{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T20:38:08Z","timestamp":1789763888286,"version":"4.0.1"},"reference-count":144,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2017,2,10]],"date-time":"2017-02-10T00:00:00Z","timestamp":1486684800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The mitochondrial calcium uniporter (MCU)\u2014a calcium uniporter on the inner membrane of mitochondria\u2014controls the mitochondrial calcium uptake in normal and abnormal situations. Mitochondrial calcium is essential for the production of adenosine triphosphate (ATP); however, excessive calcium will induce mitochondrial dysfunction. Calcium homeostasis disruption and mitochondrial dysfunction is observed in many neurodegenerative disorders. However, the role and regulatory mechanism of the MCU in the development of these diseases are obscure. In this review, we summarize the role of the MCU in controlling oxidative stress-elevated mitochondrial calcium and its function in neurodegenerative disorders. Inhibition of the MCU signaling pathway might be a new target for the treatment of neurodegenerative disorders.<\/jats:p>","DOI":"10.3390\/ijms18020248","type":"journal-article","created":{"date-parts":[[2017,2,15]],"date-time":"2017-02-15T10:09:07Z","timestamp":1487153347000},"page":"248","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":77,"title":["The Function of the Mitochondrial Calcium Uniporter in Neurodegenerative Disorders"],"prefix":"10.3390","volume":"18","author":[{"given":"Yajin","family":"Liao","sequence":"first","affiliation":[{"name":"The Brain Science Center, Beijing Institute of Basic Medical Sciences, No. 27 Taiping Road, Haidian District, Beijing 100039, China"},{"name":"The State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuan","family":"Dong","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Qingdao University Medical College, Qingdao 266071, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinbo","family":"Cheng","sequence":"additional","affiliation":[{"name":"The State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,2,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/27094","article-title":"Calcium\u2014A life and death signal","volume":"395","author":"Berridge","year":"1998","journal-title":"Nature"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1042\/bss0670177","article-title":"Dysfunctional intracellular calcium homoeostasis: A central cause of neurodegeneration in Alzheimer\u2019s disease","volume":"67","author":"Cowburn","year":"2001","journal-title":"Biochem. Soc. Symp."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/nrneurol.2010.31","article-title":"Parkinson disease: Calcium channel blockers and Parkinson disease","volume":"6","author":"Pfeiffer","year":"2010","journal-title":"Nat. Rev. Neurol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5780","DOI":"10.1074\/jbc.M704704200","article-title":"Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease","volume":"283","author":"Lim","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.nbd.2011.01.016","article-title":"Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: Mechanistic relationship and differential sensitivity to intervention","volume":"42","author":"Tradewell","year":"2011","journal-title":"Neurobiol. Dis."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1073\/pnas.47.11.1744","article-title":"Calcium uptake by rat kidney mitochondria","volume":"47","author":"Deluca","year":"1961","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","first-page":"95","article-title":"Strontium and Calcium Uptake by Rat Liver and Kidney Mitochondria. Hw-76000","volume":"86","author":"Mraz","year":"1963","journal-title":"US At. Energy Comm."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1016\/S0021-9258(18)81146-2","article-title":"Calcium ion uptake by fragments of rat liver mitochondria and its dependence on electron transport","volume":"238","author":"Vasington","year":"1963","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0079-6123(08)63782-6","article-title":"Evidence that high frequency stimulation influences the phosphorylation of pyruvate dehydrogenase and that the activity of this enzyme is linked to mitochondrial calcium sequestration","volume":"56","author":"Browning","year":"1982","journal-title":"Prog. Brain Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1104\/pp.88.4.1031","article-title":"Regulation of the phosphorylation of mitochondrial pyruvate dehydrogenase complex in situ: Effects of respiratory substrates and calcium","volume":"88","author":"Budde","year":"1988","journal-title":"Plant Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0166-6851(96)02705-3","article-title":"Characterization of the \u03b1-ketoglutarate dehydrogenase complex from Fasciola hepatica: Potential implications for the role of calcium in the regulation of helminth mitochondrial metabolism","volume":"81","author":"Diaz","year":"1996","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1016\/j.bbabio.2009.01.005","article-title":"Regulation of mitochondrial dehydrogenases by calcium ions","volume":"1787","author":"Denton","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/BF01076578","article-title":"Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions","volume":"149\u2013150","author":"Nichols","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1042\/BJ20081981","article-title":"Mitochondrial calcium overload triggers complement-dependent superoxide-mediated programmed cell death in Trypanosoma cruzi","volume":"418","author":"Irigoin","year":"2009","journal-title":"Biochem. J."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/nature02246","article-title":"The mitochondrial calcium uniporter is a highly selective ion channel","volume":"427","author":"Kirichok","year":"2004","journal-title":"Nature"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1042\/bj1400143","article-title":"The inhibition of mitochondrial calcium transport by lanthanides and ruthenium red","volume":"140","author":"Reed","year":"1974","journal-title":"Biochem. J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/0014-5793(77)80947-2","article-title":"The inhibition of calcium uptake and release by rat liver mitochondria by ruthenium red","volume":"81","author":"Luthra","year":"1977","journal-title":"FEBS Lett."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10230","article-title":"A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter","volume":"476","author":"Raffaello","year":"2011","journal-title":"Nature"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/nature10234","article-title":"Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter","volume":"476","author":"Baughman","year":"2011","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/nature09358","article-title":"MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake","volume":"467","author":"Perocchi","year":"2010","journal-title":"Nature"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Plovanich, M., Bogorad, R.L., Sancak, Y., Kamer, K.J., Strittmatter, L., Li, A.A., Girgis, H.S., Kuchimanchi, S., de Groot, J., and Speciner, L. (2013). MICU2, a Paralog of MICU1, Resides within the Mitochondrial Uniporter Complex to Regulate Calcium Handling. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055785"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1038\/emboj.2013.157","article-title":"The mitochondrial calcium uniporter is a multimer that can include a dominant-negative pore-forming subunit","volume":"32","author":"Raffaello","year":"2013","journal-title":"EMBO J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1038\/ncb2622","article-title":"MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism","volume":"14","author":"Mallilankaraman","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1126\/science.1242993","article-title":"EMRE Is an Essential Component of the Mitochondrial Calcium Uniporter Complex","volume":"342","author":"Sancak","year":"2013","journal-title":"Science"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/nature17656","article-title":"Architecture of the mitochondrial calcium uniporter","volume":"533","author":"Oxenoid","year":"2016","journal-title":"Nature"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1038\/ncb2868","article-title":"The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter","volume":"15","author":"Pan","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.bbrc.2014.04.144","article-title":"Unresolved questions from the analysis of mice lacking MCU expression","volume":"449","author":"Murphy","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"3381","DOI":"10.1093\/nar\/gkg520","article-title":"SWISS-MODEL: An automated protein homology-modeling server","volume":"31","author":"Schwede","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1016\/j.celrep.2013.11.026","article-title":"MICU1 Motifs Define Mitochondrial Calcium Uniporter Binding and Activity","volume":"5","author":"Hoffman","year":"2013","journal-title":"Cell Rep."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1002\/embj.201386523","article-title":"Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake","volume":"33","author":"Wang","year":"2014","journal-title":"EMBO J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1016\/j.cmet.2013.04.020","article-title":"MICU1 controls both the threshold and cooperative activation of the mitochondrial Ca2+ uniporter","volume":"17","author":"Csordas","year":"2013","journal-title":"Cell Metab."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1016\/j.celrep.2016.07.011","article-title":"MICU1 Serves as a Molecular Gatekeeper to Prevent In Vivo Mitochondrial Calcium Overload","volume":"16","author":"Liu","year":"2016","journal-title":"Cell Rep."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/ng.2851","article-title":"Loss-of-function mutations in MICU1 cause a brain and muscle disorder linked to primary alterations in mitochondrial calcium signaling","volume":"46","author":"Logan","year":"2014","journal-title":"Nat. Genet."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.molcel.2016.08.020","article-title":"The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria","volume":"64","author":"Konig","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.bbabio.2016.03.019","article-title":"Analysis of the structure and function of EMRE in a yeast expression system","volume":"1857","author":"Yamamoto","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1016\/j.celrep.2016.04.050","article-title":"MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics","volume":"15","author":"Tomar","year":"2016","journal-title":"Cell Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.cmet.2014.12.004","article-title":"CCDC90A (MCUR1) Is a Cytochrome c Oxidase Assembly Factor and Not a Regulator of the Mitochondrial Calcium Uniporter","volume":"21","author":"Paupe","year":"2015","journal-title":"Cell Metab."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1038\/nrm4039","article-title":"The molecular era of the mitochondrial calcium uniporter","volume":"16","author":"Kamer","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2282","DOI":"10.1046\/j.1471-4159.1996.67062282.x","article-title":"Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells","volume":"67","author":"Budd","year":"1996","journal-title":"J. Neurochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1097\/00005072-199708000-00008","article-title":"Glutamate transporter alterations in Alzheimer disease are possibly associated with abnormal APP expression","volume":"56","author":"Li","year":"1997","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1503\/jpn.110190","article-title":"Glutamate system, amyloid \u03b2 peptides and tau protein: Functional interrelationships and relevance to Alzheimer disease pathology","volume":"38","author":"Revett","year":"2013","journal-title":"J. Psychiatry Neurosci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.expneurol.2009.09.027","article-title":"Glutamate, excitotoxicity, and programmed cell death in Parkinson disease","volume":"220","author":"Caudle","year":"2009","journal-title":"Exp. Neurol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0074-7742(06)81005-6","article-title":"An in vitro model of stroke-induced epilepsy: Elucidation of the roles of glutamate and calcium in the induction and maintenance of stroke-induced epileptogenesis","volume":"81","author":"DeLorenzo","year":"2007","journal-title":"Int. Rev. Neurobiol."},{"key":"ref_44","first-page":"203","article-title":"Glutamate receptor antagonism: Neurotoxicity, anti-akinetic effects, and psychosis","volume":"34","author":"Riederer","year":"1991","journal-title":"J. Neural Transm. Suppl."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S1353-8020(99)00038-3","article-title":"Reactive oxygen species in NMDA receptor-mediated glutamate neurotoxicity","volume":"5","author":"Akaike","year":"1999","journal-title":"Park. Relat. Disord."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1523\/JNEUROSCI.21-07-02224.2001","article-title":"The influence of glutamate receptor 2 expression on excitotoxicity in Glur2 null mutant mice","volume":"21","author":"Iihara","year":"2001","journal-title":"J. Neurosci."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"10277","DOI":"10.1523\/JNEUROSCI.18-24-10277.1998","article-title":"Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells","volume":"18","author":"Castilho","year":"1998","journal-title":"J. Neurosci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S0306-4522(02)00002-7","article-title":"Group I metabotropic glutamate receptor inhibition selectively blocks a prolonged Ca2+ elevation associated with age-dependent excitotoxicity","volume":"112","author":"Attucci","year":"2002","journal-title":"Neuroscience"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1111\/j.1469-7793.1999.0451m.x","article-title":"Glutamate-induced mitochondrial depolarisation and perturbation of calcium homeostasis in cultured rat hippocampal neurones","volume":"519","author":"Vergun","year":"1999","journal-title":"J. Physiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1089\/neu.2008.0532","article-title":"Calcium-permeable AMPA receptors appear in cortical neurons after traumatic mechanical injury and contribute to neuronal fate","volume":"25","author":"Spaethling","year":"2008","journal-title":"J. Neurotrauma"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1007\/BF00972471","article-title":"Regulation of N-methyl-d-aspartate receptor-mediated calcium transport and norepinephrine release in rat hippocampus synaptosomes by polyamines","volume":"19","author":"Siddiqui","year":"1994","journal-title":"Neurochem. Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"3019","DOI":"10.1113\/jphysiol.2012.232942","article-title":"Functional coupling of the metabotropic glutamate receptor, InsP3 receptor and L-type Ca2+ channel in mouse CA1 pyramidal cells","volume":"590","author":"Kato","year":"2012","journal-title":"J. Physiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2509","DOI":"10.1113\/jphysiol.2012.248526","article-title":"Calcium dynamics during NMDA-induced membrane potential oscillations in lamprey spinal neurons\u2014Contribution of L-type calcium channels (Cav1.3)","volume":"591","author":"Wang","year":"2013","journal-title":"J. Physiol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/j.mehy.2005.03.032","article-title":"Calcium-mediated aponecrosis plays a central role in the pathogenesis of estrogenic chemical-induced neurotoxicity","volume":"65","author":"Pretorius","year":"2005","journal-title":"Med. Hypotheses"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"7208","DOI":"10.1523\/JNEUROSCI.20-19-07208.2000","article-title":"Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells","volume":"20","author":"Ward","year":"2000","journal-title":"J. Neurosci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1002\/jnr.21218","article-title":"Simultaneous age-related depolarization of mitochondrial membrane potential and increased mitochondrial reactive oxygen species production correlate with age-related glutamate excitotoxicity in rat hippocampal neurons","volume":"85","author":"Parihar","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.bbabio.2008.04.017","article-title":"Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity","volume":"1777","author":"Abramov","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Qiu, J., Tan, Y.W., Hagenston, A.M., Martel, M.A., Kneisel, N., Skehel, P.A., Wyllie, D.J.A., Bading, H., and Hardingham, G.E. (2013). Mitochondrial calcium uniporter Mcu controls excitotoxicity and is transcriptionally repressed by neuroprotective nuclear calcium signals. Nat. Commun.","DOI":"10.1038\/ncomms3034"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1866","DOI":"10.1111\/j.1471-4159.2008.05541.x","article-title":"Neuromelanin can protect against iron-mediated oxidative damage in system modeling iron overload of brain aging and Parkinson\u2019s disease","volume":"106","author":"Zecca","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1007\/s10534-012-9544-8","article-title":"Iron and ER stress in neurodegenerative disease","volume":"25","author":"Liu","year":"2012","journal-title":"Biometals"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0361-9230(01)00510-X","article-title":"Iron and neurodegenerative disorders","volume":"55","author":"Thompson","year":"2001","journal-title":"Brain Res. Bull."},{"key":"ref_62","first-page":"743","article-title":"Iron involvement in neural damage and microgliosis in models of neurodegenerative diseases","volume":"46","author":"Shoham","year":"2000","journal-title":"Cell. Mol. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1586\/ern.12.128","article-title":"Brain iron accumulation in aging and neurodegenerative disorders","volume":"12","author":"Hagemeier","year":"2012","journal-title":"Expert Rev. Neurother."},{"key":"ref_64","first-page":"1161","article-title":"[Iron accumulation and neurodegenerative diseases]","volume":"74","author":"Yoshida","year":"2016","journal-title":"Nihon Rinsho. Jpn. J. Clin. Med."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"38","DOI":"10.3389\/fphar.2014.00038","article-title":"The interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders","volume":"5","author":"Urrutia","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"33380","DOI":"10.1074\/jbc.M111.268409","article-title":"Enhanced autophagy from chronic toxicity of iron and mutant A53T \u03b1-synuclein: Implications for neuronal cell death in Parkinson disease","volume":"286","author":"Chew","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.jtemb.2014.11.009","article-title":"Age-related changes of brain iron load changes in the frontal cortex in APPswe\/PS1\u0394E9 transgenic mouse model of Alzheimer\u2019s disease","volume":"30","author":"Dong","year":"2015","journal-title":"J. Trace Elem. Med. Biol. Organ Soc. Miner. Trace Elem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1128\/MCB.01685-08","article-title":"Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2","volume":"29","author":"Paradkar","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Garringer, H.J., Irimia, J.M., Li, W., Goodwin, C.B., Richine, B., Acton, A., Chan, R.J., Peacock, M., Muhoberac, B.B., and Ghetti, B. (2016). Effect of Systemic Iron Overload and a Chelation Therapy in a Mouse Model of the Neurodegenerative Disease Hereditary Ferritinopathy. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0161341"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/0006-8993(93)90341-J","article-title":"Iron induced oxidative stress and mitochondrial dysfunction: Relevance to Parkinson\u2019s disease","volume":"627","author":"Harley","year":"1993","journal-title":"Brain Res."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.bbadis.2003.12.013","article-title":"Iron uncouples oxidative phosphorylation in brain mitochondria isolated from vitamin E-deficient rats","volume":"1688","author":"Vatassery","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/j.bbrc.2014.12.073","article-title":"Blockage of mitochondrial calcium uniporter prevents iron accumulation in a model of experimental subarachnoid hemorrhage","volume":"456","author":"Yan","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1111\/apha.12162","article-title":"Blockade of mitochondrial calcium uniporter prevents cardiac mitochondrial dysfunction caused by iron overload","volume":"210","author":"Sripetchwandee","year":"2014","journal-title":"Acta Physiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.lfs.2013.01.004","article-title":"Mitochondrial calcium uniporter blocker effectively prevents brain mitochondrial dysfunction caused by iron overload","volume":"92","author":"Sripetchwandee","year":"2013","journal-title":"Life Sci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1007\/s10863-009-9250-6","article-title":"Brain mitochondrial dysfunction and oxidative damage in Parkinson\u2019s disease","volume":"41","author":"Navarro","year":"2009","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1007\/s11064-007-9482-y","article-title":"Mitochondrial dysfunction and oxidative stress in Parkinson\u2019s disease","volume":"33","author":"Onyango","year":"2008","journal-title":"Neurochem. Res."},{"key":"ref_77","first-page":"14a","article-title":"Secretases, oxidative stress, and perturbed calcium homeostasis in AD and stroke","volume":"132","author":"Mattson","year":"2008","journal-title":"J. Gen. Physiol."},{"key":"ref_78","first-page":"G1489","article-title":"Effect of oxidative stress on cellular functions and cytosolic free calcium of rat pancreatic acinar cells","volume":"272","author":"Schreiber","year":"1997","journal-title":"Am. J. Physiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1111\/j.1471-4159.2004.02964.x","article-title":"Alteration of cytosolic free calcium homeostasis by SIN-1: High sensitivity of L-type Ca2+ channels to extracellular oxidative\/nitrosative stress in cerebellar granule cells","volume":"92","author":"Henao","year":"2005","journal-title":"J. Neurochem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1159\/000321335","article-title":"Serum Calcium Levels and Long-Term Mortality in Patients with Acute Stroke","volume":"31","author":"Appel","year":"2011","journal-title":"Cerebrovasc. Dis."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1007\/s13238-015-0144-6","article-title":"Mitochondrial calcium uniporter protein MCU is involved in oxidative stress-induced cell death","volume":"6","author":"Liao","year":"2015","journal-title":"Protein Cell"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"5420","DOI":"10.3390\/ijms16035420","article-title":"MiR-25 protects cardiomyocytes against oxidative damage by targeting the mitochondrial calcium uniporter","volume":"16","author":"Pan","year":"2015","journal-title":"Int. J. Mol. Sci."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.neulet.2016.06.012","article-title":"Inhibition of mitochondrial calcium uniporter protects neurocytes from ischemia\/reperfusion injury via the inhibition of excessive mitophagy","volume":"628","author":"Yu","year":"2016","journal-title":"Neurosci. Lett."},{"key":"ref_84","first-page":"1720","article-title":"Effects of the mitochondrial calcium uniporter on cerebral edema in a rat model of cerebral ischemia reperfusion injury","volume":"6","author":"Li","year":"2011","journal-title":"Neural Regen. Res."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1111\/j.1460-9568.2011.07760.x","article-title":"Mitochondrial calcium and its regulation in neurodegeneration induced by oxidative stress","volume":"34","author":"Barsukova","year":"2011","journal-title":"Eur. J. Neurosci."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1097\/YCO.0000000000000140","article-title":"Inflammation and neurodegenerative disorders: Is there still hope for therapeutic intervention?","volume":"28","author":"Baune","year":"2015","journal-title":"Curr. Opin. Psychiatry"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"30","DOI":"10.2174\/1874609810801010030","article-title":"Inflammation in neurodegenerative disorders: Friend or foe?","volume":"1","author":"Galimberti","year":"2008","journal-title":"Curr. Aging Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1111\/j.1471-4159.2009.05886.x","article-title":"Inflammation mediates varying effects in neurogenesis: Relevance to the pathogenesis of brain injury and neurodegenerative disorders","volume":"108","author":"Whitney","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1006\/brbi.1997.0496","article-title":"Inflammatory events at the blood brain barrier: Regulation of adhesion molecules, cytokines, and chemokines by reactive nitrogen and oxygen species","volume":"11","author":"Merrill","year":"1997","journal-title":"Brain Behav. Immun."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.exer.2007.06.013","article-title":"Pro-inflammatory cytokines increase reactive oxygen species through mitochondria and NADPH oxidase in cultured RPE cells","volume":"85","author":"Yang","year":"2007","journal-title":"Exp. Eye Res."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.freeradbiomed.2009.06.013","article-title":"In vivo imaging of reactive oxygen and nitrogen species in inflammation using the luminescent probe L-012","volume":"47","author":"Kielland","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/jpi.12337","article-title":"Melatonin attenuates traumatic brain injury-induced inflammation: A possible role for mitophagy","volume":"61","author":"Lin","year":"2016","journal-title":"J. Pineal Res."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Huang, S.H., Lien, J.C., Chen, C.J., Liu, Y.C., Wang, C.Y., Ping, C.F., Lin, Y.F., Huang, A.C., and Lin, C.W. (2016). Antiviral Activity of a Novel Compound CW-33 against Japanese Encephalitis Virus through Inhibiting Intracellular Calcium Overload. Int. J. Mol. Sci.","DOI":"10.3390\/ijms17091386"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1002\/jnr.21566","article-title":"Sulfated polymannuroguluronate, a novel anti-acquired immune deficiency syndrome drug candidate, decreased vulnerability of PC12 cells to human immunodeficiency virus tat protein through attenuating calcium overload","volume":"86","author":"Hui","year":"2008","journal-title":"J. Neurosci. Res."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1105\/tpc.10.4.585","article-title":"Role of calcium in signal transduction during the hypersensitive response caused by basidiospore-derived infection of the cowpea rust fungus","volume":"10","author":"Xu","year":"1998","journal-title":"Plant Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1002\/ijc.2910440433","article-title":"In vitro infection of cell lines with HTLV-I and SIVmac results in altered intracellular free calcium concentration and increased membrane polarization","volume":"44","author":"Wright","year":"1989","journal-title":"Int. J. Cancer"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"6201","DOI":"10.1038\/ncomms7201","article-title":"Mitochondrial Ca2+-dependent NLRP3 activation exacerbates the Pseudomonas aeruginosa-driven inflammatory response in cystic fibrosis","volume":"6","author":"Rimessi","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Cheng, J.B., Liao, Y.J., Zhou, L.J., Peng, S.Y., Chen, H., and Yuan, Z.Q. (2016). Amplified RLR signaling activation through an interferon-stimulated gene-endoplasmic reticulum stress-mitochondrial calcium uniporter protein loop. Sci. Rep., 6.","DOI":"10.1038\/srep20158"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/s13760-013-0220-8","article-title":"Intermittent hypoxia protects cerebral mitochondrial function from calcium overload","volume":"113","author":"Chen","year":"2013","journal-title":"Acta Neurol. Belg."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1161\/hh2201.100341","article-title":"Opening of mitochondrial K(ATP) channels attenuates the ouabain-induced calcium overload in mitochondria","volume":"89","author":"Ishida","year":"2001","journal-title":"Circ. Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/S0361-9230(00)00370-1","article-title":"Molecular mechanism of neurodegeneration induced by Alzheimer\u2019s \u03b2-amyloid protein: Channel formation and disruption of calcium homeostasis","volume":"53","author":"Kawahara","year":"2000","journal-title":"Brain Res. Bull."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1111\/j.1471-4159.2009.05932.x","article-title":"Mutant Pink1 induces mitochondrial dysfunction in a neuronal cell model of Parkinson\u2019s disease by disturbing calcium flux","volume":"108","author":"Marongiu","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"3070","DOI":"10.1074\/jbc.M112.407726","article-title":"Dysregulation of mitochondrial calcium signaling and superoxide flashes cause mitochondrial genomic DNA damage in Huntington disease","volume":"288","author":"Wang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2865","DOI":"10.1093\/brain\/aws208","article-title":"The mitochondrial calcium regulator cyclophilin D is an essential component of oestrogen-mediated neuroprotection in amyotrophic lateral sclerosis","volume":"135","author":"Kim","year":"2012","journal-title":"Brain J. Neurol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1001\/jamaneurol.2016.2642","article-title":"Longitudinal \u03b2-Amyloid Deposition and Hippocampal Volume in Preclinical Alzheimer Disease and Suspected Non-Alzheimer Disease Pathophysiology","volume":"73","author":"Gordon","year":"2016","journal-title":"JAMA Neurol."},{"key":"ref_106","first-page":"843649","article-title":"Accumulation of exogenous amyloid-\u03b2 peptide in hippocampal mitochondria causes their dysfunction: A protective role for melatonin","volume":"2012","author":"Tan","year":"2012","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"13145","DOI":"10.1073\/pnas.0806192105","article-title":"The amyloid \u03b2-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae","volume":"105","author":"Alikhani","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1111\/j.1460-9568.2010.07248.x","article-title":"Interaction of a novel mitochondrial protein, 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1 (NIPSNAP1), with the amyloid precursor protein family","volume":"31","author":"Tummala","year":"2010","journal-title":"Eur. J. Neurosci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1159\/000323264","article-title":"Further evidence on mitochondrial targeting of \u03b2-amyloid and specificity of \u03b2-amyloid-induced mitotoxicity in neurons","volume":"8","author":"Tillement","year":"2011","journal-title":"Neuro-Degener. Dis."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"753","DOI":"10.3233\/JAD-2011-110686","article-title":"Aging promotes amyloid-\u03b2 peptide induced mitochondrial dysfunctions in rat brain: A molecular link between aging and Alzheimer\u2019s disease","volume":"27","author":"Sinha","year":"2011","journal-title":"J. Alzheimer\u2019s Dis. JAD"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Cha, M.Y., Han, S.H., Son, S.M., Hong, H.S., Choi, Y.J., Byun, J., and Mook-Jung, I. (2012). Mitochondria-specific accumulation of amyloid \u03b2 induces mitochondrial dysfunction leading to apoptotic cell death. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034929"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"30322","DOI":"10.1074\/jbc.274.42.30322","article-title":"Activation of the L voltage-sensitive calcium channel by mitogen-activated protein (MAP) kinase following exposure of neuronal cells to \u03b2-amyloid\u2014Map kinase mediates \u03b2-amyloid-induced neurodegeneration","volume":"274","author":"Ekinci","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_113","first-page":"61A","article-title":"\u03b2-Amyloid-induced calcium influx induces neurodegeneration in culture by oxidative stress rather than tau phosphorylation","volume":"10","author":"Ekinci","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2137","DOI":"10.1016\/S0006-3495(94)80717-9","article-title":"Theoretical models of the ion channel structure of amyloid \u03b2-protein","volume":"67","author":"Durell","year":"1994","journal-title":"Biophys. J."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1016\/j.bbamem.2007.04.021","article-title":"Amyloid \u03b2 ion channel: 3D structure and relevance to amyloid channel paradigm","volume":"1768","author":"Lal","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1529\/biophysj.107.110148","article-title":"Models of \u03b2-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process","volume":"93","author":"Jang","year":"2007","journal-title":"Biophys. J."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/j.arr.2010.05.003","article-title":"Modulation of mitochondrial calcium as a pharmacological target for Alzheimer\u2019s disease","volume":"9","author":"Hung","year":"2010","journal-title":"Ageing Res. Rev."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1111\/jnc.13731","article-title":"Mitochondrial dysfunction in Parkinson\u2019s disease","volume":"139","author":"Bose","year":"2016","journal-title":"J. Neurochem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1159\/000197890","article-title":"Significance of brain lesions in Parkinson disease dementia and Lewy body dementia","volume":"24","author":"Jellinger","year":"2009","journal-title":"Front. Neurol. Neurosci."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1007\/s00702-011-0596-7","article-title":"\u03b1-Synuclein increases U251 cells vulnerability to hydrogen peroxide by disrupting calcium homeostasis","volume":"118","author":"Ying","year":"2011","journal-title":"J. Neural Transm."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.1016\/j.neurobiolaging.2013.06.006","article-title":"Deregulation of calcium homeostasis mediates secreted \u03b1-synuclein-induced neurotoxicity","volume":"34","author":"Melachroinou","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Schmidt, F., Levin, J., Kamp, F., Kretzschmar, H., Giese, A., and Botzel, K. (2012). Single-channel electrophysiology reveals a distinct and uniform pore complex formed by \u03b1-synuclein oligomers in lipid membranes. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0042545"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1016\/j.neurobiolaging.2005.03.028","article-title":"Assessment of PINK1 (PARK6) polymorphisms in Finnish PD","volume":"27","author":"Clarimon","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1212\/WNL.62.12.2335-a","article-title":"Assessment of a DJ-1 (PARK7) polymorphism in Finnish PD","volume":"62","author":"Healy","year":"2004","journal-title":"Neurology"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1186\/s12974-016-0588-5","article-title":"Inflammatory profile in LRRK2-associated prodromal and clinical PD","volume":"13","author":"Brockmann","year":"2016","journal-title":"J. Neuroinflamm."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.conb.2007.04.010","article-title":"Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson\u2019s disease","volume":"17","author":"Dodson","year":"2007","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s00401-011-0902-3","article-title":"Parkin, PINK1 and mitochondrial integrity: Emerging concepts of mitochondrial dysfunction in Parkinson\u2019s disease","volume":"123","author":"Pilsl","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Liu, W., Vives-Bauza, C., Acin-Perez, R., Yamamoto, A., Tan, Y., Li, Y., Magrane, J., Stavarache, M.A., Shaffer, S., and Chang, S. (2009). PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and \u03b1-synuclein aggregation in cell culture models of Parkinson\u2019s disease. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0004597"},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Di Nottia, M., Masciullo, M., Verrigni, D., Petrillo, S., Modoni, A., Rizzo, V., Di Giuda, D., Rizza, T., Niceta, M., and Torraco, A. (2016). DJ-1 modulates mitochondrial response to oxidative stress: Clues from a novel diagnosis of PARK7. Clin. Genet.","DOI":"10.1111\/cge.12841"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1016\/j.bbagen.2014.02.015","article-title":"LRRK2, but not pathogenic mutants, protects against H2O2 stress depending on mitochondrial function and endocytosis in a yeast model","volume":"1840","author":"Pereira","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Soman, S., Keatinge, M., Moein, M., Da Costa, M., Mortiboys, H., Skupin, A., Sugunan, S., Bazala, M., Kuznicki, J., and Bandmann, O. (2016). Inhibition of the mitochondrial calcium uniporter rescues dopaminergic neurons in pink1\u2212\/\u2212 zebrafish. Eur. J. Neurosci.","DOI":"10.1111\/ejn.13473"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1002\/ana.21937","article-title":"L-type calcium channel blockers and Parkinson disease in Denmark","volume":"67","author":"Ritz","year":"2010","journal-title":"Ann. Neurol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/jcbfm.1994.104","article-title":"Calcium Accumulation Following Middle Cerebral-Artery Occlusion in Stroke-Prone Spontaneously Hypertensive Rats","volume":"14","author":"Shirotani","year":"1994","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1161\/01.STR.32.5.1234-a","article-title":"Glutamate, interleukin-6, and early clinical worsening in patients with acute stroke","volume":"32","author":"Vila","year":"2001","journal-title":"Stroke"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1053\/jscd.2000.18908","article-title":"Neurotransmitters and pathophysiology of stroke: Evidence for the release of glutamate and other transmitters\/mediators in animals and humans","volume":"9","author":"Davalos","year":"2000","journal-title":"J. Stroke Cerebrovasc. Dis."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/s10571-014-0107-0","article-title":"High plasma glutamate levels are associated with poor functional outcome in acute ischemic stroke","volume":"35","author":"Meng","year":"2015","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1007\/s11055-010-9292-6","article-title":"Use of the glutamate NMDA receptor antagonist PK-Merz in acute stroke","volume":"40","author":"Krivonos","year":"2010","journal-title":"Neurosci. Behav. Physiol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1161\/01.STR.26.4.602","article-title":"Safety and tolerability of the glutamate antagonist CGS 19755 (Selfotel) in patients with acute ischemic stroke. Results of a phase IIa randomized trial","volume":"26","author":"Grotta","year":"1995","journal-title":"Stroke"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2813","DOI":"10.1161\/01.STR.0000043823.37955.FB","article-title":"AMPA antagonist ZK200775 in patients with acute ischemic stroke: Possible glial cell toxicity detected by monitoring of S-100B serum levels","volume":"33","author":"Elting","year":"2002","journal-title":"Stroke"},{"key":"ref_140","first-page":"79","article-title":"A calcium antagonist, NB-818, improves blood flow distribution in the brain and other major organs of stroke-prone spontaneously hypertensive rats (SHRSP)","volume":"23","author":"Higashino","year":"1997","journal-title":"J. Brain Sci."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1111\/j.2042-7158.1997.tb06136.x","article-title":"Effects of the calcium antagonist AE0047 on the development of neurological deficit and infarction after middle cerebral artery occlusion in stroke-prone spontaneously hypertensive rats","volume":"49","author":"Shinyama","year":"1997","journal-title":"J. Pharm. Pharmacol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1007\/s00421-016-3392-0","article-title":"Impact of aortic root size on left ventricular afterload and stroke volume","volume":"116","author":"Sahlen","year":"2016","journal-title":"Eur. J. Appl. Physiol."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Zhang, J., Yang, J., Zhang, C.F., Jiang, X.Q., Zhou, H.Q., and Liu, M. (2012). Calcium antagonists for acute ischemic stroke. Cochrane Database Syst. Rev.","DOI":"10.1002\/14651858.CD001928.pub2"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/j.lfs.2005.05.076","article-title":"Involvement of the mitochondrial calcium uniporter in cardioprotection by ischemic preconditioning","volume":"78","author":"Zhang","year":"2006","journal-title":"Life Sci."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/18\/2\/248\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:27:57Z","timestamp":1760207277000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/18\/2\/248"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,2,10]]},"references-count":144,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2017,2]]}},"alternative-id":["ijms18020248"],"URL":"https:\/\/doi.org\/10.3390\/ijms18020248","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,2,10]]}}}