume":"27","author":"Prasad","year":"2018","journal-title":"Int. J. Angiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1042\/BJ20120298","article-title":"Advanced-glycation-end-product-induced formation of immunoproteasomes: Involvement of RAGE and Jak2\/STAT1","volume":"448","author":"Grimm","year":"2012","journal-title":"Biochem. J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1189\/jlb.1012519","article-title":"RAGE regulation and signaling in inflammation and beyond","volume":"94","author":"Kierdorf","year":"2013","journal-title":"J. Leukoc. Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.redox.2013.12.016","article-title":"Role of advanced glycation end products in cellular signaling","volume":"2","author":"Ott","year":"2014","journal-title":"Redox Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"9467819","DOI":"10.1155\/2017\/9467819","article-title":"Persistent Unresolved Inflammation in the Mecp2-308 Female Mutated Mouse Model of Rett Syndrome","volume":"2017","author":"Cortelazzo","year":"2017","journal-title":"Mediators Inflamm."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.cyto.2015.10.002","article-title":"Cytokines profile and peripheral blood mononuclear cells morphology in Rett and autistic patients","volume":"77","author":"Pecorelli","year":"2016","journal-title":"Cytokine"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/8\/2\/161\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:32:20Z","timestamp":1760185940000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/8\/2\/161"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,2,15]]},"references-count":72,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2019,2]]}},"alternative-id":["cells8020161"],"URL":"https:\/\/doi.org\/10.3390\/cells8020161","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,2,15]]}}}