{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,3]],"date-time":"2026-11-03T16:31:17Z","timestamp":1793723477823,"version":"4.6.1"},"reference-count":211,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2022,4,20]],"date-time":"2022-04-20T00:00:00Z","timestamp":1650412800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"UNAM-PAPIIT","award":["IN218821"],"award-info":[{"award-number":["IN218821"]}]},{"name":"UNAM-PAPIIT","award":["IN203222"],"award-info":[{"award-number":["IN203222"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Calcium is used in many cellular processes and is maintained within the cell as free calcium at low concentrations (approximately 100 nM), compared with extracellular (millimolar) concentrations, to avoid adverse effects such as phosphate precipitation. For this reason, cells have adapted buffering strategies by compartmentalizing calcium into mitochondria and the endoplasmic reticulum (ER). In mitochondria, the calcium concentration is in the millimolar range, as it is in the ER. Mitochondria actively contribute to buffering cellular calcium, but if matrix calcium increases beyond physiological demands, it can promote the opening of the mitochondrial permeability transition pore (mPTP) and, consequently, trigger apoptotic or necrotic cell death. The pathophysiological implications of mPTP opening in ischemia-reperfusion, liver, muscle, and lysosomal storage diseases, as well as those affecting the central nervous system, for example, Parkinson\u2019s disease (PD), Alzheimer\u2019s disease (AD), Huntington\u2019s disease (HD), and amyotrophic lateral sclerosis (ALS) have been reported. In this review, we present an updated overview of the main cellular mechanisms of mitochondrial calcium regulation. We specially focus on neurodegenerative diseases related to imbalances in calcium homeostasis and summarize some proposed therapies studied to attenuate these diseases.<\/jats:p>","DOI":"10.3390\/antiox11050801","type":"journal-article","created":{"date-parts":[[2022,4,21]],"date-time":"2022-04-21T01:55:51Z","timestamp":1650506151000},"page":"801","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":268,"title":["Mitochondrial Calcium: Effects of Its Imbalance in Disease"],"prefix":"10.3390","volume":"11","author":[{"given":"Deyamira","family":"Matuz-Mares","sequence":"first","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 3000, Cd. Universitaria, Coyoac\u00e1n, Ciudad de M\u00e9xico 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8910-3035","authenticated-orcid":false,"given":"Martin","family":"Gonz\u00e1lez-Andrade","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 3000, Cd. Universitaria, Coyoac\u00e1n, Ciudad de M\u00e9xico 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minerva Georgina","family":"Araiza-Villanueva","sequence":"additional","affiliation":[{"name":"Institute of Microbiology, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda Magdalena","family":"Vilchis-Landeros","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 3000, Cd. Universitaria, Coyoac\u00e1n, Ciudad de M\u00e9xico 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8312-3115","authenticated-orcid":false,"given":"H\u00e9ctor","family":"V\u00e1zquez-Meza","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 3000, Cd. Universitaria, Coyoac\u00e1n, Ciudad de M\u00e9xico 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1111\/j.1365-2958.2004.04276.x","article-title":"Calcium signalling in bacteria","volume":"54","author":"Dominguez","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/j.molcel.2017.05.028","article-title":"Intracellular Ca2+ Sensing: Its Role in Calcium Homeostasis and Signaling","volume":"66","author":"Bagur","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Li, X., Fang, P., Mai, J., Choi, E.T., Wang, H., and Yang, X.F. (2013). Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers. J. Hematol. Oncol., 6.","DOI":"10.1186\/1756-8722-6-19"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1007\/s10545-015-9819-7","article-title":"Peroxisome-mitochondria interplay and disease","volume":"38","author":"Schrader","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.tem.2016.12.003","article-title":"Peroxisomal Dysfunction in Age-Related Diseases","volume":"28","author":"Cipolla","year":"2017","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.cell.2010.03.008","article-title":"SnapShot: Reactive Oxygen Intermediates (ROI)","volume":"140","author":"Nathan","year":"2010","journal-title":"Cell"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1159\/000485089","article-title":"Antioxidants Maintain Cellular Redox Homeostasis by Elimination of Reactive Oxygen Species","volume":"44","author":"He","year":"2017","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Osorio Alves, J., Matta Pereira, L., Cabral Coutinho do Rego Monteiro, I., Pontes Dos Santos, L.H., Soares Marreiros Ferraz, A., Carneiro Loureiro, A.C., Calado Lima, C., Leal-Cardoso, J.H., Pires Carvalho, D., and Soares Fortunato, R. (2020). Strenuous Acute Exercise Induces Slow and Fast Twitch-Dependent NADPH Oxidase Expression in Rat Skeletal Muscle. Antioxidants, 9.","DOI":"10.3390\/antiox9010057"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1083\/jcb.201102095","article-title":"Signal transduction by reactive oxygen species","volume":"194","author":"Finkel","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11010-019-03667-9","article-title":"ROS and diseases: Role in metabolism and energy supply","volume":"467","author":"Yang","year":"2020","journal-title":"Mol. Cell. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4250","DOI":"10.1073\/pnas.1816556116","article-title":"Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows","volume":"116","author":"Blum","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1083\/jcb.200605138","article-title":"Dynamic subcompartmentalization of the mitochondrial inner membrane","volume":"175","author":"Vogel","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1777","DOI":"10.1093\/emboj\/19.8.1777","article-title":"Supercomplexes in the respiratory chains of yeast and mammalian mitochondria","volume":"19","author":"Schagger","year":"2000","journal-title":"EMBO J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.bbabio.2008.04.007","article-title":"Is supercomplex organization of the respiratory chain required for optimal electron transfer activity?","volume":"1777","author":"Genova","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.bj.2017.12.001","article-title":"Structure and mechanism of mitochondrial electron transport chain","volume":"41","author":"Guo","year":"2018","journal-title":"Biomed. J."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Protasoni, M., and Zeviani, M. (2021). Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22020586"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1161\/CIRCRESAHA.118.310082","article-title":"Calcium Signaling and Reactive Oxygen Species in Mitochondria","volume":"122","author":"Bertero","year":"2018","journal-title":"Circ. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1042\/BST20110766","article-title":"Calcium signalling remodelling and disease","volume":"40","author":"Berridge","year":"2012","journal-title":"Biochem. Soc. Trans."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Christakos, S., Lieben, L., Masuyama, R., and Carmeliet, G. (2014). Vitamin D endocrine system and the intestine. Bonekey Rep., 3.","DOI":"10.1038\/bonekey.2013.230"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1100\/tsw.2001.489","article-title":"Extracellular and intracellular regulation of calcium homeostasis","volume":"1","author":"Bronner","year":"2001","journal-title":"ScientificWorldJournal"},{"key":"ref_21","first-page":"1155","article-title":"Mitochondrial calcium: Transport and modulation of cellular processes in homeostasis and cancer (Review)","volume":"54","year":"2019","journal-title":"Int. J. Oncol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1111\/j.1469-7793.1998.411bb.x","article-title":"Relations between intracellular Ca2+ stores and store-operated Ca2+ entry in primary cultured human glioblastoma cells","volume":"513","author":"Hartmann","year":"1998","journal-title":"J. Physiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.bbamcr.2017.01.011","article-title":"Identification of residues that control Li+ versus Na+ dependent Ca2+ exchange at the transport site of the mitochondrial NCLX","volume":"1864","author":"Roy","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1038\/nature22082","article-title":"The mitochondrial Na+\/Ca2+ exchanger is essential for Ca2+ homeostasis and viability","volume":"545","author":"Luongo","year":"2017","journal-title":"Nature"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Austin, S., Tavakoli, M., Pfeiffer, C., Seifert, J., Mattarei, A., De Stefani, D., Zoratti, M., and Nowikovsky, K. (2017). LETM1-Mediated K+ and Na+ Homeostasis Regulates Mitochondrial Ca2+ Efflux. Front. Physiol., 8.","DOI":"10.3389\/fphys.2017.00839"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1083\/jcb.201510019","article-title":"Ca2+\/H+ exchange by acidic organelles regulates cell migration in vivo","volume":"212","author":"Melchionda","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1038\/cdd.2016.52","article-title":"The coming of age of the mitochondria-ER contact: A matter of thickness","volume":"23","author":"Giacomello","year":"2016","journal-title":"Cell Death Differ."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.jprot.2012.12.018","article-title":"In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)","volume":"79","author":"Poston","year":"2013","journal-title":"J. Proteom."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.bbrc.2011.12.022","article-title":"The role of cholesterol in the association of endoplasmic reticulum membranes with mitochondria","volume":"417","author":"Fujimoto","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"4106","DOI":"10.1038\/emboj.2012.202","article-title":"Upregulated function of mitochondria-associated ER membranes in Alzheimer disease","volume":"31","author":"Tambini","year":"2012","journal-title":"EMBO J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"E3179","DOI":"10.1073\/pnas.1422363112","article-title":"Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly","volume":"112","author":"AhYoung","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Rajagopal, S., and Ponnusamy, M. (2017). Calcium Ion in Biological Systems. Calcium Signaling: From Physiology to Diseases, Springer.","DOI":"10.1007\/978-981-10-5160-9"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1073\/pnas.0308565100","article-title":"Agonist-induced Ca2+ entry determined by inositol 1,4,5-trisphosphate recognition","volume":"101","author":"Patterson","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1146\/annurev.biochem.73.071403.161303","article-title":"Inositol 1,4,5-trisphosphate receptors as signal integrators","volume":"73","author":"Patterson","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.tcb.2018.01.002","article-title":"Calcium Dynamics as a Machine for Decoding Signals","volume":"28","author":"Giorgi","year":"2018","journal-title":"Trends Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/s41580-018-0052-8","article-title":"The machineries, regulation and cellular functions of mitochondrial calcium","volume":"19","author":"Giorgi","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1007\/BF00762734","article-title":"Physiological role of mitochondrial Ca2+ transport","volume":"26","author":"Hansford","year":"1994","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/nrm1150","article-title":"Regulation of cell death: The calcium-apoptosis link","volume":"4","author":"Orrenius","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1054\/ceca.2000.0138","article-title":"Mitochondrial Ca2+ homeostasis in the regulation of apoptotic and necrotic cell deaths","volume":"28","author":"Zhu","year":"2000","journal-title":"Cell Calcium"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1111\/nph.14966","article-title":"Advances and current challenges in calcium signaling","volume":"218","author":"Kudla","year":"2018","journal-title":"New Phytol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1111\/j.1469-7793.1997.497bm.x","article-title":"Regulation of the cytosolic Ca2+ concentration by Ca2+ stores in single smooth muscle cells from rat cerebral arteries","volume":"501","author":"Kamishima","year":"1997","journal-title":"J. Physiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1111\/j.1469-7793.2000.t01-2-00285.x","article-title":"Mechanisms that regulate [Ca2+]i following depolarization in rat systemic arterial smooth muscle cells","volume":"522","author":"Kamishima","year":"2000","journal-title":"J. Physiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/978-3-030-12457-1_7","article-title":"Cytoplasmic Calcium Buffering: An Integrative Crosstalk","volume":"1131","author":"Gilabert","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3550001","article-title":"Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling","volume":"355","author":"Chiesa","year":"2001","journal-title":"Biochem. J."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1083\/jcb.200105057","article-title":"VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release","volume":"155","author":"Madesh","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Schwaller, B. (2010). Cytosolic Ca2+ buffers. Cold Spring Harb. Perspect. Biol., 2.","DOI":"10.1101\/cshperspect.a004051"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Duvvuri, B., and Lood, C. (2021). Mitochondrial Calcification. Immunometabolism, 3.","DOI":"10.20900\/immunometab20210008"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Shoshan-Barmatz, V., and Mizrachi, D. (2012). VDAC1: From structure to cancer therapy. Front. Oncol., 2.","DOI":"10.3389\/fonc.2012.00164"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1466","DOI":"10.1016\/j.bbamem.2011.10.005","article-title":"VDAC isoforms in mammals","volume":"1818","author":"Messina","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.ceca.2017.06.007","article-title":"VDAC1 functions in Ca2+ homeostasis and cell life and death in health and disease","volume":"69","author":"Krelin","year":"2018","journal-title":"Cell Calcium"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1016\/j.bbamem.2011.12.026","article-title":"VDAC structure, selectivity, and dynamics","volume":"1818","author":"Colombini","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/cdd.2011.92","article-title":"VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria","volume":"19","author":"Bononi","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1038\/s41586-020-2309-6","article-title":"Structure and mechanism of the mitochondrial Ca2+ uniporter holocomplex","volume":"582","author":"Fan","year":"2020","journal-title":"Nature"},{"key":"ref_54","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_55","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1113\/jphysiol.2013.268235","article-title":"The mitochondrial calcium uniporter complex: Molecular components, structure and physiopathological implications","volume":"592","author":"Marchi","year":"2014","journal-title":"J. Physiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.yjmcc.2014.11.015","article-title":"The mitochondrial Ca2+ uniporter complex","volume":"78","author":"Foskett","year":"2015","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_57","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_58","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_59","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_60","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.molcel.2014.01.013","article-title":"MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity","volume":"53","author":"Patron","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_61","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_62","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_63","doi-asserted-by":"crossref","first-page":"11011","DOI":"10.1073\/pnas.1309531110","article-title":"Canonical transient receptor potential 3 channels regulate mitochondrial calcium uptake","volume":"110","author":"Feng","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1038\/ncb1556","article-title":"Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport","volume":"9","author":"Trenker","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1126\/science.1175145","article-title":"Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+\/H+ antiporter","volume":"326","author":"Jiang","year":"2009","journal-title":"Science"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Nakamura, S., Matsui, A., Akabane, S., Tamura, Y., Hatano, A., Miyano, Y., Omote, H., Kajikawa, M., Maenaka, K., and Moriyama, Y. (2020). The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain. Commun Biol., 3.","DOI":"10.1038\/s42003-020-0832-5"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1085\/jgp.201110757","article-title":"Perspectives on: SGP symposium on mitochondrial physiology and medicine: The pathophysiology of LETM1","volume":"139","author":"Nowikovsky","year":"2012","journal-title":"J. Gen. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1016\/j.tibs.2019.04.002","article-title":"LETM1: Essential for Mitochondrial Biology and Cation Homeostasis?","volume":"44","author":"Austin","year":"2019","journal-title":"Trends Biochem. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1042\/bj20021381","article-title":"Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity","volume":"371","author":"Turner","year":"2003","journal-title":"Biochem. J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/ncb1150","article-title":"Rapid vesicular translocation and insertion of TRP channels","volume":"6","author":"Bezzerides","year":"2004","journal-title":"Nat. Cell Biol."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Oancea, E., Vriens, J., Brauchi, S., Jun, J., Splawski, I., and Clapham, D.E. (2009). TRPM1 forms ion channels associated with melanin content in melanocytes. Sci. Signal., 2.","DOI":"10.1126\/scisignal.2000146"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Lange, I., Yamamoto, S., Partida-Sanchez, S., Mori, Y., Fleig, A., and Penner, R. (2009). TRPM2 functions as a lysosomal Ca2+-release channel in beta cells. Sci. Signal., 2.","DOI":"10.1126\/scisignal.2000278"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1038\/nature07311","article-title":"The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel","volume":"455","author":"Dong","year":"2008","journal-title":"Nature"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1021\/pr070496k","article-title":"Analysis of TRPC3-interacting proteins by tandem mass spectrometry","volume":"7","author":"Lockwich","year":"2008","journal-title":"J. Proteome Res."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"10556","DOI":"10.1073\/pnas.1106183108","article-title":"PKC-dependent coupling of calcium permeation through transient receptor potential canonical 3 (TRPC3) to calcineurin signaling in HL-1 myocytes","volume":"108","author":"Poteser","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_76","first-page":"667","article-title":"Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling","volume":"29","author":"Jezek","year":"2018","journal-title":"Antioxid. Redox Signal."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1469-7793.2000.00003.x","article-title":"Mitochondrial uncoupling proteins: From mitochondria to the regulation of energy balance","volume":"529","author":"Ricquier","year":"2000","journal-title":"J. Physiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.mito.2020.10.003","article-title":"The contribution of uncoupling protein 2 to mitochondrial Ca2+ homeostasis in health and disease\u2014A short revisit","volume":"55","author":"Koshenov","year":"2020","journal-title":"Mitochondrion"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Gottschalk, B., Klec, C., Leitinger, G., Bernhart, E., Rost, R., Bischof, H., Madreiter-Sokolowski, C.T., Radulovic, S., Eroglu, E., and Sattler, W. (2019). MICU1 controls cristae junction and spatially anchors mitochondrial Ca2+ uniporter complex. Nat. Commun., 10.","DOI":"10.1038\/s41467-019-11692-x"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"215","DOI":"10.2174\/1389202917666160202215748","article-title":"Transport of Calcium Ions into Mitochondria","volume":"17","author":"Xu","year":"2016","journal-title":"Curr. Genom."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Lanner, J.T., Georgiou, D.K., Joshi, A.D., and Hamilton, S.L. (2010). Ryanodine receptors: Structure, expression, molecular details, and function in calcium release. Cold Spring Harb. Perspect. Biol., 2.","DOI":"10.1101\/cshperspect.a003996"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Bauerova-Hlinkova, V., Hajduchova, D., and Bauer, J.A. (2020). Structure and Function of the Human Ryanodine Receptors and Their Association with Myopathies-Present State, Challenges, and Perspectives. Molecules, 25.","DOI":"10.3390\/molecules25184040"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"25234","DOI":"10.1074\/jbc.M401229200","article-title":"Lithium-calcium exchange is mediated by a distinct potassium-independent sodium-calcium exchanger","volume":"279","author":"Palty","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1074\/jbc.270.2.672","article-title":"The sodium-calcium antiport of heart mitochondria is not electroneutral","volume":"270","author":"Jung","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"3267","DOI":"10.1113\/jphysiol.2008.151977","article-title":"Analysis of cardiac mitochondrial Na+-Ca2+ exchanger kinetics with a biophysical model of mitochondrial Ca2+ handling suggests a 3:1 stoichiometry","volume":"586","author":"Dash","year":"2008","journal-title":"J. Physiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"21640","DOI":"10.1016\/S0021-9258(18)54685-8","article-title":"The Na+-independent Ca2+ efflux mechanism of liver mitochondria is not a passive Ca2+\/2H+ exchanger","volume":"266","author":"Gunter","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_87","first-page":"5566","article-title":"NCX3 regulates mitochondrial Ca2+ handling through the AKAP121-anchored signaling complex and prevents hypoxia-induced neuronal death","volume":"126","author":"Scorziello","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1126\/science.8235595","article-title":"Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria","volume":"262","author":"Rizzuto","year":"1993","journal-title":"Science"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1016\/j.bbabio.2009.03.015","article-title":"Ca2+ transfer from the ER to mitochondria: When, how and why","volume":"1787","author":"Rizzuto","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Scorrano, L., De Matteis, M.A., Emr, S., Giordano, F., Hajnoczky, G., Kornmann, B., Lackner, L.L., Levine, T.P., Pellegrini, L., and Reinisch, K. (2019). Coming together to define membrane contact sites. Nat. Commun., 10.","DOI":"10.1038\/s41467-019-09253-3"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Montes de Oca Balderas, P. (2021). Mitochondria-plasma membrane interactions and communication. J. Biol. Chem., 297.","DOI":"10.1016\/j.jbc.2021.101164"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.bbabio.2010.05.005","article-title":"Mitochondria: The calcium connection","volume":"1797","author":"Contreras","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1113\/jphysiol.2013.255661","article-title":"The coupling of plasma membrane calcium entry to calcium uptake by endoplasmic reticulum and mitochondria","volume":"592","year":"2014","journal-title":"J. Physiol."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Bartok, A., Weaver, D., Golenar, T., Nichtova, Z., Katona, M., Bansaghi, S., Alzayady, K.J., Thomas, V.K., Ando, H., and Mikoshiba, K. (2019). IP3 receptor isoforms differently regulate ER-mitochondrial contacts and local calcium transfer. Nat. Commun., 10.","DOI":"10.1038\/s41467-019-11646-3"},{"key":"ref_95","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":"ref_96","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s00424-012-1112-0","article-title":"Mitochondria, calcium-dependent neuronal death and neurodegenerative disease","volume":"464","author":"Duchen","year":"2012","journal-title":"Pflugers Arch."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1016\/j.celrep.2016.05.013","article-title":"Presenilin 2 Modulates Endoplasmic Reticulum-Mitochondria Coupling by Tuning the Antagonistic Effect of Mitofusin 2","volume":"15","author":"Filadi","year":"2016","journal-title":"Cell Rep."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1126\/science.1132814","article-title":"A century of Alzheimer\u2019s disease","volume":"314","author":"Goedert","year":"2006","journal-title":"Science"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1172\/JCI30447","article-title":"Familial Alzheimer disease-linked mutations specifically disrupt Ca2+ leak function of presenilin 1","volume":"117","author":"Nelson","year":"2007","journal-title":"J. Clin. Investig."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"357","DOI":"10.4161\/cib.4.3.15160","article-title":"Presenilin-2 modulation of ER-mitochondria interactions: FAD mutations, mechanisms and pathological consequences","volume":"4","author":"Zampese","year":"2011","journal-title":"Commun. Integr. Biol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"S265","DOI":"10.3233\/JAD-2010-100339","article-title":"The Alzheimer\u2019s disease mitochondrial cascade hypothesis","volume":"20","author":"Swerdlow","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"ref_102","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_103","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1083\/jcb.200608073","article-title":"Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels","volume":"175","author":"Szabadkai","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.neo.2018.03.005","article-title":"Role of Mitochondria-Associated ER Membranes in Calcium Regulation in Cancer-Specific Settings","volume":"20","author":"Morciano","year":"2018","journal-title":"Neoplasia"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1083\/jcb.200205091","article-title":"Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria","volume":"159","author":"Rapizzi","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.cell.2007.08.036","article-title":"Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca2+ signaling and cell survival","volume":"131","author":"Hayashi","year":"2007","journal-title":"Cell"},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Ouyang, Y.B., and Giffard, R.G. (2012). ER-Mitochondria Crosstalk during Cerebral Ischemia: Molecular Chaperones and ER-Mitochondrial Calcium Transfer. Int. J. Cell Biol., 2012.","DOI":"10.1155\/2012\/493934"},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Stoica, R., De Vos, K.J., Paillusson, S., Mueller, S., Sancho, R.M., Lau, K.F., Vizcay-Barrena, G., Lin, W.L., Xu, Y.F., and Lewis, J. (2014). ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS\/FTD-associated TDP-43. Nat. Commun., 5.","DOI":"10.1038\/ncomms4996"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1093\/hmg\/ddr559","article-title":"VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis","volume":"21","author":"Morotz","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1126\/science.aab1370","article-title":"PI4P\/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts","volume":"349","author":"Chung","year":"2015","journal-title":"Science"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1126\/science.aaq0141","article-title":"Mediating ER-mitochondrial cross-talk","volume":"358","author":"Lombardi","year":"2017","journal-title":"Science"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Pascual-Ahuir, A., Manzanares-Estreder, S., and Proft, M. (2017). Pro- and Antioxidant Functions of the Peroxisome-Mitochondria Connection and Its Impact on Aging and Disease. Oxid. Med. Cell. Longev., 2017.","DOI":"10.1155\/2017\/9860841"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.abb.2014.05.001","article-title":"Oxidatively generated base damage to cellular DNA by hydroxyl radical and one-electron oxidants: Similarities and differences","volume":"557","author":"Cadet","year":"2014","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1016\/j.bcp.2008.11.009","article-title":"Reactive oxygen species: Destroyers or messengers?","volume":"77","author":"Bartosz","year":"2009","journal-title":"Biochem. Pharmacol."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Di Meo, S., Reed, T.T., Venditti, P., and Victor, V.M. (2016). Role of ROS and RNS Sources in Physiological and Pathological Conditions. Oxid. Med. Cell. Longev., 2016.","DOI":"10.1155\/2016\/1245049"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.redox.2016.12.035","article-title":"Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress","volume":"11","author":"Sies","year":"2017","journal-title":"Redox. Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1042\/bst0290345","article-title":"Role of reactive oxygen species in cell signalling pathways","volume":"29","author":"Hancock","year":"2001","journal-title":"Biochem. Soc. Trans."},{"key":"ref_118","first-page":"5850","article-title":"Absorption, metabolism and protective role of fruits and vegetables polyphenols against gastric cancer","volume":"21","author":"Metere","year":"2017","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., and Wang, H. (2019). Biochemical basis and metabolic interplay of redox regulation. Redox. Biol., 26.","DOI":"10.1016\/j.redox.2019.101284"},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Tan, B.L., Norhaizan, M.E., Liew, W.P., and Sulaiman Rahman, H. (2018). Antioxidant and Oxidative Stress: A Mutual Interplay in Age-Related Diseases. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.01162"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.redox.2015.08.010","article-title":"Calcium and ROS: A mutual interplay","volume":"6","author":"Gorlach","year":"2015","journal-title":"Redox. Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"S413","DOI":"10.3233\/JAD-2010-100465","article-title":"Calcium and mitochondrial reactive oxygen species generation: How to read the facts","volume":"20","author":"Starkov","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"C817","DOI":"10.1152\/ajpcell.00139.2004","article-title":"Calcium, ATP, and ROS: A mitochondrial love-hate triangle","volume":"287","author":"Brookes","year":"2004","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.2741\/3303","article-title":"Crosstalk signaling between mitochondrial Ca2+ and ROS","volume":"14","author":"Feissner","year":"2009","journal-title":"Front. Biosci."},{"key":"ref_125","first-page":"1077","article-title":"Cross-talk between reactive oxygen species and calcium in living cells","volume":"68","author":"Gordeeva","year":"2003","journal-title":"Biochemistry"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/978-1-62703-386-2_12","article-title":"Oxidative modifications of mitochondria complex II","volume":"1005","author":"Zhang","year":"2013","journal-title":"Methods Mol. Biol."},{"key":"ref_127","first-page":"75","article-title":"Relationship between metabolic rate, free radicals, differentiation and aging: A unified theory","volume":"35","author":"Sohal","year":"1985","journal-title":"Basic Life Sci."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1042\/bj20021121","article-title":"Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state","volume":"368","author":"Kushnareva","year":"2002","journal-title":"Biochem. J."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"4127","DOI":"10.1074\/jbc.M310341200","article-title":"Characterization of superoxide-producing sites in isolated brain mitochondria","volume":"279","author":"Kudin","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/CS20110643","article-title":"Systems biology of antioxidants","volume":"123","author":"Andriantsitohaina","year":"2012","journal-title":"Clin. Sci."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1111\/j.1749-6632.2010.05634.x","article-title":"Oxidative stress caused by mitochondrial calcium overload","volume":"1201","author":"Peng","year":"2010","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1172\/JCI120849","article-title":"Mitochondrial dysfunction in pathophysiology of heart failure","volume":"128","author":"Zhou","year":"2018","journal-title":"J. Clin. Investig."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1084\/jem.192.7.1001","article-title":"Reactive oxygen species (ROS)-induced ROS release: A new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes","volume":"192","author":"Zorov","year":"2000","journal-title":"J. Exp. Med."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Millare, B., O\u2019Rourke, B., and Trayanova, N. (2020). Hydrogen peroxide diffusion and scavenging shapes mitochondrial network instability and failure by sensitizing ROS-induced ROS release. Sci. Rep., 10.","DOI":"10.1038\/s41598-020-71308-z"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1007\/s11897-017-0347-7","article-title":"Targeting Mitochondrial Calcium Handling and Reactive Oxygen Species in Heart Failure","volume":"14","author":"Dietl","year":"2017","journal-title":"Curr. Heart Fail. Rep."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.freeradbiomed.2017.11.028","article-title":"ROS-induced ROS release in plant and animal cells","volume":"122","author":"Zandalinas","year":"2018","journal-title":"Free Radic Biol. Med."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"2777","DOI":"10.1073\/pnas.1100735108","article-title":"Presenilin 2 modulates endoplasmic reticulum (ER)-mitochondria interactions and Ca2+ cross-talk","volume":"108","author":"Zampese","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Simon-Gozalbo, A., Rodriguez-Blazquez, C., Forjaz, M.J., and Martinez-Martin, P. (2020). Clinical Characterization of Parkinson\u2019s Disease Patients with Cognitive Impairment. Front. Neurol., 11.","DOI":"10.3389\/fneur.2020.00731"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","article-title":"A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington\u2019s disease chromosomes","volume":"72","author":"MacDonald","year":"1993","journal-title":"Cell"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"952","DOI":"10.2174\/1567205013666160314150501","article-title":"Molecular Basis of Familial and Sporadic Alzheimer\u2019s Disease","volume":"13","author":"Dorszewska","year":"2016","journal-title":"Curr. Alzheimer Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease at 25 years","volume":"8","author":"Selkoe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"13145","DOI":"10.1073\/pnas.0806192105","article-title":"The amyloid beta-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_143","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.mito.2013.03.008","article-title":"Mitochondrial respiratory chain Complexes I and IV are impaired by beta-amyloid via direct interaction and through Complex I-dependent ROS production, respectively","volume":"13","author":"Bobba","year":"2013","journal-title":"Mitochondrion"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.ceca.2009.12.014","article-title":"The dysregulation of intracellular calcium in Alzheimer disease","volume":"47","author":"Supnet","year":"2010","journal-title":"Cell Calcium"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.bbadis.2009.07.005","article-title":"Mitochondrial permeability transition pore in Alzheimer\u2019s disease: Cyclophilin D and amyloid beta","volume":"1802","author":"Du","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Britti, E., Ros, J., Esteras, N., and Abramov, A.Y. (2020). Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death. Cell Calcium, 86.","DOI":"10.1016\/j.ceca.2019.102150"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/CS20200844","article-title":"Mitochondria-associated membranes (MAMs): A potential therapeutic target for treating Alzheimer\u2019s disease","volume":"135","author":"Yu","year":"2021","journal-title":"Clin. Sci."},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Cheung, K.H., Mei, L., Mak, D.O., Hayashi, I., Iwatsubo, T., Kang, D.E., and Foskett, J.K. (2010). Gain-of-function enhancement of IP3 receptor modal gating by familial Alzheimer\u2019s disease-linked presenilin mutants in human cells and mouse neurons. Sci. Signal., 3.","DOI":"10.1126\/scisignal.2000818"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"18195","DOI":"10.1074\/jbc.M000040200","article-title":"Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons","volume":"275","author":"Chan","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1534\/genetics.115.182808","article-title":"A gamma-Secretase Independent Role for Presenilin in Calcium Homeostasis Impacts Mitochondrial Function and Morphology in Caenorhabditis elegans","volume":"201","author":"Sarasija","year":"2015","journal-title":"Genetics"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1046\/j.1471-4159.1995.64020749.x","article-title":"Neurochemical correlates of dementia severity in Alzheimer\u2019s disease: Relative importance of the cholinergic deficits","volume":"64","author":"Bierer","year":"1995","journal-title":"J. Neurochem."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Jadiya, P., Garbincius, J.F., and Elrod, J.W. (2021). Reappraisal of metabolic dysfunction in neurodegeneration: Focus on mitochondrial function and calcium signaling. Acta Neuropathol. Commun., 9.","DOI":"10.1186\/s40478-021-01224-4"},{"key":"ref_153","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_154","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj1280161","article-title":"Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase","volume":"128","author":"Denton","year":"1972","journal-title":"Biochem. J."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1002\/mds.27723","article-title":"Peripheral mitochondrial function correlates with clinical severity in idiopathic Parkinson\u2019s disease","volume":"34","author":"Milanese","year":"2019","journal-title":"Mov. Disord."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1002\/ana.24571","article-title":"Mitochondrial DNA Depletion in Respiratory Chain-Deficient Parkinson Disease Neurons","volume":"79","author":"Grunewald","year":"2016","journal-title":"Ann. Neurol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/B978-0-12-800223-0.00003-7","article-title":"Vesicular neurotransmitter transporters: Mechanistic aspects","volume":"73","author":"Anne","year":"2014","journal-title":"Curr. Top. Membr."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2058","DOI":"10.1093\/brain\/aws133","article-title":"Alterations in axonal transport motor proteins in sporadic and experimental Parkinson\u2019s disease","volume":"135","author":"Chu","year":"2012","journal-title":"Brain"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.nbd.2012.05.015","article-title":"The interplay of neuronal mitochondrial dynamics and bioenergetics: Implications for Parkinson\u2019s disease","volume":"51","author":"Berman","year":"2013","journal-title":"Neurobiol. Dis."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Modesti, L., Danese, A., Angela Maria Vitto, V., Ramaccini, D., Aguiari, G., Gafa, R., Lanza, G., Giorgi, C., and Pinton, P. (2021). Mitochondrial Ca2+ Signaling in Health, Disease and Therapy. Cells, 10.","DOI":"10.3390\/cells10061317"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/j.bbrc.2016.08.168","article-title":"Calcium and Parkinson\u2019s disease","volume":"483","author":"Surmeier","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/nature05865","article-title":"\u2018Rejuvenation\u2019 protects neurons in mouse models of Parkinson\u2019s disease","volume":"447","author":"Chan","year":"2007","journal-title":"Nature"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1111\/j.1749-6632.1992.tb24523.x","article-title":"Midbrain dopaminergic cell loss in Parkinson\u2019s disease and MPTP-induced parkinsonism: Sparing of calbindin-D28k-containing cells","volume":"648","author":"German","year":"1992","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/33416","article-title":"Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism","volume":"392","author":"Kitada","year":"1998","journal-title":"Nature"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1126\/science.1096284","article-title":"Hereditary early-onset Parkinson\u2019s disease caused by mutations in PINK1","volume":"304","author":"Valente","year":"2004","journal-title":"Science"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.molcel.2009.02.013","article-title":"PINK1-associated Parkinson\u2019s disease is caused by neuronal vulnerability to calcium-induced cell death","volume":"33","author":"Gandhi","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Ge, P., Dawson, V.L., and Dawson, T.M. (2020). PINK1 and Parkin mitochondrial quality control: A source of regional vulnerability in Parkinson\u2019s disease. Mol. Neurodegener., 15.","DOI":"10.1186\/s13024-020-00367-7"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Huang, E., Qu, D., Huang, T., Rizzi, N., Boonying, W., Krolak, D., Ciana, P., Woulfe, J., Klein, C., and Slack, R.S. (2017). PINK1-mediated phosphorylation of LETM1 regulates mitochondrial calcium transport and protects neurons against mitochondrial stress. Nat. Commun., 8.","DOI":"10.1038\/s41467-017-01435-1"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Ludtmann, M.H.R., Kostic, M., Horne, A., Gandhi, S., Sekler, I., and Abramov, A.Y. (2019). LRRK2 deficiency induced mitochondrial Ca2+ efflux inhibition can be rescued by Na+\/Ca2+\/Li+ exchanger upregulation. Cell Death Dis., 10.","DOI":"10.1038\/s41419-019-1469-5"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"11151","DOI":"10.1523\/JNEUROSCI.3791-16.2017","article-title":"Mitochondrial Calcium Dysregulation Contributes to Dendrite Degeneration Mediated by PD\/LBD-Associated LRRK2 Mutants","volume":"37","author":"Verma","year":"2017","journal-title":"J. Neurosci."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"12305","DOI":"10.1523\/JNEUROSCI.3088-08.2008","article-title":"Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria","volume":"28","author":"Nakamura","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1523\/JNEUROSCI.2507-13.2014","article-title":"alpha-Synuclein is localized to mitochondria-associated ER membranes","volume":"34","author":"Rub","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1002\/biof.162","article-title":"Huntington\u2019s disease, calcium, and mitochondria","volume":"37","author":"Giacomello","year":"2011","journal-title":"Biofactors"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/j.mcn.2003.11.014","article-title":"Potentiation of NMDA receptor-mediated excitotoxicity linked with intrinsic apoptotic pathway in YAC transgenic mouse model of Huntington\u2019s disease","volume":"25","author":"Zeron","year":"2004","journal-title":"Mol. Cell Neurosci."},{"key":"ref_175","doi-asserted-by":"crossref","unstructured":"Abramov, A.Y., Potapova, E.V., Dremin, V.V., and Dunaev, A.V. (2020). Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration. Life, 10.","DOI":"10.3390\/life10070101"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nn884","article-title":"Early mitochondrial calcium defects in Huntington\u2019s disease are a direct effect of polyglutamines","volume":"5","author":"Panov","year":"2002","journal-title":"Nat. Neurosci."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1111\/jnc.13165","article-title":"Ca2+ handling in isolated brain mitochondria and cultured neurons derived from the YAC128 mouse model of Huntington\u2019s disease","volume":"134","author":"Pellman","year":"2015","journal-title":"J. Neurochem."},{"key":"ref_178","first-page":"2762","article-title":"Oxidative metabolism and Ca2+ handling in isolated brain mitochondria and striatal neurons from R6\/2 mice, a model of Huntington\u2019s disease","volume":"25","author":"Hamilton","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Smith, E.F., Shaw, P.J., and De Vos, K.J. (2019). The role of mitochondria in amyotrophic lateral sclerosis. Neurosci. Lett., 710.","DOI":"10.1016\/j.neulet.2017.06.052"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/nn.3584","article-title":"State of play in amyotrophic lateral sclerosis genetics","volume":"17","author":"Renton","year":"2014","journal-title":"Nat. Neurosci."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.mad.2010.05.003","article-title":"Mitochondrial dysfunction and intracellular calcium dysregulation in ALS","volume":"131","author":"Kawamata","year":"2010","journal-title":"Mech. Ageing Dev."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Barrett, E.F., Barrett, J.N., and David, G. (2014). Dysfunctional mitochondrial Ca2+ handling in mutant SOD1 mouse models of fALS: Integration of findings from motor neuron somata and motor terminals. Front. Cell Neurosci., 8.","DOI":"10.3389\/fncel.2014.00184"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.expneurol.2015.09.019","article-title":"Excitotoxicity in ALS: Overstimulation, or overreaction?","volume":"275","author":"King","year":"2016","journal-title":"Exp. Neurol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"R844","DOI":"10.1152\/ajpregu.00528.2010","article-title":"Metabolic and functional differences between brain and spinal cord mitochondria underlie different predisposition to pathology","volume":"300","author":"Panov","year":"2011","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.neuron.2016.12.034","article-title":"Transient Opening of the Mitochondrial Permeability Transition Pore Induces Microdomain Calcium Transients in Astrocyte Processes","volume":"93","author":"Agarwal","year":"2017","journal-title":"Neuron"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.neuron.2004.06.021","article-title":"Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria","volume":"43","author":"Pasinelli","year":"2004","journal-title":"Neuron"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1046\/j.1471-4159.2002.01112.x","article-title":"Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis","volume":"83","author":"Jung","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_188","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_189","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_190","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_191","doi-asserted-by":"crossref","first-page":"12239","DOI":"10.1073\/pnas.220403797","article-title":"Frataxin activates mitochondrial energy conversion and oxidative phosphorylation","volume":"97","author":"Ristow","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Britti, E., Delaspre, F., Tamarit, J., and Ros, J. (2018). Mitochondrial calcium signalling and neurodegenerative diseases. Neuronal. Signal., 2.","DOI":"10.1042\/NS20180061"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1002\/mus.20598","article-title":"Approaches to the treatment of mitochondrial diseases","volume":"34","author":"DiMauro","year":"2006","journal-title":"Muscle Nerve"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1196\/annals.1293.023","article-title":"Mitochondrial encephalomyopathies: Therapeutic approach","volume":"1011","author":"Dimauro","year":"2004","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/s10540-007-9041-4","article-title":"Mitochondrial diseases: Therapeutic approaches","volume":"27","author":"DiMauro","year":"2007","journal-title":"Biosci. Rep."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nrg1606","article-title":"Mitochondrial DNA mutations in human disease","volume":"6","author":"Taylor","year":"2005","journal-title":"Nat. Rev. Genet."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/bs.pmbts.2014.12.004","article-title":"Chapter Five\u2014The Contribution of Mitochondria to Sensory Processing and Pain","volume":"Volume 131","author":"Price","year":"2015","journal-title":"Progress in Molecular Biology and Translational Science"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1002\/cpt.1548","article-title":"N-Acetyl Cysteine Is Associated with Dopaminergic Improvement in Parkinson\u2019s Disease","volume":"106","author":"Monti","year":"2019","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Wright, D.J., Renoir, T., Smith, Z.M., Frazier, A.E., Francis, P.S., Thorburn, D.R., McGee, S.L., Hannan, A.J., and Gray, L.J. (2015). N-Acetylcysteine improves mitochondrial function and ameliorates behavioral deficits in the R6\/1 mouse model of Huntington\u2019s disease. Transl. Psychiatry, 5.","DOI":"10.1038\/tp.2014.131"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1089\/ars.2016.6905","article-title":"Mito-Apocynin Prevents Mitochondrial Dysfunction, Microglial Activation, Oxidative Damage, and Progressive Neurodegeneration in MitoPark Transgenic Mice","volume":"27","author":"Langley","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/s11481-016-9650-4","article-title":"Mitoapocynin Treatment Protects Against Neuroinflammation and Dopaminergic Neurodegeneration in a Preclinical Animal Model of Parkinson\u2019s Disease","volume":"11","author":"Ghosh","year":"2016","journal-title":"J. Neuroimmune Pharmacol."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"6251","DOI":"10.1007\/s12035-015-9527-1","article-title":"N-Methyl, N-propynyl-2-phenylethylamine (MPPE), a Selegiline Analog, Attenuates MPTP-induced Dopaminergic Toxicity with Guaranteed Behavioral Safety: Involvement of Inhibitions of Mitochondrial Oxidative Burdens and p53 Gene-elicited Pro-apoptotic Change","volume":"53","author":"Shin","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.ejphar.2006.11.011","article-title":"Novel neuroprotective mechanisms of pramipexole, an anti-Parkinson drug, against endogenous dopamine-mediated excitotoxicity","volume":"557","author":"Izumi","year":"2007","journal-title":"Eur. J. Pharmacol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1002\/jcph.1575","article-title":"Pharmacokinetics, Safety, and Tolerability of Orally Administered Ursodeoxycholic Acid in Patients with Parkinson\u2019s Disease-A Pilot Study","volume":"60","author":"Sathe","year":"2020","journal-title":"J. Clin. Pharmacol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1007\/s12035-014-9043-8","article-title":"Ursodeoxycholic Acid Ameliorates Apoptotic Cascade in the Rotenone Model of Parkinson\u2019s Disease: Modulation of Mitochondrial Perturbations","volume":"53","author":"Abdelkader","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Hawking, Z.L. (2016). Alzheimer\u2019s disease: The role of mitochondrial dysfunction and potential new therapies. Biosci. Horiz. Int. J. Stud. Res., 9.","DOI":"10.1093\/biohorizons\/hzw014"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1016\/j.bbadis.2013.10.015","article-title":"Oxidative stress and mitochondrial dysfunction in Alzheimer\u2019s disease","volume":"1842","author":"Wang","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1517\/14728222.9.4.639","article-title":"Novel therapeutic targets for Huntington\u2019s disease","volume":"9","author":"Hannan","year":"2005","journal-title":"Expert Opin. Ther. Targets"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.aquatox.2018.03.024","article-title":"Effects of bisphenol A and its analogs bisphenol F and S on life parameters, antioxidant system, and response of defensome in the marine rotifer Brachionus koreanus","volume":"199","author":"Park","year":"2018","journal-title":"Aquat. Toxicol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1042\/BST20170501","article-title":"Mitochondrial abnormalities in Parkinson\u2019s disease and Alzheimer\u2019s disease: Can mitochondria be targeted therapeutically?","volume":"46","author":"Macdonald","year":"2018","journal-title":"Biochem. Soc. Trans."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/bs.ircmb.2016.08.003","article-title":"Mitochondria in Multiple Sclerosis: Molecular Mechanisms of Pathogenesis","volume":"328","author":"Patergnani","year":"2017","journal-title":"Int. Rev. Cell Mol. Biol."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/11\/5\/801\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:57:34Z","timestamp":1760137054000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/11\/5\/801"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,20]]},"references-count":211,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["antiox11050801"],"URL":"https:\/\/doi.org\/10.3390\/antiox11050801","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,20]]}}}