{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:25:25Z","timestamp":1790641525043,"version":"4.1.0"},"reference-count":93,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2014,3,1]],"date-time":"2014-03-01T00:00:00Z","timestamp":1393632000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"crossref","award":["FP7-241622"],"award-info":[{"award-number":["FP7-241622"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100008731","name":"European Leukodystrophy Association","doi-asserted-by":"crossref","award":["ELA2009-035I4"],"award-info":[{"award-number":["ELA2009-035I4"]}],"id":[{"id":"10.13039\/501100008731","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100008731","name":"European Leukodystrophy Association","doi-asserted-by":"crossref","award":["ELA2009-036C5"],"award-info":[{"award-number":["ELA2009-036C5"]}],"id":[{"id":"10.13039\/501100008731","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100008731","name":"European Leukodystrophy Association","doi-asserted-by":"crossref","award":["ELA2008-040C4"],"award-info":[{"award-number":["ELA2008-040C4"]}],"id":[{"id":"10.13039\/501100008731","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Spanish Institute for Health Carlos III","award":["FIS PI080991"],"award-info":[{"award-number":["FIS PI080991"]}]},{"name":"Spanish Institute for Health Carlos III","award":["FIS PI11\/01043"],"award-info":[{"award-number":["FIS PI11\/01043"]}]},{"name":"Oliver's army"},{"name":"Hesperia Foundation"},{"name":"Autonomous Government of Catalonia","award":["2009SGR85"],"award-info":[{"award-number":["2009SGR85"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2014,3]]},"DOI":"10.1016\/j.biochi.2013.09.012","type":"journal-article","created":{"date-parts":[[2013,9,24]],"date-time":"2013-09-24T17:01:33Z","timestamp":1380042093000},"page":"143-149","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":50,"special_numbering":"C","title":["Mitochondrial dysfunction and oxidative damage cooperatively fuel axonal degeneration in X-linked adrenoleukodystrophy"],"prefix":"10.1016","volume":"98","author":[{"given":"St\u00e9phane","family":"Fourcade","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jone","family":"L\u00f3pez-Erauskin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Montserrat","family":"Ruiz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isidre","family":"Ferrer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aurora","family":"Pujol","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2013.09.012_bib1","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/ana.101","article-title":"Adrenoleukodystrophy: incidence, new mutation rate, and results of extended family screening","volume":"49","author":"Bezman","year":"2001","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib2","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1111\/j.1750-3639.2010.00390.x","article-title":"General aspects and neuropathology of X-linked adrenoleukodystrophy","volume":"20","author":"Ferrer","year":"2010","journal-title":"Brain Pathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib3","series-title":"The Metabolic and Molecular Bases of Inherited Disease","first-page":"3257","article-title":"X-linked adrenoleukodystrophy","author":"Moser","year":"2001"},{"key":"10.1016\/j.biochi.2013.09.012_bib4","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1186\/1750-1172-7-51","article-title":"X-linked adrenoleukodystrophy (X-ALD): clinical presentation and guidelines for diagnosis, follow-up and management","volume":"7","author":"Engelen","year":"2012","journal-title":"Orphanet. J. Rare Dis."},{"key":"10.1016\/j.biochi.2013.09.012_bib5","first-page":"470","article-title":"X-linked adrenoleukodystrophy is a frequent cause of idiopathic Addison's disease in young adult male patients","volume":"81","author":"Laureti","year":"1996","journal-title":"J.\u00a0Clin. Endocrinol. Metab."},{"key":"10.1016\/j.biochi.2013.09.012_bib6","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1093\/jnen\/59.2.89","article-title":"Adrenomyeloneuropathy: a neuropathologic review featuring its noninflammatory myelopathy","volume":"59","author":"Powers","year":"2000","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib7","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1111\/j.1750-3639.2010.00393.x","article-title":"Current and future pharmacological treatment strategies in X-linked adrenoleukodystrophy","volume":"20","author":"Berger","year":"2010","journal-title":"Brain Pathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib8","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1126\/science.1171242","article-title":"Hematopoietic stem cell gene therapy with a lentiviral vector in X-linked adrenoleukodystrophy","volume":"326","author":"Cartier","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.biochi.2013.09.012_bib9","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1182\/blood-2003-10-3402","article-title":"Cerebral X-linked adrenoleukodystrophy: the international hematopoietic cell transplantation experience from 1982 to 1999","volume":"104","author":"Peters","year":"2004","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2013.09.012_bib10","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/S0140-6736(00)02629-5","article-title":"Long-term effect of bone-marrow transplantation for childhood-onset cerebral X-linked adrenoleukodystrophy","volume":"356","author":"Shapiro","year":"2000","journal-title":"Lancet"},{"key":"10.1016\/j.biochi.2013.09.012_bib11","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1126\/science.182.4107.62","article-title":"Peroxisomal and mitochondrial defects in the cerebro-hepato-renal syndrome","volume":"182","author":"Goldfischer","year":"1973","journal-title":"Science"},{"key":"10.1016\/j.biochi.2013.09.012_bib12","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1093\/jnen\/60.5.493","article-title":"The dorsal root ganglia in adrenomyeloneuropathy: neuronal atrophy and abnormal mitochondria","volume":"60","author":"Powers","year":"2001","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib13","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1007\/s004010050490","article-title":"Mitochondrial abnormalities and intrafamilial variability of sural nerve biopsy findings in adrenomyeloneuropathy","volume":"92","author":"Schroder","year":"1996","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib14","doi-asserted-by":"crossref","first-page":"3565","DOI":"10.1093\/hmg\/ddi384","article-title":"Inactivation of the peroxisomal ABCD2 transporter in\u00a0the mouse leads to late-onset ataxia involving mitochondria, Golgi and\u00a0endoplasmic reticulum damage","volume":"14","author":"Ferrer","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib15","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1128\/MCB.23.2.744-753.2003","article-title":"Role of ALDP (ABCD1) and mitochondria in X-linked adrenoleukodystrophy","volume":"23","author":"McGuinness","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.biochi.2013.09.012_bib16","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1016\/S0002-9440(10)62534-5","article-title":"Mitochondrial alterations caused by defective peroxisomal biogenesis in a mouse model for Zellweger syndrome (PEX5 knockout mouse)","volume":"159","author":"Baumgart","year":"2001","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib17","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1002\/hep.20628","article-title":"Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER abnormalities","volume":"41","author":"Dirkx","year":"2005","journal-title":"Hepatology"},{"key":"10.1016\/j.biochi.2013.09.012_bib18","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1089\/ars.2009.3074","article-title":"Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders","volume":"13","author":"Calabrese","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biochi.2013.09.012_bib19","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.tins.2012.04.001","article-title":"Mitochondria as a central sensor for axonal degenerative stimuli","volume":"35","author":"Court","year":"2012","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.biochi.2013.09.012_bib20","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1007\/s11064-010-0295-z","article-title":"Oxidative damage in rat brain during aging: interplay between energy and metabolic key target proteins","volume":"35","author":"Di Domenico","year":"2010","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.biochi.2013.09.012_bib21","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1016\/j.neurobiolaging.2007.12.005","article-title":"Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice","volume":"30","author":"Hauptmann","year":"2009","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.biochi.2013.09.012_bib22","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.1089\/ars.2007.1763","article-title":"Mitochondrial dysfunction: the first domino in brain aging and Alzheimer's disease?","volume":"9","author":"Leuner","year":"2007","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biochi.2013.09.012_bib23","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/nature05292","article-title":"Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases","volume":"443","author":"Lin","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2013.09.012_bib24","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1111\/j.1750-3639.2009.00326.x","article-title":"Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates","volume":"20","author":"Martinez","year":"2010","journal-title":"Brain Pathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib25","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1196\/annals.1427.010","article-title":"Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows","volume":"1147","author":"Pratico","year":"2008","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.biochi.2013.09.012_bib26","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1196\/annals.1427.008","article-title":"Evidence of oxidant damage in Huntington's disease: translational strategies using antioxidants","volume":"1147","author":"Stack","year":"2008","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.biochi.2013.09.012_bib27","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1196\/annals.1427.023","article-title":"Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance","volume":"1147","author":"Zhou","year":"2008","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.biochi.2013.09.012_bib28","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1111\/j.1471-4159.1991.tb02003.x","article-title":"Fatty acid composition of human myelin proteolipid protein in peroxisomal disorders","volume":"56","author":"Bizzozero","year":"1991","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.biochi.2013.09.012_bib29","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1002\/(SICI)1097-4547(19971201)50:5<829::AID-JNR19>3.0.CO;2-W","article-title":"Targeted inactivation of the X-linked adrenoleukodystrophy gene in mice","volume":"50","author":"Forss-Petter","year":"1997","journal-title":"J.\u00a0Neurosci. Res."},{"key":"10.1016\/j.biochi.2013.09.012_bib30","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1006\/bbrc.1997.6340","article-title":"Adrenoleukodystrophy protein-deficient mice represent abnormality of very long chain fatty acid metabolism","volume":"232","author":"Kobayashi","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2013.09.012_bib31","doi-asserted-by":"crossref","first-page":"9366","DOI":"10.1073\/pnas.94.17.9366","article-title":"A\u00a0mouse model for X-linked adrenoleukodystrophy","volume":"94","author":"Lu","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2013.09.012_bib32","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1093\/hmg\/11.5.499","article-title":"Late onset neurological phenotype of the X-ALD gene inactivation in mice: a mouse model for adrenomyeloneuropathy","volume":"11","author":"Pujol","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib33","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.1093\/hmg\/ddh323","article-title":"Functional overlap between ABCD1 (ALD) and ABCD2 (ALDR) transporters: a therapeutic target for X-adrenoleukodystrophy","volume":"13","author":"Pujol","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib34","doi-asserted-by":"crossref","first-page":"E211","DOI":"10.1152\/ajpendo.90736.2008","article-title":"A\u00a0key role for the peroxisomal ABCD2 transporter in fatty acid homeostasis","volume":"296","author":"Fourcade","year":"2009","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.biochi.2013.09.012_bib35","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1194\/jlr.M022160","article-title":"The absence of ABCD2 sensitizes mice to disruptions in lipid metabolism by dietary erucic acid","volume":"53","author":"Liu","year":"2012","journal-title":"J.\u00a0Lipid. Res."},{"key":"10.1016\/j.biochi.2013.09.012_bib36","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1194\/jlr.M900237-JLR200","article-title":"ABCD2 is abundant in adipose tissue and opposes the accumulation of dietary erucic acid (C22:1) in fat","volume":"51","author":"Liu","year":"2010","journal-title":"J.\u00a0Lipid. Res."},{"key":"10.1016\/j.biochi.2013.09.012_bib37","doi-asserted-by":"crossref","first-page":"2005","DOI":"10.1093\/hmg\/ddq082","article-title":"Valproic acid induces antioxidant effects in X-linked adrenoleukodystrophy","volume":"19","author":"Fourcade","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib38","doi-asserted-by":"crossref","first-page":"3490","DOI":"10.1046\/j.1432-1327.2001.02249.x","article-title":"Fibrate induction of the adrenoleukodystrophy-related gene (ABCD2): promoter analysis and role of the peroxisome proliferator-activated receptor PPARalpha","volume":"268","author":"Fourcade","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2013.09.012_bib39","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1124\/mol.63.6.1296","article-title":"Thyroid hormone induction of the adrenoleukodystrophy-related gene (ABCD2)","volume":"63","author":"Fourcade","year":"2003","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.biochi.2013.09.012_bib40","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1016\/j.biochi.2007.06.013","article-title":"Dehydroepiandrosterone up-regulates the Adrenoleukodystrophy-related gene (ABCD2) independently of PPARalpha in rodents","volume":"89","author":"Gueugnon","year":"2007","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2013.09.012_bib41","doi-asserted-by":"crossref","first-page":"e56242","DOI":"10.1371\/journal.pone.0056242","article-title":"ABCD2 is a direct target of beta-catenin and TCF-4: implications for X-linked adrenoleukodystrophy therapy","volume":"8","author":"Park","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2013.09.012_bib42","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1006\/geno.2000.6367","article-title":"Characterization of the adrenoleukodystrophy-related (ALDR, ABCD2) gene promoter: inductibility by retinoic acid and forskolin","volume":"70","author":"Pujol","year":"2000","journal-title":"Genomics"},{"key":"10.1016\/j.biochi.2013.09.012_bib43","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/j.bbalip.2013.01.004","article-title":"Caffeic acid phenethyl ester induces adrenoleukodystrophy (Abcd2) gene in human X-ALD fibroblasts and inhibits the proinflammatory response in Abcd1\/2 silenced mouse primary astrocytes","volume":"1831","author":"Singh","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2013.09.012_bib44","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1002\/ana.22363","article-title":"Antioxidants halt axonal degeneration in a mouse model of X-adrenoleukodystrophy","volume":"70","author":"Lopez-Erauskin","year":"2011","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib45","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1002\/ana.21677","article-title":"Insulin-like growth factor-1 and neurotrophin-3 gene therapy prevents motor decline in an X-linked adrenoleukodystrophy mouse model","volume":"66","author":"Mastroeni","year":"2009","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib46","doi-asserted-by":"crossref","first-page":"2432","DOI":"10.1093\/brain\/awt143","article-title":"Pioglitazone halts axonal degeneration in a mouse model of X-linked adrenoleukodystrophy","volume":"136","author":"Morato","year":"2013","journal-title":"Brain"},{"key":"10.1016\/j.biochi.2013.09.012_bib47","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1093\/hmg\/ddr536","article-title":"Functional genomic analysis unravels a metabolic-inflammatory interplay in adrenoleukodystrophy","volume":"21","author":"Schluter","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib48","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1172\/JCI64595","article-title":"Alzheimer's disease and insulin resistance: translating basic science into clinical applications","volume":"123","author":"De Felice","year":"2013","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2013.09.012_bib49","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1111\/j.1750-3639.2010.00392.x","article-title":"Pathomechanisms underlying X-adrenoleukodystrophy: a three-hit hypothesis","volume":"20","author":"Singh","year":"2010","journal-title":"Brain Pathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib50","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1089\/ars.2011.4313","article-title":"Redox sensing by proteins: oxidative modifications on cysteines and the consequent events","volume":"16","author":"Wang","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biochi.2013.09.012_bib51","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.arr.2007.06.002","article-title":"Highly resistant macromolecular components and low rate of generation of endogenous damage: two key traits of longevity","volume":"6","author":"Pamplona","year":"2007","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.biochi.2013.09.012_bib52","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/j.bbadis.2012.02.005","article-title":"Oxidative stress underlying axonal degeneration in adrenoleukodystrophy: a paradigm for multifactorial neurodegenerative diseases?","volume":"1822","author":"Galea","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2013.09.012_bib53","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1097\/01.jnen.0000190064.28559.a4","article-title":"Adreno-leukodystrophy: oxidative stress of mice and men","volume":"64","author":"Powers","year":"2005","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib54","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.bbadis.2003.10.004","article-title":"Evidence that oxidative stress is increased in patients with X-linked adrenoleukodystrophy","volume":"1688","author":"Vargas","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2013.09.012_bib55","doi-asserted-by":"crossref","first-page":"1762","DOI":"10.1093\/hmg\/ddn085","article-title":"Early oxidative damage underlying neurodegeneration in X-adrenoleukodystrophy","volume":"17","author":"Fourcade","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib56","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1111\/j.1471-4159.1976.tb01593.x","article-title":"Brain gangliosides in adrenoleukodystrophy","volume":"27","author":"Garashi","year":"1976","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.biochi.2013.09.012_bib57","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1212\/WNL.27.10.928","article-title":"Adrenoleukodystrophy. Accumulation of cholesterol esters with very long chain fatty acids","volume":"27","author":"Menkes","year":"1977","journal-title":"Neurology"},{"key":"10.1016\/j.biochi.2013.09.012_bib58","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1093\/hmg\/ddn066","article-title":"Toxic effects of X-linked adrenoleukodystrophy-associated, very long chain fatty acids on glial cells and neurons from rat hippocampus in culture","volume":"17","author":"Hein","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.neuroscience.2012.03.058","article-title":"Evidence of oxidative stress in very long chain fatty acid-treated oligodendrocytes and potentialization of ROS production using RNA interference-directed knockdown of ABCD1 and ACOX1 peroxisomal proteins","volume":"213","author":"Baarine","year":"2012","journal-title":"Neuroscience"},{"key":"10.1016\/j.biochi.2013.09.012_bib60","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.neuro.2011.10.007","article-title":"Incidence of Abcd1 level on the induction of cell death and organelle dysfunctions triggered by very long chain fatty acids and TNF-alpha on oligodendrocytes and astrocytes","volume":"33","author":"Baarine","year":"2012","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.biochi.2013.09.012_bib61","doi-asserted-by":"crossref","first-page":"623257","DOI":"10.1155\/2012\/623257","article-title":"Induction of mitochondrial changes associated with oxidative stress on very long chain fatty acids (C22:0, C24:0, or C26:0)-treated human neuronal cells (SK-NB-E)","volume":"2012","author":"Zarrouk","year":"2012","journal-title":"Oxid. Med. Cell. Longev"},{"key":"10.1016\/j.biochi.2013.09.012_bib62","series-title":"Lipid Peroxidation: Biological Implications","first-page":"47","article-title":"Membrane unsaturation, selective neuronal vulnerability, and age-related neurodegenerative diseases","author":"Naudi","year":"2011"},{"key":"10.1016\/j.biochi.2013.09.012_bib63","doi-asserted-by":"crossref","first-page":"L1005","DOI":"10.1152\/ajplung.2000.279.6.L1005","article-title":"Reactive oxygen species in cell signaling","volume":"279","author":"Thannickal","year":"2000","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"10.1016\/j.biochi.2013.09.012_bib64","doi-asserted-by":"crossref","first-page":"2095","DOI":"10.1089\/ars.2010.3877","article-title":"Oxidative damage compromises energy metabolism in the axonal degeneration mouse model of x-adrenoleukodystrophy","volume":"15","author":"Galino","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biochi.2013.09.012_bib65","doi-asserted-by":"crossref","first-page":"3296","DOI":"10.1093\/hmg\/ddt186","article-title":"Impaired mitochondrial oxidative phosphorylation in the peroxisomal disease X-linked adrenoleukodystrophy","volume":"22","author":"Lopez-Erauskin","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2013.09.012_bib66","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.pneurobio.2012.01.003","article-title":"The ubiquitin proteasome system in neurodegenerative diseases: culprit, accomplice or victim?","volume":"96","author":"Dennissen","year":"2012","journal-title":"Prog. Neurobiol."},{"key":"10.1016\/j.biochi.2013.09.012_bib67","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1038\/nature02263","article-title":"Protein degradation and protection against misfolded or damaged proteins","volume":"426","author":"Goldberg","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2013.09.012_bib68","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s00401-009-0508-1","article-title":"RNA oxidation in Alzheimer disease and related neurodegenerative disorders","volume":"118","author":"Nunomura","year":"2009","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.biochi.2013.09.012_bib69","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1093\/brain\/aws370","article-title":"Oxidative stress regulates the ubiquitin-proteasome system and immunoproteasome functioning in a mouse model of X-adrenoleukodystrophy","volume":"136","author":"Launay","year":"2013","journal-title":"Brain"},{"key":"10.1016\/j.biochi.2013.09.012_bib70","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0092-8674(94)90396-4","article-title":"The ubiquitin-proteasome proteolytic pathway","volume":"79","author":"Ciechanover","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.biochi.2013.09.012_bib71","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1016\/j.ceb.2011.05.007","article-title":"Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation","volume":"23","author":"Karbowski","year":"2011","journal-title":"Curr. Opin. Cell. Biol."},{"key":"10.1016\/j.biochi.2013.09.012_bib72","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1038\/ncb0511-521","article-title":"Mitochondria unite to survive","volume":"13","author":"Blackstone","year":"2011","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/j.biochi.2013.09.012_bib73","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.bbadis.2009.07.005","article-title":"Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta","volume":"1802","author":"Du","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2013.09.012_bib74","doi-asserted-by":"crossref","first-page":"439","DOI":"10.2174\/187152710791556113","article-title":"Oxidative stress and altered mitochondrial function in neurodegenerative diseases: lessons from mouse models","volume":"9","author":"Fernandez-Checa","year":"2010","journal-title":"CNS Neurol. Disord. Drug Targets"},{"key":"10.1016\/j.biochi.2013.09.012_bib75","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"},{"key":"10.1016\/j.biochi.2013.09.012_bib76","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1091\/mbc.E10-11-0919","article-title":"Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk","volume":"22","author":"Ivashchenko","year":"2011","journal-title":"Mol. Biol. Cell."},{"key":"10.1016\/j.biochi.2013.09.012_bib77","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1172\/JCI113292","article-title":"Effects of long-chain, saturated fatty acids on membrane microviscosity and adrenocorticotropin responsiveness of human adrenocortical cells in\u00a0vitro","volume":"81","author":"Whitcomb","year":"1988","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2013.09.012_bib78","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1172\/JCI118182","article-title":"Interactions of a very long chain fatty acid with model membranes and serum albumin. Implications for the pathogenesis of adrenoleukodystrophy","volume":"96","author":"Ho","year":"1995","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2013.09.012_bib79","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1038\/nature03434","article-title":"Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death","volume":"434","author":"Baines","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2013.09.012_bib80","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1038\/nature03317","article-title":"Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death","volume":"434","author":"Nakagawa","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2013.09.012_bib81","doi-asserted-by":"crossref","first-page":"12005","DOI":"10.1073\/pnas.0505294102","article-title":"Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia","volume":"102","author":"Schinzel","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2013.09.012_bib82","doi-asserted-by":"crossref","first-page":"5887","DOI":"10.1073\/pnas.1217823110","article-title":"Dimers of mitochondrial ATP synthase form the permeability transition pore","volume":"110","author":"Giorgio","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2013.09.012_bib83","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.1093\/brain\/aws292","article-title":"Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy","volume":"135","author":"Lopez-Erauskin","year":"2012","journal-title":"Brain"},{"key":"10.1016\/j.biochi.2013.09.012_bib84","first-page":"357","article-title":"Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress","volume":"255","author":"Crompton","year":"1988","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2013.09.012_bib85","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1038\/nm.1868","article-title":"Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease","volume":"14","author":"Du","year":"2008","journal-title":"Nat. Med."},{"key":"10.1016\/j.biochi.2013.09.012_bib86","doi-asserted-by":"crossref","first-page":"7558","DOI":"10.1073\/pnas.0702228104","article-title":"Cyclophilin D inactivation protects axons in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis","volume":"104","author":"Forte","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2013.09.012_bib87","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1093\/brain\/aws304","article-title":"Cyclophilin D: a therapeutic target to counteract reactive oxygen species-mediated damage in neurodegenerative disease?","volume":"135","author":"Fransen","year":"2012","journal-title":"Brain"},{"key":"10.1016\/j.biochi.2013.09.012_bib88","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.molcel.2009.02.013","article-title":"PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death","volume":"33","author":"Gandhi","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.biochi.2013.09.012_bib89","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1042\/bj2680153","volume":"268","author":"Halestrap","year":"1990","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2013.09.012_bib90","doi-asserted-by":"crossref","first-page":"128","DOI":"10.3171\/jns.2004.101.1.0128","article-title":"Life span extension and reduced neuronal death after weekly intraventricular cyclosporin injections in the G93A transgenic mouse model of amyotrophic lateral sclerosis","volume":"101","author":"Karlsson","year":"2004","journal-title":"J.\u00a0Neurosurg."},{"key":"10.1016\/j.biochi.2013.09.012_bib91","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.bbadis.2009.07.009","article-title":"The mitochondrial permeability transition pore: a molecular target for amyotrophic lateral sclerosis therapy","volume":"1802","author":"Martin","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2013.09.012_bib92","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.expneurol.2009.02.015","article-title":"The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice","volume":"218","author":"Martin","year":"2009","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.biochi.2013.09.012_bib93","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1089\/ars.2010.3849","article-title":"Mitochondrial permeability transition pore component cyclophilin D distinguishes nigrostriatal dopaminergic death paradigms in the MPTP mouse model of Parkinson's disease","volume":"16","author":"Thomas","year":"2011","journal-title":"Antioxid. Redox Signal."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S030090841300326X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S030090841300326X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,5,8]],"date-time":"2020-05-08T17:59:03Z","timestamp":1588960743000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S030090841300326X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,3]]},"references-count":93,"alternative-id":["S030090841300326X"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2013.09.012","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2014,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mitochondrial dysfunction and oxidative damage cooperatively fuel axonal degeneration in X-linked adrenoleukodystrophy","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2013.09.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}