{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T01:44:27Z","timestamp":1776822267465,"version":"3.51.2"},"reference-count":69,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2016,10,11]],"date-time":"2016-10-11T00:00:00Z","timestamp":1476144000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Diseases"],"abstract":"<jats:p>Lysosomal storage diseases (LSDs) describe a heterogeneous group of rare inherited metabolic disorders that result from the absence or loss of function of lysosomal hydrolases or transporters, resulting in the progressive accumulation of undigested material in lysosomes. The accumulation of substances affects the function of lysosomes and other organelles, resulting in secondary alterations such as impairment of autophagy, mitochondrial dysfunction, inflammation and apoptosis. LSDs frequently involve the central nervous system (CNS), where neuronal dysfunction or loss results in progressive neurodegeneration and premature death. Many LSDs exhibit signs of mitochondrial dysfunction, which include mitochondrial morphological changes, decreased mitochondrial membrane potential (\u0394\u03a8m), diminished ATP production and increased generation of reactive oxygen species (ROS). Furthermore, reduced autophagic flux may lead to the persistence of dysfunctional mitochondria. Gaucher disease (GD), the LSD with the highest prevalence, is caused by mutations in the GBA1 gene that results in defective and insufficient activity of the enzyme \u03b2-glucocerebrosidase (GCase). Decreased catalytic activity and\/or instability of GCase leads to accumulation of glucosylceramide (GlcCer) and glucosylsphingosine (GlcSph) in the lysosomes of macrophage cells and visceral organs. Mitochondrial dysfunction has been reported to occur in numerous cellular and mouse models of GD. The aim of this manuscript is to review the current knowledge and implications of mitochondrial dysfunction in LSDs.<\/jats:p>","DOI":"10.3390\/diseases4040031","type":"journal-article","created":{"date-parts":[[2016,10,11]],"date-time":"2016-10-11T11:27:28Z","timestamp":1476185248000},"page":"31","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":59,"title":["Mitochondrial Dysfunction in Lysosomal Storage Disorders"],"prefix":"10.3390","volume":"4","author":[{"given":"Mario","family":"De la Mata","sequence":"first","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"given":"David","family":"Cot\u00e1n","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"given":"Marina","family":"Villanueva-Paz","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"given":"Isabel","family":"De Lavera","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"given":"M\u00f3nica","family":"\u00c1lvarez-C\u00f3rdoba","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2957-7981","authenticated-orcid":false,"given":"Raquel","family":"Luz\u00f3n-Hidalgo","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6260-7284","authenticated-orcid":false,"given":"Juan","family":"Su\u00e1rez-Rivero","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]},{"given":"Gustavo","family":"Tiscornia","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences and Medicine, University of Algarve, Faro 8005-139, Portugal"}]},{"given":"Manuel","family":"Oropesa-\u00c1vila","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo (CABD-CSIC-Universidad Pablo de Olavide), Sevilla 41013, Spain"}]}],"member":"1968","published-online":{"date-parts":[[2016,10,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1146\/annurev.bi.54.070185.005055","article-title":"The mitochondrial electron transport and oxidative phosphorylation system","volume":"54","author":"Hatefi","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/bies.201500013","article-title":"Mitochondrial quality control pathways as determinants of metabolic health","volume":"37","author":"Held","year":"2015","journal-title":"Bioessays"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.nbd.2015.10.011","article-title":"Mitochondrial fusion\/fission dynamics in neurodegeneration and neuronal plasticity","volume":"90","author":"Bertholet","year":"2016","journal-title":"Neurobiol. Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.biopha.2015.07.025","article-title":"Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight","volume":"74","author":"Bhat","year":"2015","journal-title":"Biomed. Pharmacother."},{"key":"ref_5","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":"ref_6","doi-asserted-by":"crossref","unstructured":"Lloyd-Evans, E., and Haslett, L.J. (2016). The lysosomal storage disease continuum with ageing-related neurodegenerative disease. Ageing Res. Rev.","DOI":"10.1016\/j.arr.2016.07.005"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"259","DOI":"10.4161\/auto.3906","article-title":"Autophagy, mitochondria and cell death in lysosomal storage diseases","volume":"3","author":"Kiselyov","year":"2007","journal-title":"Autophagy"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1083\/jcb.201208152","article-title":"The cell biology of disease: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction","volume":"199","author":"Platt","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1093\/hmg\/ddm289","article-title":"A block of autophagy in lysosomal storage disorders","volume":"17","author":"Settembre","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"20423","DOI":"10.1074\/jbc.R110.134452","article-title":"Common and uncommon pathogenic cascades in lysosomal storage diseases","volume":"285","author":"Vitner","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1089\/ars.2011.4405","article-title":"Lysosomal function and dysfunction: Mechanism and disease","volume":"17","author":"Boya","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/nrm3565","article-title":"Signals from the lysosome: A control centre for cellular clearance and energy metabolism","volume":"14","author":"Settembre","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1126\/science.290.5497.1717","article-title":"Autophagy as a regulated pathway of cellular degradation","volume":"290","author":"Klionsky","year":"2000","journal-title":"Science"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"113","DOI":"10.4161\/auto.5227","article-title":"Lysosomal storage diseases as disorders of autophagy","volume":"4","author":"Settembre","year":"2008","journal-title":"Autophagy"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"168","DOI":"10.3390\/cells1020168","article-title":"Macroautophagy and cell responses related to mitochondrial dysfunction, lipid metabolism and unconventional secretion of proteins","volume":"1","author":"Demine","year":"2012","journal-title":"Cells"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1958","DOI":"10.1111\/bph.12453","article-title":"Quality control gone wrong: Mitochondria, lysosomal storage disorders and neurodegeneration","volume":"171","author":"Osellame","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1111\/bph.12430","article-title":"Mitochondrial protein quality control in health and disease","volume":"171","author":"Baker","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.abb.2007.03.034","article-title":"Selective degradation of mitochondria by mitophagy","volume":"462","author":"Kim","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"297","DOI":"10.4161\/auto.7.3.14502","article-title":"Mitochondria removal by autophagy","volume":"7","author":"Wang","year":"2011","journal-title":"Autophagy"},{"key":"ref_20","first-page":"126","article-title":"Mitophagy: Selective degradation of mitochondria by autophagy","volume":"83","author":"Hirota","year":"2011","journal-title":"Seikagaku"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/S0065-2423(09)49003-6","article-title":"Biochemical basis of fabry disease with emphasis on mitochondrial function and protein trafficking","volume":"49","author":"Das","year":"2009","journal-title":"Adv. Clin. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1038\/nature04399","article-title":"Role of cholesterol and lipid organization in disease","volume":"438","author":"Maxfield","year":"2005","journal-title":"Nature"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1002\/ajmg.c.31317","article-title":"Autophagy and mitochondria in pompe disease: Nothing is so new as what has long been forgotten","volume":"160","author":"Raben","year":"2012","journal-title":"Am. J. Med. Genet. C Semin. Med. Genet."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1080\/15548627.2015.1009779","article-title":"Defects in calcium homeostasis and mitochondria can be reversed in pompe disease","volume":"11","author":"Lim","year":"2015","journal-title":"Autophagy"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4851","DOI":"10.1093\/hmg\/ddr424","article-title":"Human pompe disease-induced pluripotent stem cells for pathogenesis modeling, drug testing and disease marker identification","volume":"20","author":"Huang","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/S0887-8994(00)00145-4","article-title":"Mitochondrial activity in pompe\u2019s disease","volume":"23","author":"Selak","year":"2000","journal-title":"Pediatr. Neurol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"425","DOI":"10.18632\/aging.100038","article-title":"Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy","volume":"1","author":"Wu","year":"2009","journal-title":"Aging (Albany NY)"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1770","DOI":"10.1093\/hmg\/ddr610","article-title":"Impaired parkin-mediated mitochondrial targeting to autophagosomes differentially contributes to tissue pathology in lysosomal storage diseases","volume":"21","author":"Saide","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1093\/brain\/awu355","article-title":"Neuroinflammation, mitochondrial defects and neurodegeneration in mucopolysaccharidosis III type c mouse model","volume":"138","author":"Martins","year":"2015","journal-title":"Brain"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e1049793","DOI":"10.1080\/21675511.2015.1049793","article-title":"Crosstalk between 2 organelles: Lysosomal storage of heparan sulfate causes mitochondrial defects and neuronal death in mucopolysaccharidosis III type c","volume":"3","author":"Pshezhetsky","year":"2015","journal-title":"Rare Dis."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1080\/15548627.2015.1046671","article-title":"Lysosomal storage of heparan sulfate causes mitochondrial defects, altered autophagy, and neuronal death in the mouse model of mucopolysaccharidosis III type c","volume":"12","author":"Pshezhetsky","year":"2016","journal-title":"Autophagy"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Tessitore, A., Pirozzi, M., and Auricchio, A. (2009). Abnormal autophagy, ubiquitination, inflammation and apoptosis are dependent upon lysosomal storage and are useful biomarkers of mucopolysaccharidosis vi. Pathogenetics.","DOI":"10.1186\/1755-8417-2-4"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"445","DOI":"10.2174\/1566524023362276","article-title":"The molecular basis of mucolipidosis type iv","volume":"2","author":"Slaugenhaupt","year":"2002","journal-title":"Curr. Mol. Med."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"35283","DOI":"10.1074\/jbc.M111.267930","article-title":"Lysosomal storage causes cellular dysfunction in mucolipidosis II skin fibroblasts","volume":"286","author":"Otomo","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1091\/mbc.e10-07-0584","article-title":"Vacuolization of mucolipidosis type II mouse exocrine gland cells represents accumulation of autolysosomes","volume":"22","author":"Boonen","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.ymgme.2009.07.002","article-title":"Inhibition of autophagosome formation restores mitochondrial function in mucolipidosis II and III skin fibroblasts","volume":"98","author":"Otomo","year":"2009","journal-title":"Mol. Genet. Metab."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/j.molcel.2009.10.021","article-title":"Gm1-ganglioside accumulation at the mitochondria-associated er membranes links er stress to Ca(2+)-dependent mitochondrial apoptosis","volume":"36","author":"Sano","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/j.bbrc.2007.12.187","article-title":"Enhanced autophagy and mitochondrial aberrations in murine g(m1)-gangliosidosis","volume":"367","author":"Takamura","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.ymgme.2004.01.011","article-title":"Fabry disease: Reduced activities of respiratory chain enzymes with decreased levels of energy-rich phosphates in fibroblasts","volume":"82","author":"Lucke","year":"2004","journal-title":"Mol. Genet. Metab"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/8904_2013_246","article-title":"Accumulation of ordered ceramide-cholesterol domains in farber disease fibroblasts","volume":"12","author":"Ferreira","year":"2014","journal-title":"JIMD Rep."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1002\/ana.22400","article-title":"Acid beta-glucosidase mutants linked to gaucher disease, parkinson disease, and lewy body dementia alter alpha-synuclein processing","volume":"69","author":"Cullen","year":"2011","journal-title":"Ann. Neurol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.nbd.2015.09.006","article-title":"Mitochondrial dysfunction associated with glucocerebrosidase deficiency","volume":"90","author":"Gegg","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.neuint.2012.10.010","article-title":"Glucocerebrosidase inhibition causes mitochondrial dysfunction and free radical damage","volume":"62","author":"Cleeter","year":"2013","journal-title":"Neurochem. Int."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.cmet.2013.04.014","article-title":"Mitochondria and quality control defects in a mouse model of gaucher disease\u2014links to parkinson\u2019s disease","volume":"17","author":"Osellame","year":"2013","journal-title":"Cell Metab."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1093\/hmg\/ddu105","article-title":"Multiple pathogenic proteins implicated in neuronopathic gaucher disease mice","volume":"23","author":"Xu","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"21490","DOI":"10.1074\/jbc.M113.545749","article-title":"Soluble, prefibrillar alpha-synuclein oligomers promote complex i-dependent, Ca2+-induced mitochondrial dysfunction","volume":"289","author":"Luth","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1038\/ncomms5028","article-title":"Ipsc-derived neurons from gba1-associated parkinson\u2019s disease patients show autophagic defects and impaired calcium homeostasis","volume":"5","author":"Schondorf","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Uemura, N., Koike, M., Ansai, S., Kinoshita, M., Ishikawa-Fujiwara, T., Matsui, H., Naruse, K., Sakamoto, N., Uchiyama, Y., and Todo, T. (2015). Viable neuronopathic gaucher disease model in medaka (oryzias latipes) displays axonal accumulation of alpha-synuclein. PLoS Genet., 11.","DOI":"10.1371\/journal.pgen.1005065"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"6640","DOI":"10.1093\/hmg\/ddv369","article-title":"Glucocerebrosidase 1 deficient danio rerio mirror key pathological aspects of human gaucher disease and provide evidence of early microglial activation preceding alpha-synuclein-independent neuronal cell death","volume":"24","author":"Keatinge","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"10903","DOI":"10.1038\/srep10903","article-title":"Pharmacological chaperones and coenzyme q10 treatment improves mutant beta-glucocerebrosidase activity and mitochondrial function in neuronopathic forms of gaucher disease","volume":"5","author":"Cotan","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1093\/hmg\/ddt468","article-title":"Neuronal accumulation of glucosylceramide in a mouse model of neuronopathic gaucher disease leads to neurodegeneration","volume":"23","author":"Vitner","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.ymgme.2013.12.003","article-title":"Neuroinflammation and alpha-synuclein accumulation in response to glucocerebrosidase deficiency are accompanied by synaptic dysfunction","volume":"111","author":"Ginns","year":"2014","journal-title":"Mol. Genet. Metab."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1126\/science.277.5323.228","article-title":"Niemann-pick c1 disease gene: Homology to mediators of cholesterol homeostasis","volume":"277","author":"Carstea","year":"1997","journal-title":"Science"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.abb.2016.02.012","article-title":"Mitochondrial dysfunction in fibroblasts derived from patients with niemann-pick type c disease","volume":"593","author":"Wos","year":"2016","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1194\/jlr.M002345","article-title":"Mln64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional niemann-pick type c1 protein","volume":"51","author":"Charman","year":"2010","journal-title":"J. Lipid Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4876","DOI":"10.1093\/hmg\/dds324","article-title":"Impaired proteolysis underlies autophagic dysfunction in niemann-pick type c disease","volume":"21","author":"Elrick","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.4161\/auto.20668","article-title":"Defective mitophagy in human niemann-pick type c1 neurons is due to abnormal autophagy activation","volume":"8","author":"Ordonez","year":"2012","journal-title":"Autophagy"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"11731","DOI":"10.1074\/jbc.M412898200","article-title":"Altered cholesterol metabolism in niemann-pick type c1 mouse brains affects mitochondrial function","volume":"280","author":"Yu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/79095","article-title":"Identification of the gene causing mucolipidosis type iv","volume":"26","author":"Bargal","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"39041","DOI":"10.1074\/jbc.M607982200","article-title":"Mitochondrial aberrations in mucolipidosis type iv","volume":"281","author":"Jennings","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"971","DOI":"10.4161\/auto.6.7.13099","article-title":"Abnormal mitochondrial autophagy in nephropathic cystinosis","volume":"6","author":"Sansanwal","year":"2010","journal-title":"Autophagy"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1681\/ASN.2009040383","article-title":"Mitochondrial autophagy promotes cellular injury in nephropathic cystinosis","volume":"21","author":"Sansanwal","year":"2010","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1212\/WNL.0b013e31825f0547","article-title":"New nomenclature and classification scheme for the neuronal ceroid lipofuscinoses","volume":"79","author":"Williams","year":"2012","journal-title":"Neurology"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/S0197-0186(01)00128-0","article-title":"Mitochondrial dysfunction in the neuronal ceroid-lipofuscinoses (batten disease)","volume":"40","author":"Jolly","year":"2002","journal-title":"Neurochem. Int."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1002\/jnr.21015","article-title":"Batten disease (jncl) is linked to disturbances in mitochondrial, cytoskeletal, and synaptic compartments","volume":"84","author":"Luiro","year":"2006","journal-title":"J. Neurosci. Res."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"619","DOI":"10.2741\/4231","article-title":"Clinical applications of coenzyme q10","volume":"19","author":"Cordero","year":"2014","journal-title":"Front. Biosci."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"8892","DOI":"10.1073\/pnas.95.15.8892","article-title":"Coenzyme q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects","volume":"95","author":"Matthews","year":"1998","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/j.bbadis.2006.03.004","article-title":"Dose ranging and efficacy study of high-dose coenzyme q10 formulations in huntington\u2019s disease mice","volume":"1762","author":"Smith","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_69","first-page":"597","article-title":"Coenzyme q10 effects in neurodegenerative disease","volume":"5","author":"Spindler","year":"2009","journal-title":"Neuropsychiatr. Dis. Treat."}],"container-title":["Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-9721\/4\/4\/31\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:32:41Z","timestamp":1760211161000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-9721\/4\/4\/31"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10,11]]},"references-count":69,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2016,12]]}},"alternative-id":["diseases4040031"],"URL":"https:\/\/doi.org\/10.3390\/diseases4040031","relation":{},"ISSN":["2079-9721"],"issn-type":[{"value":"2079-9721","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,10,11]]}}}