{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T16:38:08Z","timestamp":1789144688622,"version":"build-2803163510"},"reference-count":245,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["425914\/2016\u20130"],"award-info":[{"award-number":["425914\/2016\u20130"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004263","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado do Rio Grande do Sul","doi-asserted-by":"publisher","award":["17\/2551-0000800-6"],"award-info":[{"award-number":["17\/2551-0000800-6"]}],"id":[{"id":"10.13039\/501100004263","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1016\/j.abb.2020.108646","type":"journal-article","created":{"date-parts":[[2020,10,21]],"date-time":"2020-10-21T11:18:44Z","timestamp":1603279124000},"page":"108646","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"special_numbering":"C","title":["Disruption of mitochondrial functions and oxidative stress contribute to neurologic dysfunction in organic acidurias"],"prefix":"10.1016","volume":"696","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9803-7746","authenticated-orcid":false,"given":"Moacir","family":"Wajner","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carmen Regla","family":"Vargas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6512-0714","authenticated-orcid":false,"given":"Alexandre Umpierrez","family":"Amaral","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2020.108646_bib1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1038\/s41582-019-0161-9","article-title":"Neurological manifestations of organic acidurias","volume":"15","author":"Wajner","year":"2019","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib2","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1007\/s10545-008-0823-z","article-title":"Pathogenesis of CNS involvement in disorders of amino and organic acid metabolism","volume":"31","author":"K\u00f6ker","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib3","article-title":"Organic acidurias: major gaps, new challenges, and a yet unfulfilled promise","author":"Dimitrov","year":"2020","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib4","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1007\/s10545-015-9839-3","article-title":"The phenotypic spectrum of organic acidurias and urea cycle disorders. Part 1: the initial presentation","volume":"38","author":"K\u00f6lker","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib5","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/8904_2016_537","article-title":"Newborn screening programmes in Europe, arguments and efforts regarding harmonisation: focus on organic acidurias","volume":"32","author":"H\u00f6rster","year":"2017","journal-title":"JIMD Rep"},{"key":"10.1016\/j.abb.2020.108646_bib6","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s10238-016-0435-0","article-title":"\u201cClassical organic acidurias\u201d: diagnosis and pathogenesis","volume":"17","author":"Villani","year":"2017","journal-title":"Clin. Exp. Med."},{"key":"10.1016\/j.abb.2020.108646_bib7","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1007\/s10545-015-9840-x","article-title":"The phenotypic spectrum of organic acidurias and urea cycle disorders. Part 2: the evolving clinical phenotype","volume":"38","author":"K\u00f6lker","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib8","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1007\/s10545-006-0278-z","article-title":"\u201cClassical\u201d organic acidurias, propionic aciduria, methylmalonic aciduria and isovaleric aciduria: long-term outcome and effects of expanded newborn screening using tandem mass spectrometry","volume":"29","author":"Dionisi-Vici","year":"2006","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib9","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1186\/1750-1172-8-148","article-title":"Long-term neurological outcome of a cohort of 80 patients with classical organic acidurias","volume":"8","author":"Nizon","year":"2013","journal-title":"Orphanet J. Rare Dis."},{"key":"10.1016\/j.abb.2020.108646_bib10","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1002\/ajmg.a.35387","article-title":"Survey of health status and complications among propionic acidemia patients","volume":"158 A","author":"Pena","year":"2012","journal-title":"Am. J. Med. Genet."},{"key":"10.1016\/j.abb.2020.108646_bib11","first-page":"179","article-title":"Inborn errors of metabolism overview: pathophysiology, manifestations, evaluation, and management","volume":"65","author":"Saudubray","year":"2018","journal-title":"Pediatr. Clin."},{"key":"10.1016\/j.abb.2020.108646_bib12","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1007\/s10545-017-0135-2","article-title":"Organic acidurias in adults: late complications and management","volume":"41","author":"Tuncel","year":"2018","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib13","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1007\/s00431-014-2359-6","article-title":"Propionic acidemia in a previously healthy adolescent with acute onset of dilated cardiomyopathy","volume":"173","author":"Laemmle","year":"2014","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib14","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1097\/PEC.0000000000001028","article-title":"Acute illness protocol for organic acidemias: methylmalonic acidemia and propionic acidemia","volume":"33","author":"Aldubayan","year":"2017","journal-title":"Pediatr. Emerg. Care"},{"key":"10.1016\/j.abb.2020.108646_bib15","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.tem.2015.12.001","article-title":"Mitochondrial dynamics and metabolic regulation","volume":"27","author":"Wai","year":"2016","journal-title":"Trends Endocrinol. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib16","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/nature11707","article-title":"Mitochondrial disorders as windows into an ancient organelle","volume":"491","author":"Vafai","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.abb.2020.108646_bib17","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1111\/j.1474-9728.2003.00079.x","article-title":"Mitochondrial membrane potential and aging","volume":"3","author":"Nicholls","year":"2004","journal-title":"Aging Cell"},{"key":"10.1016\/j.abb.2020.108646_bib18","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/ncb2012","article-title":"PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1","volume":"12","author":"Geisler","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.abb.2020.108646_bib19","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrneurol.2014.228","article-title":"Disturbed mitochondrial dynamics and neurodegenerative disorders","volume":"11","author":"Burt\u00e9","year":"2015","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib20","doi-asserted-by":"crossref","first-page":"16942","DOI":"10.1016\/S0021-9258(18)37482-9","volume":"263","author":"Schlegel","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib21","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/bj2810021","article-title":"Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the \u201cphosphocreatine circuit\u201d for cellular energy homeostasis","volume":"281","author":"Wallimann","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2020.108646_bib22","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/0005-2728(92)90096-K","article-title":"Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism","volume":"1102","author":"Wyss","year":"1992","journal-title":"BBA - Bioenerg."},{"key":"10.1016\/j.abb.2020.108646_bib23","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1089\/ars.2012.4729","article-title":"Mitochondria as a source of reactive oxygen and nitrogen species: from molecular mechanisms to human health","volume":"18","author":"Figueira","year":"2013","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.abb.2020.108646_bib24","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1002\/1873-3468.12964","article-title":"Role of mitochondrial ROS in the brain: from physiology to neurodegeneration","volume":"592","author":"Angelova","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2020.108646_bib25","doi-asserted-by":"crossref","first-page":"7779","DOI":"10.1523\/JNEUROSCI.1899-04.2004","article-title":"Mitochondrial \u03b1-ketoglutarate dehydrogenase complex generates reactive oxygen species","volume":"24","author":"Starkov","year":"2004","journal-title":"J. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib26","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1385\/MN:31:1-3:043","article-title":"The \u03b1-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration","volume":"31","author":"Gibson","year":"2005","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib27","doi-asserted-by":"crossref","first-page":"38079","DOI":"10.1074\/jbc.M205256200","article-title":"Biochemistry of mitochondrial nitric-oxide synthase","volume":"277","author":"Elfering","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib28","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0014-5793(97)01397-5","article-title":"Nitric oxide synthase activity in mitochondria","volume":"418","author":"Ghafourifar","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2020.108646_bib29","doi-asserted-by":"crossref","first-page":"11038","DOI":"10.1074\/jbc.273.18.11038","article-title":"Production of nitric oxide by mitochondria","volume":"273","author":"Giulivi","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib30","doi-asserted-by":"crossref","first-page":"14126","DOI":"10.1073\/pnas.241380298","article-title":"Identification of a neuronal nitric oxide synthase in isolated cardiac mitochondria using electrochemical detection","volume":"98","author":"Kanai","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.abb.2020.108646_bib31","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1007\/s10863-010-9309-4","article-title":"Effects of rotenone and pyridaben on complex i electron transfer and on mitochondrial nitric oxide synthase functional activity","volume":"42","author":"Navarro","year":"2010","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.abb.2020.108646_bib32","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.bbabio.2006.02.013","article-title":"Mitochondrial metabolic states and membrane potential modulate mtNOS activity","volume":"1757","author":"Valdez","year":"2006","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"10.1016\/j.abb.2020.108646_bib33","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.neuroscience.2018.02.017","article-title":"Nitric oxide and mitochondrial function in neurological diseases","volume":"376","author":"Ghasemi","year":"2018","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib34","doi-asserted-by":"crossref","first-page":"32590","DOI":"10.1074\/jbc.M806934200","article-title":"Nitrite reductase activity of cytochrome c","volume":"283","author":"Basu","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib35","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0014-5793(99)00788-7","article-title":"Nitrite reductase activity is a novel function of mammalian mitochondria","volume":"454","author":"Kozlov","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.abb.2020.108646_bib36","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1021\/bi9020378","article-title":"Signaling functions of reactive oxygen species","volume":"49","author":"Forman","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.abb.2020.108646_bib37","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.bbabio.2006.03.010","article-title":"Mitochondrial NADPH, transhydrogenase and disease","volume":"1757","author":"Rydstr\u00f6m","year":"2006","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"10.1016\/j.abb.2020.108646_bib38","doi-asserted-by":"crossref","first-page":"20173","DOI":"10.1074\/jbc.M116.730473","article-title":"The Contribution of nicotinamide nucleotide transhydrogenase to peroxide detoxification is dependent on the respiratory state and counterbalanced by other sources of NADPH in liver mitochondria","volume":"291","author":"Ronchi","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib39","series-title":"Free Radicals Biol. Med","first-page":"187","article-title":"Cellular responses to oxidative stress: adaptation, damage, repair, senescence and death","author":"Halliwell","year":"2007"},{"key":"10.1016\/j.abb.2020.108646_bib40","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nrm3412","article-title":"Mitochondria as sensors and regulators of calcium signalling","volume":"13","author":"Rizzuto","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.abb.2020.108646_bib41","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1146\/annurev-biochem-060614-034216","article-title":"Enjoy the trip: calcium in mitochondria back and forth","volume":"85","author":"De Stefani","year":"2016","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.abb.2020.108646_bib42","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1177\/0271678X16680637","article-title":"Mitochondrial calcium homeostasis: implications for neurovascular and neurometabolic coupling","volume":"37","author":"Kannurpatti","year":"2017","journal-title":"J. Cerebr. Blood Flow Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2018.08.034","article-title":"Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition","volume":"129","author":"Vercesi","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2020.108646_bib44","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.neuint.2016.12.018","article-title":"Brain mitochondrial calcium transport: origins of the set-point concept and its application to physiology and pathology","volume":"109","author":"Nicholls","year":"2017","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.abb.2020.108646_bib45","doi-asserted-by":"crossref","first-page":"10479","DOI":"10.1073\/pnas.1300410110","article-title":"Mitochondrial calcium uptake","volume":"110","author":"Williams","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.abb.2020.108646_bib46","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/978-3-319-55330-6_2","article-title":"Mitochondrial calcium handling in physiology and disease","volume":"982","author":"Granatiero","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.abb.2020.108646_bib47","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.ceca.2012.03.004","article-title":"The permeability transition pore as a Ca2+ release channel: new answers to an old question","volume":"52","author":"Bernardi","year":"2012","journal-title":"Cell Calcium"},{"key":"10.1016\/j.abb.2020.108646_bib48","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.ceca.2011.04.007","article-title":"Mitochondrial permeability transition in Ca2+-dependent apoptosis and necrosis","volume":"50","author":"Rasola","year":"2011","journal-title":"Cell Calcium"},{"key":"10.1016\/j.abb.2020.108646_bib49","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s12640-019-00061-7","article-title":"Mitochondria and the brain: bioenergetics and beyond","volume":"36","author":"Belenguer","year":"2019","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.abb.2020.108646_bib50","doi-asserted-by":"crossref","first-page":"10625","DOI":"10.1073\/pnas.91.22.10625","article-title":"Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization","volume":"91","author":"Pellerin","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.abb.2020.108646_bib51","doi-asserted-by":"crossref","first-page":"3347","DOI":"10.1002\/jnr.21444","article-title":"The glutamate-glutamine cycle is not stoichiometric: fates of glutamate in brain","volume":"85","author":"McKenna","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib52","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1111\/jnc.12812","article-title":"Glutamate synthesis has to be matched by its degradation - where do all the carbons go?","volume":"131","author":"Sonnewald","year":"2014","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib53","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1177\/0271678X16629482","article-title":"Compartmentalised energy metabolism supporting glutamatergic neurotransmission in response to increased activity in the rat cerebral cortex: a 13C MRS study in vivo at 14.1 T","volume":"36","author":"Sonnay","year":"2015","journal-title":"J. Cerebr. Blood Flow Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib54","doi-asserted-by":"crossref","first-page":"288","DOI":"10.3389\/fnins.2017.00288","article-title":"How energy metabolism supports cerebral function: insights from 13C magnetic resonance studies in vivo","volume":"11","author":"Sonnay","year":"2017","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/j.mam.2019.10.003","article-title":"Neurological disorders and mitochondria","volume":"71","author":"Cabral-Costa","year":"2020","journal-title":"Mol. Aspect. Med."},{"key":"10.1016\/j.abb.2020.108646_bib56","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.mito.2018.11.002","article-title":"Mitochondrial dynamics, a key executioner in neurodegenerative diseases","volume":"47","author":"Panchal","year":"2019","journal-title":"Mitochondrion"},{"key":"10.1016\/j.abb.2020.108646_bib57","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s10863-011-9324-0","article-title":"Disruption of mitochondrial homeostasis in organic acidurias: insights from human and animal studies","volume":"43","author":"Wajner","year":"2011","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.abb.2020.108646_bib58","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1016\/S0140-6736(89)92366-0","article-title":"Mitochondrial complex I deficiency in Parkinson\u2019s disease","volume":"333","author":"Schapira","year":"1989","journal-title":"Lancet"},{"key":"10.1016\/j.abb.2020.108646_bib59","doi-asserted-by":"crossref","first-page":"2142","DOI":"10.1111\/j.1471-4159.1990.tb05809.x","article-title":"Anatomic and disease specificity of NADH CoQ1 reductase (Complex I) deficiency in Parkinson's disease","volume":"55","author":"Schapira","year":"1990","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib60","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1111\/j.1471-4159.1992.tb09439.x","article-title":"Brain cytochrome oxidase in alzheimer's disease","volume":"59","author":"Kish","year":"1992","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib61","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1212\/WNL.40.8.1302","article-title":"Cytochrome oxidase deficiency in Alzheimer's disease","volume":"40","author":"Parker","year":"1990","journal-title":"Neurology"},{"key":"10.1016\/j.abb.2020.108646_bib62","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1002\/ana.410390317","article-title":"Mitochondrial defect in Huntington's disease caudate nucleus","volume":"39","author":"Gu","year":"1996","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib63","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1002\/ana.410410514","article-title":"Oxidative damage and metabolic dysfunction in huntington's disease: selective vulnerability of the basal ganglia","volume":"41","author":"Browne","year":"1997","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib64","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1038\/13518","article-title":"Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization","volume":"5","author":"Sawa","year":"1999","journal-title":"Nat. Med."},{"key":"10.1016\/j.abb.2020.108646_bib65","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1007\/s10545-013-9600-8","article-title":"Current concepts in organic acidurias: understanding intra- and extracerebral disease manifestation","volume":"36","author":"Kolker","year":"2013","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib66","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s10863-011-9330-2","article-title":"Mitochondrial energy metabolism in neurodegeneration associated with methylmalonic acidemia","volume":"43","author":"Melo","year":"2011","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.abb.2020.108646_bib67","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/s10545-007-0571-5","article-title":"Neurodegeneration and chronic renal failure in methylmalonic aciduria - a pathophysiological approach","volume":"31","author":"Morath","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib68","doi-asserted-by":"crossref","first-page":"390","DOI":"10.14336\/AD.2015.0827","article-title":"Phenylketonuria pathophysiology: on the role of metabolic alterations","volume":"6","author":"Schuck","year":"2015","journal-title":"Aging Dis"},{"key":"10.1016\/j.abb.2020.108646_bib69","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20150240","article-title":"Mitochondrial dysfunction in fatty acid oxidation disorders: insights from human and animal studies","volume":"36","author":"Wajner","year":"2016","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.abb.2020.108646_bib70","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2012\/428010","article-title":"Mechanism of oxidative stress in neurodegeneration","author":"Gandhi","year":"2012","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2020.108646_bib71","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.mito.2019.07.003","article-title":"Mitochondrial dysfunction in neurodegenerative diseases and drug targets via apoptotic signaling","volume":"49","author":"Wu","year":"2019","journal-title":"Mitochondrion"},{"key":"10.1016\/j.abb.2020.108646_bib72","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1007\/s00204-007-0209-2","article-title":"Comparative study of activities in reactive oxygen species production\/defense system in mitochondria of rat brain and liver, and their susceptibility to methylmercury toxicity","volume":"81","author":"Mori","year":"2007","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.abb.2020.108646_bib73","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1016\/j.neuroscience.2008.10.015","article-title":"\u03b1-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ","volume":"158","author":"Z\u00fcndorf","year":"2009","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib74","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.freeradbiomed.2017.02.046","article-title":"Protein S-glutathionylation alters superoxide\/hydrogen peroxide emission from pyruvate dehydrogenase complex","volume":"106","author":"O'Brien","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2020.108646_bib75","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/aps.2009.24","article-title":"Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases","volume":"30","author":"Dong","year":"2009","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.abb.2020.108646_bib76","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.ejphar.2012.10.032","article-title":"Excitotoxicity: bridge to various triggers in neurodegenerative disorders","volume":"698","author":"Mehta","year":"2013","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.abb.2020.108646_bib77","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2015\/964518","article-title":"Mechanisms of neuronal protection against excitotoxicity, endoplasmic reticulum stress, and mitochondrial dysfunction in stroke and neurodegenerative diseases","author":"Prentice","year":"2015","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2020.108646_bib78","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1023\/A:1025682611389","article-title":"Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: implications for the pathogenesis of neurodegenerative diseases","volume":"28","author":"Rego","year":"2003","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.abb.2020.108646_bib79","doi-asserted-by":"crossref","first-page":"3593","DOI":"10.1111\/j.1742-4658.2005.04781.x","article-title":"Oxidative stress is involved in the permeabilization of the inner membrane of brain mitochondria exposed to hypoxia\/reoxygenation and low micromolar Ca2+","volume":"272","author":"Schild","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.abb.2020.108646_bib80","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1002\/jnr.22658","article-title":"Reversible inhibition of hydrogen peroxide elimination by calcium in brain mitochondria","volume":"89","author":"Tretter","year":"2011","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib81","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1471-4159.1989.tb09133.x","article-title":"Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease","volume":"52","author":"Dexter","year":"1989","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib82","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1002\/ana.410320616","article-title":"The oxidant stress hypothesis in Parkinson's disease: evidence supporting it","volume":"32","author":"Fahn","year":"1992","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib83","doi-asserted-by":"crossref","first-page":"1594","DOI":"10.1212\/WNL.45.8.1594","article-title":"Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in alzheimer's disease","volume":"45","author":"Lovell","year":"1995","journal-title":"Neurology"},{"key":"10.1016\/j.abb.2020.108646_bib84","doi-asserted-by":"crossref","first-page":"2146","DOI":"10.1046\/j.1471-4159.1995.65052146.x","article-title":"Brain regional correspondence between alzheimer's disease histopathology and biomarkers of protein oxidation","volume":"65","author":"Hensley","year":"1995","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib85","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1111\/j.1749-6632.1996.tb39057.x","article-title":"Reactive oxygen species as causal agents in the neurotoxicity of the Alzheimer's disease-associated amyloid beta peptide","volume":"786","author":"Hensley","year":"1996","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.abb.2020.108646_bib86","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1007\/s10534-011-9504-8","article-title":"Transition metal abnormalities in progressive dementias","volume":"25","author":"Akatsu","year":"2012","journal-title":"Biometals"},{"key":"10.1016\/j.abb.2020.108646_bib87","article-title":"Meta-analysis of brain iron levels of Parkinson's disease patients determined by postmortem and MRI measurements","volume":"6","author":"Wang","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2020.108646_bib88","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1111\/j.1600-0404.1993.tb00013.x","article-title":"Altered mitochondrial function, iron metabolism and glutathione levels in Parkinson's disease","volume":"87","author":"Jenner","year":"1993","journal-title":"Acta Neurol. Scand. Suppl."},{"key":"10.1016\/j.abb.2020.108646_bib89","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.redox.2017.10.014","article-title":"Oxidative stress and the amyloid beta peptide in Alzheimer's disease","volume":"14","author":"Cheignon","year":"2018","journal-title":"Redox Biol"},{"key":"10.1016\/j.abb.2020.108646_bib90","doi-asserted-by":"crossref","first-page":"797","DOI":"10.2147\/DDDT.S130514","article-title":"Proteinopathy, oxidative stress and mitochondrial dysfunction: cross talk in alzheimer's disease and Parkinson's disease","volume":"11","author":"Ganguly","year":"2017","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.abb.2020.108646_bib91","doi-asserted-by":"crossref","first-page":"E4676","DOI":"10.1073\/pnas.1614943114","article-title":"KEAP1-modifying small molecule reveals muted NRF2 signaling responses in neural stem cells from Huntington's disease patients","volume":"114","author":"Quinti","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.abb.2020.108646_bib92","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/s10863-010-9288-5","article-title":"Mitochondrial functional alterations in relation to pathophysiology of Huntington's disease","volume":"42","author":"Pandey","year":"2010","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.abb.2020.108646_bib93","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1007\/s10545-015-9863-3","article-title":"Disturbance of redox homeostasis as a contributing underlying pathomechanism of brain and liver alterations in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency","volume":"38","author":"Leipnitz","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib94","first-page":"1","article-title":"Altered redox homeostasis in branched-chain amino acid disorders, organic acidurias, and homocystinuria","author":"Richard","year":"2018","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2020.108646_bib95","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1023\/B:BOLI.0000037353.13085.e2","article-title":"The role of oxidative damage in the neuropathology of organic acidurias: insights from animal studies","volume":"27","author":"Wajner","year":"2004","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib96","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/j.mito.2004.07.021","article-title":"Mitochondrial damage and dysfunction in traumatic brain injury","volume":"4","author":"Lifshitz","year":"2004","journal-title":"Mitochondrion"},{"key":"10.1016\/j.abb.2020.108646_bib97","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1002\/jnr.20292","article-title":"Mitochondrial permeability transition in CNS trauma: cause or effect of neuronal cell death?","volume":"79","author":"Sullivan","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib98","doi-asserted-by":"crossref","first-page":"229","DOI":"10.3390\/cells7120229","article-title":"Mitochondrial metabolism in major neurological diseases","volume":"7","author":"Zhou","year":"2018","journal-title":"Cells"},{"key":"10.1016\/j.abb.2020.108646_bib99","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1007\/s12035-018-1204-8","article-title":"Pharmacological sequestration of mitochondrial calcium uptake protects neurons against glutamate excitotoxicity","volume":"56","author":"Angelova","year":"2019","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib100","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1152\/physrev.2000.80.1.315","article-title":"Mitochondria and neuronal survival","volume":"80","author":"Nicholls","year":"2000","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.abb.2020.108646_bib101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2019\/1681254","article-title":"Overexpression of mitochondrial calcium uniporter causes neuronal death","author":"Granatiero","year":"2019","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.abb.2020.108646_bib102","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.bbamcr.2018.10.016","article-title":"Calcium, mitochondria and cell metabolism: a functional triangle in bioenergetics","volume":"1866","author":"Rossi","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"10.1016\/j.abb.2020.108646_bib103","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1016\/j.drudis.2018.08.001","article-title":"Mitochondrial permeability transition pore: a potential drug target for neurodegeneration","volume":"23","author":"Kalani","year":"2018","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.abb.2020.108646_bib104","doi-asserted-by":"crossref","first-page":"3622","DOI":"10.1111\/j.1742-4658.2010.07754.x","article-title":"Calcium-dependent mitochondrial function and dysfunction in neurons: Minireview","volume":"277","author":"Pivovarova","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.abb.2020.108646_bib105","series-title":"GeneReviews\u00ae [Internet]","first-page":"1993","article-title":"Propionic acidemia","author":"Shchelochkov","year":"2016"},{"key":"10.1016\/j.abb.2020.108646_bib106","series-title":"GeneReviews\u00ae [Internet]","first-page":"1993","article-title":"Isolated Methylmalonic acidemia","author":"Manoli","year":"2016"},{"key":"10.1016\/j.abb.2020.108646_bib107","doi-asserted-by":"crossref","first-page":"S68","DOI":"10.1007\/BF02138781","article-title":"Propionic acidaemia: clinical, biochemical and therapeutic aspects - experience in 30 patients","volume":"153","author":"Lehnert","year":"1994","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib108","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1111\/j.1442-200X.2011.03412.x","article-title":"Neonatal lactic acidosis with methylmalonic aciduria due to novel mutations in the SUCLG1 gene","volume":"53","author":"Sakamoto","year":"2011","journal-title":"Pediatr. Int."},{"key":"10.1016\/j.abb.2020.108646_bib109","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1515\/jpem-2012-0148","article-title":"Citric acid as the last therapeutic approach in an acute life-threatening metabolic decompensation of propionic acidaemia","volume":"26","author":"Siekmeyer","year":"2013","journal-title":"J. Pediatr. Endocrinol. Metab."},{"key":"10.1016\/j.abb.2020.108646_bib110","first-page":"831","article-title":"Multi-slice proton MR spectroscopy and diffusion-weighted imaging in methylmalonic acidemia: report of two cases and review of the literature","volume":"22","author":"Trinh","year":"2001","journal-title":"Am. J. Neuroradiol."},{"key":"10.1016\/j.abb.2020.108646_bib111","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1620\/tjem.137.329","article-title":"Comparison of cytosolic and mitochondrial enzyme alterations in the livers of propionic or methylmalonic acidemia: a reduction of cytochrome oxidase activity","volume":"137","author":"Hayasaka","year":"1982","journal-title":"Tohoku J. Exp. Med."},{"key":"10.1016\/j.abb.2020.108646_bib112","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1042\/BJ20060221","article-title":"Secondary mitochondrial dysfunction in propionic aciduria: a pathogenic role for endogenous mitochondrial toxins","volume":"398","author":"Schwab","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.abb.2020.108646_bib113","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1096\/fj.08-121848","article-title":"Mitochondrial dysfunction in mut methylmalonic acidemia","volume":"23","author":"Chandler","year":"2009","journal-title":"Faseb. J."},{"key":"10.1016\/j.abb.2020.108646_bib114","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1203\/PDR.0b013e3181a7c270","article-title":"Multiple OXPHOS deficiency in the liver, kidney, heart, and skeletal muscle of patients with methylmalonic aciduria and propionic aciduria","volume":"66","author":"De Keyzer","year":"2009","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.abb.2020.108646_bib115","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1111\/cge.12426","article-title":"Methylmalonic aciduria cblB type: characterization of two novel mutations and mitochondrial dysfunction studies","volume":"87","author":"Brasil","year":"2015","journal-title":"Clin. Genet."},{"key":"10.1016\/j.abb.2020.108646_bib116","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1002\/path.2248","article-title":"Methylmalonic acidaemia leads to increased production of reactive oxygen species and induction of apoptosis through the mitochondrial\/caspase pathway","volume":"213","author":"Richard","year":"2007","journal-title":"J. Pathol."},{"key":"10.1016\/j.abb.2020.108646_bib117","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1007\/s10545-009-1150-8","article-title":"Coenzyme Q10 is decreased in fibroblasts of patients with methylmalonic aciduria but not in mevalonic aciduria","volume":"32","author":"Haas","year":"2009","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib118","doi-asserted-by":"crossref","first-page":"309","DOI":"10.3109\/01913123.2014.921657","article-title":"Abnormal hepatocellular mitochondria in methylmalonic acidemia","volume":"38","author":"Wilnai","year":"2014","journal-title":"Ultrastruct. Pathol."},{"key":"10.1016\/j.abb.2020.108646_bib119","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1038\/s41467-020-14729-8","article-title":"Impaired mitophagy links mitochondrial disease to epithelial stress in methylmalonyl-CoA mutase deficiency","volume":"11","author":"Luciani","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2020.108646_bib120","doi-asserted-by":"crossref","DOI":"10.1172\/jci.insight.124351","article-title":"FGF21 underlies a hormetic response to metabolic stress in methylmalonic acidemia","volume":"3","author":"Manoli","year":"2018","journal-title":"JCI Insight"},{"key":"10.1016\/j.abb.2020.108646_bib121","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.ymgme.2019.10.007","article-title":"Tricarboxylic acid cycle enzyme activities in a mouse model of methylmalonic aciduria","volume":"128","author":"Wongkittichote","year":"2019","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib122","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2016.04.007","article-title":"In vivo evidence of mitochondrial dysfunction and altered redox homeostasis in a genetic mouse model of propionic acidemia: implications for the pathophysiology of this disorder","volume":"96","author":"Gallego-Villar","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2020.108646_bib123","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbadis.2019.165586","article-title":"Intracellular calcium mishandling leads to cardiac dysfunction and ventricular arrhythmias in a mouse model of propionic acidemia","volume":"1866","author":"Tamayo","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.abb.2020.108646_bib124","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1007\/BF00711314","article-title":"Mitochondrial 2-methylacetoacetyl-CoA thiolase deficiency: an inborn error of isoleucine and ketone body metabolism","volume":"16","author":"Sovik","year":"1993","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib125","series-title":"Metab. Mol. Bases Inherit. Dis.","first-page":"2328","article-title":"Inborn Errors of Ketone Body Metabolism","author":"Mitchell","year":"2001"},{"key":"10.1016\/j.abb.2020.108646_bib126","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/BF01804391","article-title":"Urinary excretion of 2-methylacetoacetate, 2-methyl-3-hydroxybutyrate and tiglylglycine after isoleucine loading in the diagnosis of 2-methylacetoacetyl-CoA thiolase deficiency","volume":"14","author":"Aramaki","year":"1991","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib127","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1056\/NEJM197604292941823","article-title":"Patient with defect in leucine metabolism","volume":"294","author":"Faull","year":"1976","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.abb.2020.108646_bib128","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1007\/BF02171564","article-title":"The contribution of protein catabolism to metabolic decompensation in 3-hydroxy-3-methylglutaric aciduria","volume":"149","author":"Thompson","year":"1990","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib129","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1824-7288-39-33","article-title":"A neonatal case of 3-hydroxy-3-methylglutaric-coenzyme A lyase deficiency","volume":"39","author":"Santarelli","year":"2013","journal-title":"Ital. J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib130","series-title":"Metab. Mol. Bases Inherit. Dis","first-page":"2340","article-title":"Branched chain organic acidurias","author":"Sweetman","year":"2001"},{"key":"10.1016\/j.abb.2020.108646_bib131","first-page":"378","article-title":"MR imaging and proton spectroscopy in 3-hydroxy-3-methylglutaryl coenzyme A lyase deficiency","volume":"19","author":"van der Knaap","year":"1998","journal-title":"AJNR Am. J. Neuroradiol."},{"key":"10.1016\/j.abb.2020.108646_bib132","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0887-8994(99)00013-2","article-title":"MRI and MRS in HMG-CoA lyase deficiency","volume":"20","author":"Yalcinkaya","year":"1999","journal-title":"Pediatr. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib133","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.pediatrneurol.2006.01.009","article-title":"Corticospinal tract involvement in a patient with 3-HMG coenzyme A lyase deficiency","volume":"35","author":"Yylmaz","year":"2006","journal-title":"Pediatr. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib134","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.pediatrneurol.2007.02.007","article-title":"3-Hydroxy-3-methylglutaryl coenzyme a lyase deficiency with reversible white matter changes after treatment","volume":"37","author":"Zafeiriou","year":"2007","journal-title":"Pediatr. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib135","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1007\/BF00441397","article-title":"3-Hydroxy-3-methylglutaryl-coenzyme A lyase deficiency: review of 18 reported patients","volume":"148","author":"Gibson","year":"1988","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib136","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1186\/s13023-017-0612-6","article-title":"Extrastriatal changes in patients with late-onset glutaric aciduria type i highlight the risk of long-term neurotoxicity","volume":"12","author":"Boy","year":"2017","journal-title":"Orphanet J. Rare Dis."},{"key":"10.1016\/j.abb.2020.108646_bib137","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/S0022-3476(77)81240-7","article-title":"Glutaric aciduria: biochemical and morphologic considerations","volume":"90","author":"Goodman","year":"1977","journal-title":"J. Pediatr."},{"key":"10.1016\/j.abb.2020.108646_bib138","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1203\/01.pdr.0000219387.79887.86","article-title":"Natural history, outcome, and treatment efficacy in children and adults with glutaryl-CoA dehydrogenase deficiency","volume":"59","author":"K\u00f6lker","year":"2006","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.abb.2020.108646_bib139","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1023\/B:BOLI.0000045771.66300.2a","article-title":"Neuroradiological findings in glutaric aciduria type I (glutaryl-CoA dehydrogenase deficiency)","volume":"27","author":"Neumaier-Probst","year":"2004","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib140","series-title":"Glutaric Acidemia Type 1","first-page":"1993","author":"Larson","year":"2019"},{"key":"10.1016\/j.abb.2020.108646_bib141","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1093\/brain\/awh401","article-title":"Neuropathological, biochemical and molecular findings in a glutaric acidemia type 1 cohort","volume":"128","author":"Funk","year":"2005","journal-title":"Brain"},{"key":"10.1016\/j.abb.2020.108646_bib142","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1007\/s10545-014-9676-9","article-title":"Unravelling the complex MRI pattern in glutaric aciduria type I using statistical models\u2014a cohort study in 180 patients","volume":"37","author":"Garbade","year":"2014","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib143","doi-asserted-by":"crossref","first-page":"1764","DOI":"10.1093\/brain\/awp112","article-title":"Dynamic changes of striatal and extrastriatal abnormalities in glutaric aciduria type I","volume":"132","author":"Harting","year":"2009","journal-title":"Brain"},{"key":"10.1016\/j.abb.2020.108646_bib144","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1007\/s10545-015-9826-8","article-title":"1H-MRS in glutaric aciduria type 1: impact of biochemical phenotype and age on the cerebral accumulation of neurotoxic metabolites","volume":"38","author":"Harting","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib145","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1093\/brain\/awm058","article-title":"Multimodal imaging of striatal degeneration in Amish patients with glutaryl-CoA dehydrogenase deficiency","volume":"130","author":"Strauss","year":"2007","journal-title":"Brain"},{"key":"10.1016\/j.abb.2020.108646_bib146","doi-asserted-by":"crossref","first-page":"2392","DOI":"10.1002\/mds.22313","article-title":"Spectrum of movement disorders associated with glutaric aciduria type 1: a study of 16 patients","volume":"23","author":"Gitiaux","year":"2008","journal-title":"Mov. Disord."},{"key":"10.1016\/j.abb.2020.108646_bib147","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1093\/hmg\/11.4.347","article-title":"Biochemical, pathologic and behavioral analysis of a mouse model of glutaric acidemia type I","volume":"11","author":"Koeller","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.abb.2020.108646_bib148","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1093\/brain\/awl009","article-title":"A diet-induced mouse model for glutaric aciduria type I","volume":"129","author":"Zinnanti","year":"2006","journal-title":"Brain"},{"key":"10.1016\/j.abb.2020.108646_bib149","doi-asserted-by":"crossref","first-page":"3258","DOI":"10.1172\/JCI31617","article-title":"Mechanism of age-dependent susceptibility and novel treatment strategy in glutaric acidemia type I","volume":"117","author":"Zinnanti","year":"2007","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.abb.2020.108646_bib150","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.ymgme.2012.04.015","article-title":"Marked reduction of Na+, K+-ATPase and creatine kinase activities induced by acute lysine administration in glutaryl-CoA dehydrogenase deficient mice","volume":"107","author":"Amaral","year":"2012","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib151","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.ymgme.2012.08.016","article-title":"Reduction of Na+, K+-ATPase activity and expression in cerebral cortex of glutaryl-CoA dehydrogenase deficient mice: a possible mechanism for brain injury in glutaric aciduria type I","volume":"107","author":"Amaral","year":"2012","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib152","doi-asserted-by":"crossref","first-page":"6459","DOI":"10.1007\/s12035-015-9548-9","article-title":"Oxidative stress, disrupted energy metabolism, and altered signaling pathways in glutaryl-CoA dehydrogenase knockout mice: potential implications of quinolinic acid toxicity in the neuropathology of glutaric acidemia type I","volume":"53","author":"Seminotti","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib153","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.brainres.2015.05.013","article-title":"Experimental evidence that bioenergetics disruption is not mainly involved in the brain injury of glutaryl-CoA dehydrogenase deficient mice submitted to lysine overload","volume":"1620","author":"Amaral","year":"2015","journal-title":"Brain Res."},{"key":"10.1016\/j.abb.2020.108646_bib154","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.bbadis.2014.12.022","article-title":"Multifactorial modulation of susceptibility to l-lysine in an animal model of glutaric aciduria type I","volume":"1852","author":"Sauer","year":"2015","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.abb.2020.108646_bib155","doi-asserted-by":"crossref","first-page":"2946","DOI":"10.1016\/j.celrep.2018.08.014","article-title":"Disease-linked glutarylation impairs function and interactions of mitochondrial proteins and contributes to mitochondrial heterogeneity","volume":"24","author":"Schmiesing","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.abb.2020.108646_bib156","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.ijdevneu.2019.05.005","article-title":"Pathogenesis of brain damage in glutaric acidemia type I: lessons from the genetic mice model","volume":"78","author":"Wajner","year":"2019","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib157","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/BF02312516","article-title":"D-2-hydroxyglutaric aciduria: case report and biochemical studies","volume":"3","author":"Chalmers","year":"1980","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib158","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1023\/A:1005548005393","article-title":"D-2-hydroxyglutaric aciduria: further clinical delineation","volume":"22","author":"van der Knaap","year":"1999","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib159","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1002\/1531-8249(199901)45:1<111::AID-ART17>3.0.CO;2-N","article-title":"D-2-Hydroxyglutaric aciduria: biochemical marker or clinical disease entity?","volume":"45","author":"van der Knaap","year":"1999","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib160","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1007\/s10545-012-9462-5","article-title":"Progress in understanding 2-hydroxyglutaric acidurias","volume":"35","author":"Kranendijk","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib161","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/BF02312543","article-title":"L-2-Hydroxyglutaric aciduria: an inborn error of metabolism?","volume":"3","author":"Duran","year":"1980","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib162","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0887-8994(94)90067-1","article-title":"d-2-Hydroxyglutaric aciduria in neonate with seizures and CNS dysfunction","volume":"10","author":"Craigen","year":"1994","journal-title":"Pediatr. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib163","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1148\/radiol.2513080647","article-title":"L-2-Hydroxyglutaric aciduria: pattern of MR imaging abnormalities in 56 patients","volume":"251","author":"Steenweg","year":"2009","journal-title":"Radiology"},{"key":"10.1016\/j.abb.2020.108646_bib164","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1002\/humu.21197","article-title":"An overview of L-2-hydroxyglutarate dehydrogenase gene (L2HGDH) variants: a genotype-phenotype study","volume":"31","author":"Steenweg","year":"2010","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.abb.2020.108646_bib165","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/BF01799264","article-title":"L-2-Hydroxyglutaric aciduria: neuropathological correlations and first report of severe neurodegenerative disease and neonatal death","volume":"19","author":"Chen","year":"1996","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib166","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1023\/A:1005316121584","article-title":"L-2-hydroxyglutaric aciduria and lactic acidosis","volume":"21","author":"Barth","year":"1998","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib167","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.ijdevneu.2010.01.002","article-title":"Reduction of lipid and protein damage in patients with disorders of propionate metabolism under treatment: a possible protective role of l-carnitine supplementation","volume":"28","author":"Ribas","year":"2010","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib168","doi-asserted-by":"crossref","first-page":"3941","DOI":"10.1073\/pnas.0813409106","article-title":"Inherited disorders affecting mitochondrial function are associated with glutathione deficiency and hypocitrullinemia","volume":"106","author":"Atkuri","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.abb.2020.108646_bib169","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s10571-011-9736-8","article-title":"Oxidative stress parameters in urine from patients with disorders of propionate metabolism: a beneficial effect of L-carnitine supplementation","volume":"32","author":"Ribas","year":"2012","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib170","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.ymgme.2009.06.007","article-title":"Profiling of oxidative stress in patients with inborn errors of metabolism","volume":"98","author":"Mc Guire","year":"2009","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib171","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.mrgentox.2010.07.008","article-title":"Prevention by l-carnitine of DNA damage induced by propionic and l-methylmalonic acids in human peripheral leukocytes in vitro","volume":"702","author":"Ribas","year":"2010","journal-title":"Mutat. Res. Genet. Toxicol. Environ. Mutagen"},{"key":"10.1016\/j.abb.2020.108646_bib172","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S0306-4522(97)00594-0","article-title":"Methylmalonate toxicity in primary neuronal cultures","volume":"86","author":"McLaughlin","year":"1998","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib173","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1007\/s10545-012-9545-3","article-title":"Functional characterization of novel genotypes and cellular oxidative stress studies in propionic acidemia","volume":"36","author":"Gallego-Villar","year":"2013","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib174","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/s11010-014-2322-x","article-title":"Increased oxidative stress in patients with 3-hydroxy-3-methylglutaric aciduria","volume":"402","author":"dos Santos Mello","year":"2015","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.abb.2020.108646_bib175","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.abb.2019.04.008","article-title":"Prevention by L-carnitine of DNA damage induced by 3-hydroxy-3-methylglutaric and 3-methylglutaric acids and experimental evidence of lipid and DNA damage in patients with 3-hydroxy-3-methylglutaric aciduria","volume":"668","author":"Delgado","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.abb.2020.108646_bib176","doi-asserted-by":"crossref","first-page":"10021","DOI":"10.1002\/jcb.27332","article-title":"Oxidative damage in glutaric aciduria type I patients and the protective effects of l-carnitine treatment","volume":"119","author":"Guerreiro","year":"2018","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.abb.2020.108646_bib177","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.ymgme.2012.03.002","article-title":"Induction of oxidative stress in brain of glutaryl-CoA dehydrogenase deficient mice by acute lysine administration","volume":"106","author":"Seminotti","year":"2012","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib178","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.ymgme.2012.11.001","article-title":"Disruption of brain redox homeostasis in glutaryl-CoA dehydrogenase deficient mice treated with high dietary lysine supplementation","volume":"108","author":"Seminotti","year":"2013","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib179","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.1016\/j.bbadis.2019.06.007","article-title":"L-Carnitine prevents oxidative stress in striatum of glutaryl-CoA dehydrogenase deficient mice submitted to lysine overload","volume":"1865","author":"Guerreiro","year":"2019","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.abb.2020.108646_bib180","doi-asserted-by":"crossref","first-page":"4504","DOI":"10.1093\/hmg\/ddv175","article-title":"Striatal neuronal death mediated by astrocytes from the Gcdh-\/- mouse model of glutaric acidemia type I","volume":"24","author":"Olivera-Bravo","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.abb.2020.108646_bib181","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.tiv.2017.04.006","article-title":"Experimental evidence of oxidative stress in patients with L-2-hydroxyglutaric aciduria and that L-carnitine attenuates in vitro DNA damage caused by D-2-hydroxyglutaric and L-2-hydroxyglutaric acids","volume":"42","author":"Rodrigues","year":"2017","journal-title":"Toxicol. Vitro"},{"key":"10.1016\/j.abb.2020.108646_bib182","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.3109\/10715762.2012.689428","article-title":"Oxidative damage of DNA, RNA and their metabolites in leukocytes, plasma and urine of Macaca mulatta: 8-oxoguanosine in urine is a useful marker for aging","volume":"46","author":"Shi","year":"2012","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.abb.2020.108646_bib183","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1038\/jhg.2014.4","article-title":"Founder effect confirmation of c.241A>G mutation in the L2HGDH gene and characterization of oxidative stress parameters in six Tunisian families with L-2-hydroxyglutaric aciduria","volume":"59","author":"Jellouli","year":"2014","journal-title":"J. Hum. Genet."},{"key":"10.1016\/j.abb.2020.108646_bib184","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0197-0186(01)00130-9","article-title":"Inhibition of the mitochondrial respiratory chain complex activities in rat cerebral cortex by methylmalonic acid","volume":"40","author":"Brusque","year":"2002","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.abb.2020.108646_bib185","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.ijdevneu.2005.10.005","article-title":"Differential inhibitory effects of methylmalonic acid on respiratory chain complex activities in rat tissues","volume":"24","author":"Pettenuzzo","year":"2006","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib186","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/BF00711328","article-title":"Inhibition of succinate dehydrogenase and \u03b2-hydroxybutyrate dehydrogenase activities by methylmalonate in brain and liver of developing rats","volume":"16","author":"Dutra","year":"1993","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib187","doi-asserted-by":"crossref","first-page":"14674","DOI":"10.1074\/jbc.M200997200","article-title":"Neurodegeneration in methylmalonic aciduria involves inhibition of complex II and the tricarboxylic acid cycle, and synergistically acting excitotoxicity","volume":"277","author":"Okun","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2020.108646_bib188","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1111\/j.1471-4159.1993.tb03634.x","article-title":"Inhibition of succinate dehydrogenase by malonic acid produces an \u201cexcitotoxic\u201d lesion in rat striatum","volume":"61","author":"Greene","year":"1993","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib189","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1046\/j.1528-1157.2003.42902.x","article-title":"Intrastriatal methylmalonic acid administration induces convulsions and TBARS production, and alters Na+,K+-ATPase activity in the rat striatum and cerebral cortex","volume":"44","author":"Maneck Malfatti","year":"2003","journal-title":"Epilepsia"},{"key":"10.1016\/j.abb.2020.108646_bib190","doi-asserted-by":"crossref","first-page":"2331","DOI":"10.1097\/00001756-200007140-00052","article-title":"Methylmalonate administration decreases Na+, K+ -ATPase activity in cerebral cortex of rats","volume":"11","author":"Wyse","year":"2000","journal-title":"Neuroreport"},{"key":"10.1016\/j.abb.2020.108646_bib191","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1002\/jnr.23020","article-title":"Methylmalonate impairs mitochondrial respiration supported by NADH-linked substrates: involvement of mitochondrial glutamate metabolism","volume":"90","author":"Melo","year":"2012","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib192","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1007\/s10545-007-0798-1","article-title":"Methylmalonate inhibits succinate-supported oxygen consumption by interfering with mitochondrial succinate uptake","volume":"31","author":"Mirandola","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib193","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1111\/j.1471-4159.2004.02565.x","article-title":"Mitochondrial permeability transition in neuronal damage promoted by Ca2+ and respiratory chain complex II inhibition","volume":"90","author":"Maciel","year":"2004","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib194","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/j.neuint.2004.03.006","article-title":"Inhibition of mitochondrial creatine kinase activity from rat cerebral cortex by methylmalonic acid","volume":"45","author":"Schuck","year":"2004","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.abb.2020.108646_bib195","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.freeradbiomed.2009.05.004","article-title":"Mitochondria and reactive oxygen species","volume":"47","author":"Kowaltowski","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2020.108646_bib196","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1097\/00001756-200002280-00023","article-title":"Propionic and L-methylmalonic acids induce oxidative stress in brain of young rats","volume":"11","author":"Fontella","year":"2000","journal-title":"Neuroreport"},{"key":"10.1016\/j.abb.2020.108646_bib197","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1007\/s10571-011-9675-4","article-title":"Experimental evidence that methylmalonic acid provokes oxidative damage and compromises antioxidant defenses in nerve terminal and striatum of young rats","volume":"31","author":"Fernandes","year":"2011","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib198","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.neulet.2004.11.038","article-title":"Involvement of NO in the convulsive behavior and oxidative damage induced by the intrastriatal injection of methylmalonate","volume":"376","author":"Royes","year":"2005","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.abb.2020.108646_bib199","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.pbb.2005.12.017","article-title":"Effectiveness of creatine monohydrate on seizures and oxidative damage induced by methylmalonate","volume":"83","author":"Royes","year":"2006","journal-title":"Pharmacol. Biochem. Behav."},{"key":"10.1016\/j.abb.2020.108646_bib200","doi-asserted-by":"crossref","first-page":"233","DOI":"10.3109\/10715762.2012.762771","article-title":"Acute renal failure potentiates methylmalonate-induced oxidative stress in brain and kidney of rats","volume":"47","author":"Schuck","year":"2013","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.abb.2020.108646_bib201","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/s11010-014-1996-4","article-title":"Methylmalonic acid administration induces DNA damage in rat brain and kidney","volume":"391","author":"Andrade","year":"2014","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.abb.2020.108646_bib202","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1093\/jnen\/nlw121","article-title":"Methylmalonate induces inflammatory and apoptotic potential: a link to glial activation and neurological dysfunction","volume":"76","author":"Gabbi","year":"2017","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.abb.2020.108646_bib203","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1097\/00001756-199806010-00009","article-title":"Inhibition of NA+,K+-ATPase from rat brain cortex by propionic acid","volume":"9","author":"Wyse","year":"1998","journal-title":"Neuroreport"},{"key":"10.1016\/j.abb.2020.108646_bib204","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/S0091-3057(02)00856-0","article-title":"Ascorbic acid prevents cognitive deficits caused by chronic administration of propionic acid to rats in the water maze","volume":"73","author":"Pettenuzzo","year":"2002","journal-title":"Pharmacol. Biochem. Behav."},{"key":"10.1016\/j.abb.2020.108646_bib205","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.neulet.2006.08.075","article-title":"Propionic acid induces convulsions and protein carbonylation in rats","volume":"408","author":"Rigo","year":"2006","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.abb.2020.108646_bib206","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/j.neuroscience.2015.09.043","article-title":"The effect of WIN 55,212-2 suggests a cannabinoid-sensitive component in the early toxicity induced by organic acids accumulating in glutaric acidemia type I and in related disorders of propionate metabolism in rat brain synaptosomes","volume":"310","author":"Col\u00edn-Gonz\u00e1lez","year":"2015","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib207","doi-asserted-by":"crossref","first-page":"3227","DOI":"10.1111\/j.1432-1033.2004.04255.x","article-title":"On the mechanism of action of the antifungal agent propionate. Propionyl-CoA inhibits glucose metabolism in Aspergillus nidulans","volume":"271","author":"Brock","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.abb.2020.108646_bib208","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1111\/jnc.13544","article-title":"2-Methylcitric acid impairs glutamate metabolism and induces permeability transition in brain mitochondria","volume":"137","author":"Amaral","year":"2016","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2020.108646_bib209","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1007\/s10545-005-0501-3","article-title":"Inhibition of energy metabolism by 2-methylacetoacetate and 2-methyl-3-hydroxybutyrate in cerebral cortex of developing rats","volume":"28","author":"Rosa","year":"2005","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib210","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/s11011-010-9204-z","article-title":"Evidence that 2-methylacetoacetate induces oxidative stress in rat brain","volume":"25","author":"Leipnitz","year":"2010","journal-title":"Metab. Brain Dis."},{"key":"10.1016\/j.abb.2020.108646_bib211","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijdevneu.2010.10.007","article-title":"Neurochemical evidence that 3-methylglutaric acid inhibits synaptic Na+,K+-ATPase activity probably through oxidative damage in brain cortex of young rats","volume":"29","author":"Ribeiro","year":"2011","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib212","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1007\/s12035-015-9289-9","article-title":"Induction of a proinflammatory response in cortical astrocytes by the major metabolites accumulating in HMG-CoA lyase deficiency: the role of ERK signaling pathway in cytokine release","volume":"53","author":"Fernandes","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib213","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1007\/s11064-016-1973-2","article-title":"Experimental evidence that 3-methylglutaric acid disturbs mitochondrial function and induced oxidative stress in rat brain synaptosomes: new converging mechanisms","volume":"41","author":"Col\u00edn-Gonz\u00e1lez","year":"2016","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.abb.2020.108646_bib214","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1007\/s12640-019-00122-x","article-title":"3-Hydroxy-3-Methylglutaric acid impairs redox and energy homeostasis, mitochondrial dynamics, and endoplasmic reticulum\u2013mitochondria crosstalk in rat brain","volume":"37","author":"da Rosa","year":"2020","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.abb.2020.108646_bib215","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1007\/s12640-019-00019-9","article-title":"Bezafibrate in vivo administration prevents 3-methylglutaric acid-induced impairment of redox status, mitochondrial biogenesis, and neural injury in brain of developing rats","volume":"35","author":"da Rosa-Junior","year":"2019","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.abb.2020.108646_bib216","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1002\/jnr.21527","article-title":"Evidence that 3-hydroxy-3-methylglutaric acid promotes lipid and protein oxidative damage and reduces the nonenzymatic antioxidant defenses in rat cerebral cortex","volume":"86","author":"Leipnitz","year":"2008","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib217","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1016\/j.lfs.2007.12.024","article-title":"Induction of oxidative stress by the metabolites accumulating in 3-methylglutaconic aciduria in cerebral cortex of young rats","volume":"82","author":"Leipnitz","year":"2008","journal-title":"Life Sci."},{"key":"10.1016\/j.abb.2020.108646_bib218","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.ijdevneu.2009.03.001","article-title":"Striatum is more vulnerable to oxidative damage induced by the metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency as compared to liver","volume":"27","author":"Leipnitz","year":"2009","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib219","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1007\/s11011-015-9675-z","article-title":"Evidence that 3-hydroxy-3-methylglutaric and 3-methylglutaric acids induce DNA damage in rat striatum","volume":"30","author":"da Rosa","year":"2015","journal-title":"Metab. Brain Dis."},{"key":"10.1016\/j.abb.2020.108646_bib220","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.3109\/10715762.2013.853876","article-title":"Redox homeostasis is compromised in vivo by the metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency in rat cerebral cortex and liver","volume":"47","author":"Da Rosa","year":"2013","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.abb.2020.108646_bib221","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.ymgme.2013.03.017","article-title":"In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this disorder","volume":"109","author":"Fernandes","year":"2013","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib222","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/BF02679979","article-title":"Inhibition of energy production in vitro by glutaric acid in cerebral cortex of young rats","volume":"15","author":"Silva","year":"2000","journal-title":"Metab. Brain Dis."},{"key":"10.1016\/j.abb.2020.108646_bib223","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/j.ijdevneu.2005.08.003","article-title":"Glutaric acid moderately compromises energy metabolism in rat brain","volume":"23","author":"da","year":"2005","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib224","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1007\/s11064-005-7711-9","article-title":"Glutaric acid administration impairs energy metabolism in midbrain and skeletal muscle of young rats","volume":"30","author":"Ferreira Gda","year":"2005","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.abb.2020.108646_bib225","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.nbd.2008.09.011","article-title":"Astrocytic proliferation and mitochondrial dysfunction induced by accumulated glutaric acidemia I (GAI) metabolites: possible implications for GAI pathogenesis","volume":"32","author":"Olivera","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib226","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0006-8993(02)04118-5","article-title":"Glutaric acid induces oxidative stress in brain of young rats","volume":"964","author":"de Oliveira Marques","year":"2003","journal-title":"Brain Res."},{"key":"10.1016\/j.abb.2020.108646_bib227","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.nbd.2006.01.002","article-title":"GM1 ganglioside prevents seizures, Na+,K+-ATPase activity inhibition and oxidative stress induced by glutaric acid and pentylenetetrazole","volume":"22","author":"Fighera","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib228","doi-asserted-by":"crossref","first-page":"5362","DOI":"10.1007\/s12035-017-0761-6","article-title":"Toxic synergism between quinolinic acid and glutaric acid in neuronal cells is mediated by oxidative stress: insights to a new toxic model","volume":"55","author":"Pierozan","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib229","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s11011-010-9203-0","article-title":"Induction of S100B secretion in C6 astroglial cells by the major metabolites accumulating in glutaric acidemia type I","volume":"25","author":"Quincozes-Santos","year":"2010","journal-title":"Metab. Brain Dis"},{"key":"10.1016\/j.abb.2020.108646_bib230","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1002\/jnr.23070","article-title":"m-trifluoromethyl diphenyl diselenide attenuates glutaric acid-induced seizures and oxidative stress in rat pups: involvement of the \u03b3-aminobutyric acidergic system","volume":"90","author":"Magni","year":"2012","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib231","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1007\/s10571-006-9134-9","article-title":"Induction of oxidative stress by chronic and acute glutaric acid administration to rats","volume":"27","author":"Latini","year":"2007","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1016\/j.abb.2020.108646_bib232","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0078332","article-title":"N-acetylcysteine prevents spatial memory impairment induced by chronic early postnatal glutaric acid and lipopolysaccharide in rat pups","volume":"8","author":"Rodrigues","year":"2013","journal-title":"PloS One"},{"key":"10.1016\/j.abb.2020.108646_bib233","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/S0006-8993(02)03573-4","article-title":"3-Hydroxyglutaric acid induces oxidative stress and decreases the antioxidant defenses in cerebral cortex of young rats","volume":"956","author":"Latini","year":"2002","journal-title":"Brain Res."},{"key":"10.1016\/j.abb.2020.108646_bib234","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.neuroscience.2005.05.013","article-title":"3-Hydroxyglutaric acid moderately impairs energy metabolism in brain of young rats","volume":"135","author":"Latini","year":"2005","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib235","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/s10545-005-3677-7","article-title":"Promotion of oxidative stress by 3-hydroxyglutaric acid in rat striatum","volume":"28","author":"Latini","year":"2005","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.abb.2020.108646_bib236","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/S0736-5748(03)00035-2","article-title":"L-2-Hydroxyglutaric acid inhibits mitochondrial creatine kinase activity from cerebellum of developing rats","volume":"21","author":"Da Silva","year":"2003","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib237","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1023\/A:1024936129908","article-title":"Inhibition of mitochondrial creatine kinase activity by D-2-hydroxyglutaric acid in cerebellum of young rats","volume":"28","author":"Da Silva","year":"2003","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.abb.2020.108646_bib238","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0197-0186(03)00098-6","article-title":"Inhibition of creatine kinase activity from rat cerebral cortex by D-2-hydroxyglutaric acid in vitro","volume":"44","author":"da Silva","year":"2004","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.abb.2020.108646_bib239","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0925-4439(01)00088-6","article-title":"Inhibition of cytochrome c oxidase activity in rat cerebral cortex and human skeletal muscle by D-2-hydroxyglutaric acid in vitro","volume":"1586","author":"da Silva","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2020.108646_bib240","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.ymgme.2005.05.002","article-title":"Mitochondrial energy metabolism is markedly impaired by D-2-hydroxyglutaric acid in rat tissues","volume":"86","author":"Latini","year":"2005","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.abb.2020.108646_bib241","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1046\/j.1460-9568.2003.02639.x","article-title":"D-2-hydroxyglutaric acid induces oxidative stress in cerebral cortex of young rats","volume":"17","author":"Latini","year":"2003","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.abb.2020.108646_bib242","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1002\/jnr.10735","article-title":"Induction of oxidative stress by L-2-hydroxyglutaric acid in rat brain","volume":"74","author":"Latini","year":"2003","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.abb.2020.108646_bib243","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.neuroscience.2014.07.011","article-title":"Disruption of redox homeostasis and histopathological alterations caused by in vivo intrastriatal administration of D-2-hydroxyglutaric acid to young rats","volume":"277","author":"da Rosa","year":"2014","journal-title":"Neuroscience"},{"key":"10.1016\/j.abb.2020.108646_bib244","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.freeradbiomed.2015.02.008","article-title":"In vivo intracerebral administration of L-2-hydroxyglutaric acid provokes oxidative stress and histopathological alterations in striatum and cerebellum of adolescent rats","volume":"83","author":"Da Rosa","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.abb.2020.108646_bib245","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1007\/s12640-018-9874-6","article-title":"Experimental evidence that in vivo intracerebral administration of L-2-hydroxyglutaric acid to neonatal rats provokes disruption of redox status and histopathological abnormalities in the brain","volume":"33","author":"Ribeiro","year":"2018","journal-title":"Neurotox. Res."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000398612030655X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000398612030655X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,12,3]],"date-time":"2024-12-03T13:48:25Z","timestamp":1733233705000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S000398612030655X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":245,"alternative-id":["S000398612030655X"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2020.108646","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disruption of mitochondrial functions and oxidative stress contribute to neurologic dysfunction in organic acidurias","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2020.108646","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"108646"}}