{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T16:02:03Z","timestamp":1790352123265,"version":"4.1.0"},"reference-count":219,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2023,11,16]],"date-time":"2023-11-16T00:00:00Z","timestamp":1700092800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"BioNexus KC 19-1 Patton Trust Research Grant","award":["P30 AG072973"],"award-info":[{"award-number":["P30 AG072973"]}]},{"name":"ApoPharma, Inc.","award":["P30 AG072973"],"award-info":[{"award-number":["P30 AG072973"]}]},{"DOI":"10.13039\/100000002","name":"University of Kansas Alzheimer\u2019s Disease Research Center","doi-asserted-by":"publisher","award":["P30 AG072973"],"award-info":[{"award-number":["P30 AG072973"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"University of Kansas School of Medicine Investigator Assistance Award","award":["P30 AG072973"],"award-info":[{"award-number":["P30 AG072973"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>The recently presented Azalea Hypothesis for Alzheimer\u2019s disease asserts that iron becomes sequestered, leading to a functional iron deficiency that contributes to neurodegeneration. Iron sequestration can occur by iron being bound to protein aggregates, such as amyloid \u03b2 and tau, iron-rich structures not undergoing recycling (e.g., due to disrupted ferritinophagy and impaired mitophagy), and diminished delivery of iron from the lysosome to the cytosol. Reduced iron availability for biochemical reactions causes cells to respond to acquire additional iron, resulting in an elevation in the total iron level within affected brain regions. As the amount of unavailable iron increases, the level of available iron decreases until eventually it is unable to meet cellular demands, which leads to a functional iron deficiency. Normally, the lysosome plays an integral role in cellular iron homeostasis by facilitating both the delivery of iron to the cytosol (e.g., after endocytosis of the iron\u2013transferrin\u2013transferrin receptor complex) and the cellular recycling of iron. During a lysosomal storage disorder, an enzyme deficiency causes undigested substrates to accumulate, causing a sequelae of pathogenic events that may include cellular iron dyshomeostasis. Thus, a functional deficiency of iron may be a pathogenic mechanism occurring within several lysosomal storage diseases and Alzheimer\u2019s disease.<\/jats:p>","DOI":"10.3390\/cells12222641","type":"journal-article","created":{"date-parts":[[2023,11,17]],"date-time":"2023-11-17T00:49:47Z","timestamp":1700182187000},"page":"2641","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Examining the Role of a Functional Deficiency of Iron in Lysosomal Storage Disorders with Translational Relevance to Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"12","author":[{"given":"Steven M.","family":"LeVine","sequence":"first","affiliation":[{"name":"Department of Cell Biology and Physiology, University of Kansas Medical Center, Kansas City, KS 66160, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,11,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"LeVine, S.M. (2023). The Azalea Hypothesis of Alzheimer Disease: A Functional Iron Deficiency Promotes Neurodegeneration. Neuroscientist, 10738584231191743.","DOI":"10.1177\/10738584231191743"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1111\/j.1471-4159.1993.tb03639.x","article-title":"Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of \u03b2-amyloid peptide","volume":"61","author":"Mantyh","year":"1993","journal-title":"J. Neurochem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"10992","DOI":"10.1074\/jbc.M709634200","article-title":"Single particle characterization of iron-induced pore-forming \u03b1-synuclein oligomers","volume":"283","author":"Kostka","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.bbrc.2011.06.135","article-title":"Single particle analysis of tau oligomer formation induced by metal ions and organic solvents","volume":"411","author":"Bader","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.electacta.2017.03.175","article-title":"Electrochemical studies of tau protein-iron interactions\u2014Potential implications for Alzheimer\u2019s Disease","volume":"236","author":"Ahmadi","year":"2017","journal-title":"Electrochim. Acta"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2264","DOI":"10.1073\/pnas.261708798","article-title":"Iron deficiency and iron excess damage mitochondria and mitochondrial DNA in rats","volume":"99","author":"Walter","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1159\/000448514","article-title":"Iron Deficiency Impairs Developing Hippocampal Neuron Gene Expression, Energy Metabolism, and Dendrite Complexity","volume":"38","author":"Bastian","year":"2016","journal-title":"Dev. Neurosci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1523\/JNEUROSCI.1504-18.2018","article-title":"Chronic Energy Depletion due to Iron Deficiency Impairs Dendritic Mitochondrial Motility during Hippocampal Neuron Development","volume":"39","author":"Bastian","year":"2019","journal-title":"J. Neurosci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1016\/j.bbadis.2013.09.003","article-title":"Mitochondrial permeability transition pore is a potential drug target for neurodegeneration","volume":"1842","author":"Rao","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"113309","DOI":"10.1016\/j.expneurol.2020.113309","article-title":"Mitochondrial biogenesis as a therapeutic target for traumatic and neurodegenerative CNS diseases","volume":"329","author":"Simmons","year":"2020","journal-title":"Exp. Neurol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.4103\/1673-5374.360279","article-title":"Overcoming mitochondrial dysfunction in neurodegenerative diseases","volume":"18","author":"Pessoa","year":"2023","journal-title":"Neural Regen. Res."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.neuron.2020.01.024","article-title":"Not Fade Away: Mechanisms of Neuronal ATP Homeostasis","volume":"105","author":"Davis","year":"2020","journal-title":"Neuron"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/j.cell.2012.02.035","article-title":"Mitochondria: In sickness and in health","volume":"148","author":"Nunnari","year":"2012","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/nature05292","article-title":"Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases","volume":"443","author":"Lin","year":"2006","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1152\/physrev.00026.2013","article-title":"Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release","volume":"94","author":"Zorov","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"3206","DOI":"10.1002\/jnr.21290","article-title":"Bioenergetics of mitochondria in cultured neurons and their role in glutamate excitotoxicity","volume":"85","author":"Nicholls","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e13378","DOI":"10.7554\/eLife.13378","article-title":"Alleviation of neuronal energy deficiency by mTOR inhibition as a treatment for mitochondria-related neurodegeneration","volume":"5","author":"Zheng","year":"2016","journal-title":"Elife"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1016\/j.celrep.2020.01.060","article-title":"Defective Mitochondrial Pyruvate Flux Affects Cell Bioenergetics in Alzheimer\u2019s Disease-Related Models","volume":"30","author":"Rossi","year":"2020","journal-title":"Cell Rep."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1007\/s10571-020-00924-0","article-title":"Building a Bridge Between NMDAR-Mediated Excitotoxicity and Mitochondrial Dysfunction in Chronic and Acute Diseases","volume":"41","author":"Mira","year":"2021","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"7497","DOI":"10.1093\/nar\/gkm821","article-title":"Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer\u2019s disease","volume":"35","author":"Lovell","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.3233\/JAD-160763","article-title":"Role of Glutamate and NMDA Receptors in Alzheimer\u2019s Disease","volume":"57","author":"Wang","year":"2017","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.2174\/1386207325666220428112541","article-title":"NMDA Inhibitors: A Potential Contrivance to Assist in Management of Alzheimer\u2019s Disease","volume":"26","author":"Painuli","year":"2023","journal-title":"Comb. Chem. High Throughput Screen."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1002\/glia.20784","article-title":"Oligodendrocytes and myelination: The role of iron","volume":"57","author":"Todorich","year":"2009","journal-title":"Glia"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/nrneurol.2014.118","article-title":"Iron in multiple sclerosis: Roles in neurodegeneration and repair","volume":"10","author":"Stephenson","year":"2014","journal-title":"Nat. Rev. Neurol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2637","DOI":"10.1002\/alz.12733","article-title":"Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer\u2019s disease","volume":"18","author":"Liu","year":"2022","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"LeVine, S.M., Tsau, S., and Gunewardena, S. (2023). Exploring Whether Iron Sequestration within the CNS of Patients with Alzheimer\u2019s Disease Causes a Functional Iron Deficiency That Advances Neurodegeneration. Brain Sci., 13.","DOI":"10.3390\/brainsci13030511"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Jeong, S.Y., Crooks, D.R., Wilson-Ollivierre, H., Ghosh, M.C., Sougrat, R., Lee, J., Cooperman, S., Mitchell, J.B., Beaumont, C., and Rouault, T.A. (2011). Iron insufficiency compromises motor neurons and their mitochondrial function in Irp2-null mice. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025404"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1002\/hipo.22004","article-title":"Temporal manipulation of transferrin-receptor-1-dependent iron uptake identifies a sensitive period in mouse hippocampal neurodevelopment","volume":"22","author":"Fretham","year":"2012","journal-title":"Hippocampus"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1083\/jcb.201208152","article-title":"The cell biology of disease: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction","volume":"199","author":"Platt","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1002\/iub.1288","article-title":"Impairment of homeostasis in lysosomal storage disorders","volume":"66","author":"Segatori","year":"2014","journal-title":"IUBMB Life"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Pandey, M.K. (2023). Exploring Pro-Inflammatory Immunological Mediators: Unraveling the Mechanisms of Neuroinflammation in Lysosomal Storage Diseases. Biomedicines, 11.","DOI":"10.3390\/biomedicines11041067"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.tins.2011.05.006","article-title":"Clarifying lysosomal storage diseases","volume":"34","author":"Schultz","year":"2011","journal-title":"Trends Neurosci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1111\/brv.12521","article-title":"Brain iron transport","volume":"94","author":"Qian","year":"2019","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"ref_34","first-page":"19","article-title":"Divalent metal transporter 1 (DMT1) in the brain: Implications for a role in iron transport at the blood-brain barrier, and neuronal and glial pathology","volume":"8","author":"Burkhart","year":"2015","journal-title":"Front. Mol. Neurosci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1021\/acschemneuro.8b00390","article-title":"Iron Dysregulation in Parkinson\u2019s Disease: Focused on the Autophagy\u2013Lysosome Pathway","volume":"10","author":"Chen","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"e51031","DOI":"10.7554\/eLife.51031","article-title":"Impaired lysosomal acidification triggers iron deficiency and inflammation in vivo","volume":"8","author":"Yambire","year":"2019","journal-title":"Elife"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.tibs.2021.07.003","article-title":"The lysosome as a master regulator of iron metabolism","volume":"46","author":"Rizzollo","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Clark, L.N., Chan, R., Cheng, R., Liu, X., Park, N., Parmalee, N., Kisselev, S., Cortes, E., Torres, P.A., and Pastores, G.M. (2015). Gene-wise association of variants in four lysosomal storage disorder genes in neuropathologically confirmed Lewy body disease. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0125204"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1111\/jnc.14462","article-title":"Current concepts in the neuropathogenesis of mucolipidosis type IV","volume":"148","author":"Boudewyn","year":"2019","journal-title":"J. Neurochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1111\/jnc.13040","article-title":"Molecular mechanisms of non-transferrin-bound and transferring-bound iron uptake in primary hippocampal neurons","volume":"133","author":"Ji","year":"2015","journal-title":"J. Neurochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.tibs.2015.11.012","article-title":"Regulators of Iron Homeostasis: New Players in Metabolism, Cell Death, and Disease","volume":"41","author":"Bogdan","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Pasquadibisceglie, A., Bonaccorsi di Patti, M.C., Musci, G., and Polticelli, F. (2023). Membrane Transporters Involved in Iron Trafficking: Physiological and Pathological Aspects. Biomolecules, 13.","DOI":"10.3390\/biom13081172"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2258","DOI":"10.1073\/pnas.80.8.2258","article-title":"pH and the recycling of transferrin during receptor-mediated endocytosis","volume":"80","author":"Ciechanover","year":"1983","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1038\/embor.2013.168","article-title":"Loss of iron triggers PINK1\/Parkin-independent mitophagy","volume":"14","author":"Allen","year":"2013","journal-title":"EMBO Rep."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Wu, H., Wei, H., Zhang, D., Sehgal, S.A., Zhang, D., Wang, X., Qin, Y., Liu, L., and Chen, Q. (2020). Defective mitochondrial ISCs biogenesis switches on IRP1 to fine tune selective mitophagy. Redox Biol., 36.","DOI":"10.1016\/j.redox.2020.101661"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Bou-Abdallah, F., Paliakkara, J.J., Melman, G., and Melman, A. (2018). Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication. Pharmaceuticals, 11.","DOI":"10.3390\/ph11040120"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.freeradbiomed.2018.09.041","article-title":"Ascorbate and ferritin interactions: Consequences for iron release in vitro and in vivo and implications for inflammation","volume":"133","author":"Naftalin","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.ceca.2017.06.006","article-title":"TRPML1: The Ca(2+)retaker of the lysosome","volume":"69","author":"Medina","year":"2018","journal-title":"Cell Calcium"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"107719","DOI":"10.1016\/j.celrep.2020.107719","article-title":"Depletion of the AD Risk Gene SORL1 Selectively Impairs Neuronal Endosomal Traffic Independent of Amyloidogenic APP Processing","volume":"31","author":"Knupp","year":"2020","journal-title":"Cell Rep."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"109259","DOI":"10.1016\/j.celrep.2021.109259","article-title":"SORL1 deficiency in human excitatory neurons causes APP-dependent defects in the endolysosome-autophagy network","volume":"35","author":"Hung","year":"2021","journal-title":"Cell Rep."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1186\/s13041-020-00681-7","article-title":"Brain transcriptome analysis reveals subtle effects on mitochondrial function and iron homeostasis of mutations in the SORL1 gene implicated in early onset familial Alzheimer\u2019s disease","volume":"13","author":"Barthelson","year":"2020","journal-title":"Mol. Brain."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1007\/s00018-022-04182-9","article-title":"The Alzheimer\u2019s gene SORL1 is a regulator of endosomal traffic and recycling in human neurons","volume":"79","author":"Mishra","year":"2022","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"135944","DOI":"10.1016\/j.neulet.2021.135944","article-title":"Progress in elucidating pathophysiology of mucolipidosis IV","volume":"755","author":"Misko","year":"2021","journal-title":"Neurosci. Lett."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2155","DOI":"10.1007\/s11011-021-00742-3","article-title":"White matter abnormalities and iron deposition in prenatal mucolipidosis IV\u2014Fetal imaging and pathology","volume":"36","author":"Zerem","year":"2021","journal-title":"Metab. Brain Dis."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1212\/WNL.51.2.565","article-title":"Mucolipidosis type IV: Characteristic MRI findings","volume":"51","author":"Frei","year":"1998","journal-title":"Neurology"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1073\/pnas.95.3.1207","article-title":"Constitutive achlorhydria in mucolipidosis type IV","volume":"95","author":"Schiffmann","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1097\/00000478-199912000-00010","article-title":"Lysosomal inclusions in gastric parietal cells in mucolipidosis type IV: A novel cause of achlorhydria and hypergastrinemia","volume":"23","author":"Lubensky","year":"1999","journal-title":"Am. J. Surg. Pathol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/j.bbadis.2007.01.004","article-title":"TRPML and lysosomal function","volume":"1772","author":"Zeevi","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"32040","DOI":"10.1074\/jbc.M109.037184","article-title":"Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis","volume":"284","author":"Dong","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_60","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_61","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1093\/hmg\/ddh067","article-title":"Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel","volume":"13","author":"Raychowdhury","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0009-8981(98)00183-1","article-title":"Elevated lysosomal pH in Mucolipidosis type IV cells","volume":"280","author":"Bach","year":"1999","journal-title":"Clin. Chim. Acta"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"7294","DOI":"10.1074\/jbc.M508211200","article-title":"TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity","volume":"281","author":"Soyombo","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1203\/PDR.0b013e3181a1681a","article-title":"Mucolipidosis type IV: The effect of increased lysosomal pH on the abnormal lysosomal storage","volume":"65","author":"Zeigler","year":"2009","journal-title":"Pediatr. Res."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Folts, C.J., Scott-Hewitt, N., Pr\u00f6schel, C., Mayer-Pr\u00f6schel, M., and Noble, M. (2016). Lysosomal Re-acidification Prevents Lysosphingolipid-Induced Lysosomal Impairment and Cellular Toxicity. PLoS Biol., 14.","DOI":"10.1371\/journal.pbio.1002583"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Kuk, M.U., Lee, Y.H., Kim, J.W., Hwang, S.Y., Park, J.T., and Park, S.C. (2021). Potential Treatment of Lysosomal Storage Disease through Modulation of the Mitochondrial\u2014Lysosomal Axis. Cells, 10.","DOI":"10.3390\/cells10020420"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"35283","DOI":"10.1074\/jbc.M111.267930","article-title":"Lysosomal storage causes cellular dysfunction in mucolipidosis II skin fibroblasts","volume":"286","author":"Otomo","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"19266","DOI":"10.1073\/pnas.2003236117","article-title":"Mitochondria-lysosome contacts regulate mitochondrial Ca2+ dynamics via lysosomal TRPML1","volume":"117","author":"Peng","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1042\/BJ20130647","article-title":"Loss of TRPML1 promotes production of reactive oxygen species: Is oxidative damage a factor in mucolipidosis type IV?","volume":"457","author":"Coblentz","year":"2014","journal-title":"Biochem. J."},{"key":"ref_70","first-page":"1591","article-title":"Impaired myelination and reduced brain ferric iron in the mouse model of mucolipidosis IV","volume":"8","author":"Grishchuk","year":"2015","journal-title":"Dis. Model Mech."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"dmm044230","DOI":"10.1242\/dmm.044230","article-title":"Early evidence of delayed oligodendrocyte maturation in the mouse model of mucolipidosis type IV","volume":"13","author":"Mepyans","year":"2020","journal-title":"Dis. Model Mech."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1002\/jnr.490260415","article-title":"Iron-enriched oligodendrocytes: A reexamination of their spatial distribution","volume":"26","author":"LeVine","year":"1990","journal-title":"J. Neurosci. Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1002\/jnr.490290317","article-title":"Oligodendrocytes and myelin sheaths in normal, quaking and shiverer brains are enriched in iron","volume":"29","author":"LeVine","year":"1991","journal-title":"J. Neurosci. Res."},{"key":"ref_74","first-page":"913","article-title":"Effects of low-iron status and deficiency of essential fatty acids on some biochemical constituents of rat brain","volume":"27","author":"Oloyede","year":"1992","journal-title":"Biochem. Int."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3389\/neuro.05.005.2009","article-title":"Oligodendrocyte development and the onset of myelination in the human fetal brain","volume":"3","author":"Jakovcevski","year":"2009","journal-title":"Front. Neuroanat."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1038\/s41593-021-00917-2","article-title":"Periods of synchronized myelin changes shape brain function and plasticity","volume":"24","author":"Pivonkova","year":"2021","journal-title":"Nat. Neurosci."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1038\/nm.1876","article-title":"Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium","volume":"14","author":"Morgan","year":"2008","journal-title":"Nat. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s10545-014-9794-4","article-title":"Complex lipid trafficking in Niemann-Pick disease type C","volume":"38","author":"Vanier","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.nbd.2013.12.018","article-title":"The autophagic defect in Niemann-Pick disease type C neurons differs from somatic cells and reduces neuronal viability","volume":"64","author":"Meske","year":"2014","journal-title":"Neurobiol. Dis."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Liedtke, M., V\u00f6lkner, C., Hermann, A., and Frech, M.J. (2022). Impact of Organelle Transport Deficits on Mitophagy and Autophagy in Niemann-Pick Disease Type C. Cells, 11.","DOI":"10.3390\/cells11030507"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1016\/S0960-9822(03)00531-1","article-title":"Cholesterol accumulation in NPC1-deficient neurons is ganglioside dependent","volume":"13","author":"McGlynn","year":"2003","journal-title":"Curr. Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.brainres.2016.11.031","article-title":"Diversity of glycosphingolipid GM2 and cholesterol accumulation in NPC1 patient-specific iPSC-derived neurons","volume":"1657","author":"Trilck","year":"2017","journal-title":"Brain Res."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.nbd.2009.01.015","article-title":"Critical role of iron in the pathogenesis of the murine gangliosidoses","volume":"34","author":"Jeyakumar","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"768","DOI":"10.3174\/ajnr.A7894","article-title":"Investigation of Brain Iron in Niemann-Pick Type C: A 7T Quantitative Susceptibility Mapping Study","volume":"44","author":"Ravanfar","year":"2023","journal-title":"AJNR Am. J. Neuroradiol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1039\/C3MT00308F","article-title":"Altered transition metal homeostasis in Niemann-Pick disease, type C1","volume":"6","author":"Hung","year":"2014","journal-title":"Metallomics"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s10534-020-00233-5","article-title":"Iron chelation by deferiprone does not rescue the Niemann-Pick Disease Type C1 mouse model","volume":"33","author":"Hung","year":"2020","journal-title":"Biometals"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Martins, T.S., Costa, R.S., Vila\u00e7a, R., Lemos, C., Teixeira, V., Pereira, C., and Costa, V. (2023). Iron Limitation Restores Autophagy and Increases Lifespan in the Yeast Model of Niemann-Pick Type C1. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24076221"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1006\/mgme.2000.3004","article-title":"Deficient ferritin immunoreactivity in tissues from niemann-pick type C patients: Extension of findings to fetal tissues, H and L ferritin isoforms, but also one case of the rare Niemann-Pick C2 complementation group","volume":"70","author":"Christomanou","year":"2000","journal-title":"Mol. Genet. Metab."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Liang, L., Wang, H., Yao, J., Wei, Q., Lu, Y., Wang, T., and Cao, X. (2022). NPC1 Deficiency Contributes to Autophagy-Dependent Ferritinophagy in HEI-OC1 Auditory Cells. Front. Mol. Biosci., 9.","DOI":"10.3389\/fmolb.2022.952608"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"4924","DOI":"10.1073\/pnas.95.9.4924","article-title":"Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins","volume":"95","author":"Iwai","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Santana-Codina, N., and Mancias, J.D. (2018). The Role of NCOA4-Mediated Ferritinophagy in Health and Disease. Pharmaceuticals, 11.","DOI":"10.20944\/preprints201809.0148.v1"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"C445","DOI":"10.1152\/ajpcell.00505.2005","article-title":"Release of iron from ferritin requires lysosomal activity","volume":"291","author":"Kidane","year":"2006","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"267","DOI":"10.12688\/wellcomeopenres.17261.2","article-title":"Defective iron homeostasis and hematological abnormalities in Niemann-Pick disease type C1","volume":"7","author":"Chen","year":"2023","journal-title":"Wellcome Open Res."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e1238","DOI":"10.1097\/MPH.0000000000002135","article-title":"Unexpected Cause of Persistent Microcytosis and Neurological Symptoms in a Child: Niemann-Pick Disease Type C","volume":"43","year":"2021","journal-title":"J. Pediatr. Hematol. Oncol."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Bernardo, A., De Nuccio, C., Visentin, S., Martire, A., Minghetti, L., Popoli, P., and Ferrante, A. (2021). Myelin Defects in Niemann-Pick Type C Disease: Mechanisms and Possible Therapeutic Perspectives. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22168858"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Kanninen, K.M., Grubman, A., Meyerowitz, J., Duncan, C., Tan, J.-L., Parker, S.J., Crouch, P.J., Paterson, B.M., Hickey, J.L., and Donnelly, P.S. (2013). Increased zinc and manganese in parallel with neurodegeneration, synaptic protein changes and activation of Akt\/GSK3 signaling in ovine CLN6 neuronal ceroid lipofuscinosis. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0058644"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1039\/C4MT00032C","article-title":"Deregulation of biometal homeostasis: The missing link for neuronal ceroid lipofuscinoses?","volume":"6","author":"Grubman","year":"2014","journal-title":"Metallomics"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1039\/C6MT00055J","article-title":"X-ray fluorescence microscopic measurement of elemental distribution in the mouse retina with age","volume":"8","author":"Grubman","year":"2016","journal-title":"Metallomics"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"14612","DOI":"10.1038\/ncomms14612","article-title":"Misrouting of v-ATPase subunit V0a1 dysregulates lysosomal acidification in a neurodegenerative lysosomal storage disease model","volume":"8","author":"Bagh","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1111\/cge.13829","article-title":"Autosomal dominant neuronal ceroid lipofuscinosis: Clinical features and molecular basis","volume":"99","author":"Naseri","year":"2021","journal-title":"Clin. Genet."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/s41594-020-0375-y","article-title":"Aggregation of mutant cysteine string protein-\u03b1 via Fe\u2013S cluster binding is mitigated by iron chelators","volume":"27","author":"Naseri","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1080\/17474086.2016.1268047","article-title":"Mitochondria and Iron: Current questions","volume":"10","author":"Paul","year":"2017","journal-title":"Expert Rev. Hematol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.cmet.2006.02.003","article-title":"Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis","volume":"3","author":"Tong","year":"2006","journal-title":"Cell Metab."},{"key":"ref_104","unstructured":"Pastores, G.M., and Hughes, D.A. (1993). GeneReviews\u00ae, University of Washington."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/s13024-019-0336-2","article-title":"Glucocerebrosidase and its relevance to Parkinson disease","volume":"14","author":"Do","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"23594","DOI":"10.1074\/jbc.M300212200","article-title":"Glucosylceramide and glucosylsphingosine modulate calcium mobilization from brain microsomes via different mechanisms","volume":"278","author":"Pelled","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.nbd.2004.09.004","article-title":"Enhanced calcium release in the acute neuronopathic form of Gaucher disease","volume":"18","author":"Pelled","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1093\/hmg\/ddp580","article-title":"Neuronopathic Gaucher disease in the mouse: Viable combined selective saposin C deficiency and mutant glucocerebrosidase (V394L) mice with glucosylsphingosine and glucosylceramide accumulation and progressive neurological deficits","volume":"19","author":"Sun","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1002\/sctm.20-0386","article-title":"Elevated glucosylsphingosine in Gaucher disease induced pluripotent stem cell neurons deregulates lysosomal compartment through mammalian target of rapamycin complex 1","volume":"10","author":"Srikanth","year":"2021","journal-title":"Stem Cells Transl. Med."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"114402","DOI":"10.1016\/j.addr.2022.114402","article-title":"Lysosomal functions and dysfunctions: Molecular and cellular mechanisms underlying Gaucher disease and its association with Parkinson disease","volume":"187","author":"Horowitz","year":"2022","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1007\/s00109-021-02174-z","article-title":"Gaucher disease\u2014More than just a rare lipid storage disease","volume":"100","author":"Roh","year":"2022","journal-title":"J. Mol. Med."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Hruska, K.S., Goker-Alpan, O., and Sidransky, E. (2006). Gaucher disease and the synucleinopathies. J. Biomed. Biotechnol., 2006.","DOI":"10.1155\/JBB\/2006\/78549"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Furderer, M.L., Hertz, E., Lopez, G.J., and Sidransky, E. (2022). Neuropathological Features of Gaucher Disease and Gaucher Disease with Parkinsonism. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23105842"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.cmet.2013.04.014","article-title":"Mitochondria and quality control defects in a mouse model of Gaucher disease--links to Parkinson\u2019s disease","volume":"17","author":"Osellame","year":"2013","journal-title":"Cell Metab."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"9617","DOI":"10.1523\/JNEUROSCI.1525-17.2017","article-title":"Glucosylsphingosine Promotes \u03b1-Synuclein Pathology in Mutant GBA-Associated Parkinson\u2019s Disease","volume":"37","author":"Taguchi","year":"2017","journal-title":"J. Neurosci."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1931","DOI":"10.1073\/pnas.1520335113","article-title":"\u03b1-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain-synucleinopathy models","volume":"113","author":"Mazzulli","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1002\/mds.26802","article-title":"Lysosomal trafficking defects link Parkinson\u2019s disease with Gaucher\u2019s disease","volume":"31","author":"Wong","year":"2016","journal-title":"Mov. Disord."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"44284","DOI":"10.1074\/jbc.M105343200","article-title":"Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson\u2019s disease and heavy metal exposure","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"16116","DOI":"10.1074\/jbc.M107866200","article-title":"Magnesium inhibits spontaneous and iron-induced aggregation of \u03b1-synuclein","volume":"277","author":"Golts","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.bbrc.2007.05.060","article-title":"Thermodynamics imprinting reveals differential binding of metals to \u03b1-synuclein: Relevance to Parkinson\u2019s disease","volume":"359","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.jinorgbio.2009.11.005","article-title":"Binding of \u03b1-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes","volume":"104","author":"Peng","year":"2010","journal-title":"J. Inorg. Biochem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1111\/j.1471-4159.1991.tb08170.x","article-title":"Iron and aluminum increase in the substantia nigra of patients with Parkinson\u2019s disease: An X-ray microanalysis","volume":"56","author":"Hirsch","year":"1991","journal-title":"J. Neurochem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s004010050001","article-title":"Sequestration of iron by Lewy bodies in Parkinson\u2019s disease","volume":"100","author":"Castellani","year":"2000","journal-title":"Acta Neuropathol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.freeradbiomed.2019.06.024","article-title":"Interactions between iron and \u03b1-synuclein pathology in Parkinson\u2019s disease","volume":"141","author":"Chen","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1186\/s13024-017-0218-4","article-title":"Iron regulatory protein (IRP)-iron responsive element (IRE) signaling pathway in human neurodegenerative diseases","volume":"12","author":"Zhou","year":"2017","journal-title":"Mol. Neurodegener."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"10903","DOI":"10.1038\/srep10903","article-title":"Pharmacological Chaperones and Coenzyme Q10 Treatment Improves Mutant \u03b2-Glucocerebrosidase Activity and Mitochondrial Function in Neuronopathic Forms of Gaucher Disease","volume":"5","author":"Cordero","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.ymgmr.2014.04.006","article-title":"Clinical variability in neurohepatic syndrome due to combined mitochondrial DNA depletion and Gaucher disease","volume":"1","author":"Harvengt","year":"2014","journal-title":"Mol. Genet. Metab. Rep."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1007\/s10545-017-0048-0","article-title":"Linking mitochondrial dysfunction to neurodegeneration in lysosomal storage diseases","volume":"40","author":"Saffari","year":"2017","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"6640","DOI":"10.1093\/hmg\/ddv369","article-title":"Glucocerebrosidase 1 deficient Danio rerio mirror key pathological aspects of human Gaucher disease and provide evidence of early microglial activation preceding alpha-synuclein-independent neuronal cell death","volume":"24","author":"Keatinge","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/BF02537346","article-title":"Inhibition of cytochrome c oxidase and hemolysis caused by lysosphingolipids","volume":"23","author":"Igisu","year":"1988","journal-title":"Lipids"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1203\/00006450-200008000-00009","article-title":"Perinatal iron deficiency decreases cytochrome c oxidase (CytOx) activity in selected regions of neonatal rat brain","volume":"48","author":"Rao","year":"2000","journal-title":"Pediatr. Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.ijcard.2018.02.021","article-title":"Iron deficiency without anemia is responsible for decreased left ventricular function and reduced mitochondrial complex I activity in a mouse model","volume":"266","author":"Rineau","year":"2018","journal-title":"Int. J. Cardiol."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Rineau, E., Gueguen, N., Procaccio, V., Genevi\u00e8ve, F., Reynier, P., Henrion, D., and Lasocki, S. (2021). Iron Deficiency without Anemia Decreases Physical Endurance and Mitochondrial Complex I Activity of Oxidative Skeletal Muscle in the Mouse. Nutrients, 13.","DOI":"10.3390\/nu13041056"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"616920","DOI":"10.3389\/fcvm.2020.616920","article-title":"Iron-deficiency anemia results in transcriptional and metabolic remodeling in the heart toward a glycolytic phenotype","volume":"7","author":"Chung","year":"2021","journal-title":"Front. Cardiovasc. Med."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1002\/ajh.21721","article-title":"Hyperferritinemia and iron overload in type 1 Gaucher disease","volume":"85","author":"Stein","year":"2010","journal-title":"Am. J. Hematol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.bcmd.2012.04.002","article-title":"Ferritinemia during type 1 Gaucher disease: Mechanisms and progression under treatment","volume":"49","author":"Mekinian","year":"2012","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"587","DOI":"10.3324\/haematol.2017.177816","article-title":"Involvement of hepcidin in iron metabolism dysregulation in Gaucher disease","volume":"103","author":"Lefebvre","year":"2018","journal-title":"Haematologica"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.bcmd.2016.10.010","article-title":"Ferritinemia and serum inflammatory cytokines in Swedish adults with Gaucher disease type 1","volume":"68","author":"Lorenz","year":"2018","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.ymgme.2004.04.011","article-title":"Neuropathology provides clues to the pathophysiology of Gaucher disease","volume":"82","author":"Wong","year":"2004","journal-title":"Mol. Genet. Metab."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1097\/MPG.0000000000000206","article-title":"Iron requirements of infants and toddlers","volume":"58","author":"Braegger","year":"2014","journal-title":"J. Pediatr. Gastroenterol. Nutr."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1468S","DOI":"10.1093\/jn\/133.5.1468S","article-title":"Iron deficiency alters brain development and functioning","volume":"133","author":"Beard","year":"2003","journal-title":"J. Nutr."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"2534","DOI":"10.1093\/jn\/138.12.2534","article-title":"Why iron deficiency is important in infant development","volume":"138","author":"Beard","year":"2008","journal-title":"J. Nutr."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1159\/000075667","article-title":"Perinatal iron deficiency alters apical dendritic growth in hippocampal CA1 pyramidal neurons","volume":"25","author":"Jorgenson","year":"2003","journal-title":"Dev. Neurosci."},{"key":"ref_144","first-page":"e18138","article-title":"Iron Deficiency-Induced Changes in the Hippocampus, Corpus Striatum, and Monoamines Levels That Lead to Anxiety, Depression, Sleep Disorders, and Psychotic Disorders","volume":"13","author":"Shah","year":"2021","journal-title":"Cureus"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1111\/j.1365-2141.1975.tb00851.x","article-title":"Brain iron: Persistent deficiency following short-term iron deprivation in the young rat","volume":"31","author":"Dallman","year":"1975","journal-title":"Br. J. Haematol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"2030","DOI":"10.1093\/jn\/127.10.2030","article-title":"Regional brain iron, ferritin and transferrin concentrations during iron deficiency and iron repletion in developing rats","volume":"127","author":"Erikson","year":"1997","journal-title":"J. Nutr."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1089\/thy.2015.0293","article-title":"Perinatal Iron Deficiency-Induced Hypothyroxinemia Impairs Early Brain Development Regardless of Normal Iron Levels in the Neonatal Brain","volume":"26","author":"Hu","year":"2016","journal-title":"Thyroid"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1159\/000521704","article-title":"Developmental Iron Deficiency Dysregulates TET Activity and DNA Hydroxymethylation in the Rat Hippocampus and Cerebellum","volume":"44","author":"Barks","year":"2022","journal-title":"Dev. Neurosci."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.freeradbiomed.2021.01.026","article-title":"Epigenomic regulation by labile iron","volume":"170","author":"Camarena","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Lien, Y.-C., Condon, D.E., Georgieff, M.K., Simmons, R.A., and Tran, P.V. (2019). Dysregulation of Neuronal Genes by Fetal-Neonatal Iron Deficiency Anemia Is Associated with Altered DNA Methylation in the Rat Hippocampus. Nutrients, 11.","DOI":"10.3390\/nu11051191"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.clinbiochem.2016.11.014","article-title":"The modulation of inflammatory parameters, Brain-derived neurotrophic factor levels and global histone H4 acetylation status in peripheral blood of patients with Gaucher disease type 1","volume":"50","author":"Reinaldo","year":"2017","journal-title":"Clin. Biochem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1007\/s10545-012-9460-7","article-title":"The cognitive profile of type 1 Gaucher disease patients","volume":"35","author":"Biegstraaten","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Tullo, M.G., Cerulli Irelli, E., Caramia, F., Tessari, G., Di Bonaventura, C., Turchetta, R., Giallonardo, A.T., Palumbo, G., Bianchi, S., and Atturo, F. (2023). The Spectrum of Neurological and Sensory Abnormalities in Gaucher Disease Patients: A Multidisciplinary Study (SENOPRO). Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24108844"},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Liu, S.X., Barks, A.K., Lunos, S., Gewirtz, J.C., Georgieff, M.K., and Tran, P.V. (2021). Prenatal Iron Deficiency and Choline Supplementation Interact to Epigenetically Regulate Jarid1b and Bdnf in the Rat Hippocampus into Adulthood. Nutrients, 13.","DOI":"10.3390\/nu13124527"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"122","DOI":"10.3389\/fncel.2016.00122","article-title":"New Insights into Reelin-Mediated Signaling Pathways","volume":"10","author":"Lee","year":"2016","journal-title":"Front. Cell. Neurosci."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Colucci-D\u2019Amato, L., Speranza, L., and Volpicelli, F. (2020). Neurotrophic Factor BDNF, Physiological Functions and Therapeutic Potential in Depression, Neurodegeneration and Brain Cancer. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21207777"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Jossin, Y. (2020). Reelin Functions, Mechanisms of Action and Signaling Pathways During Brain Development and Maturation. Biomolecules, 10.","DOI":"10.3390\/biom10060964"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/s40035-022-00279-0","article-title":"Brain-derived neurotrophic factor in Alzheimer\u2019s disease and its pharmaceutical potential","volume":"11","author":"Gao","year":"2022","journal-title":"Transl. Neurodegener."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1023\/A:1022436928925","article-title":"Twenty five years of the \u201cpsychosine hypothesis\u201d: A personal perspective of its history and present status","volume":"23","author":"Suzuki","year":"1998","journal-title":"Neurochem. Res."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"e1529","DOI":"10.1038\/cddis.2014.483","article-title":"Role of extracellular calcium and mitochondrial oxygen species in psychosine-induced oligodendrocyte cell death","volume":"5","author":"Voccoli","year":"2014","journal-title":"Cell Death Dis."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1111\/j.1750-3639.1995.tb00601.x","article-title":"The twitcher mouse: A model for Krabbe disease and for experimental therapies","volume":"5","author":"Suzuki","year":"1995","journal-title":"Brain Pathol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1002\/path.4328","article-title":"Neuronal inclusions of \u03b1-synuclein contribute to the pathogenesis of Krabbe disease","volume":"232","author":"Smith","year":"2014","journal-title":"J. Pathol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1093\/brain\/awac002","article-title":"Prion-like \u03b1-synuclein pathology in the brain of infants with Krabbe disease","volume":"145","author":"Hatton","year":"2022","journal-title":"Brain"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1038\/ng.3955","article-title":"A.; Ayalon, G.; et al. A meta-analysis of genome-wide association studies identifies 17 new Parkinson\u2019s disease risk loci","volume":"49","author":"Chang","year":"2017","journal-title":"Nat. Genet."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"e1724","DOI":"10.1002\/wrna.1724","article-title":"The Quaking RNA-binding proteins as regulators of cell differentiation","volume":"13","author":"Neumann","year":"2022","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/0006-8993(92)91018-A","article-title":"Morphological features of degenerating oligodendrocytes in twitcher mice","volume":"587","author":"LeVine","year":"1992","journal-title":"Brain Res."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1111\/j.1365-2990.1980.tb00219.x","article-title":"Myelination of the mouse corpus callosum","volume":"6","author":"Sturrock","year":"1980","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Lin, D.-S., Ho, C.-S., Huang, Y.-W., Wu, T.-Y., Lee, T.-H., Huang, Z.-D., Wang, T.-J., Yang, S.-J., and Chiang, M.-F. (2020). Impairment of Proteasome and Autophagy Underlying the Pathogenesis of Leukodystrophy. Cells, 9.","DOI":"10.3390\/cells9051124"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Vantaggiato, L., Shaba, E., Carleo, A., Bezzini, D., Pannuzzo, G., Luddi, A., Piomboni, P., Bini, L., and Bianchi, L. (2022). Neurodegenerative Disorder Risk in Krabbe Disease Carriers. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232113537"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1042\/bj2900139","article-title":"Kinetics of inhibition of purified and mitochondrial cytochrome c oxidase by psychosine (\u03b2-galactosylsphingosine)","volume":"290","author":"Cooper","year":"1993","journal-title":"Biochem. J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.arr.2016.05.004","article-title":"Disorders of lysosomal acidification\u2014The emerging role of v-ATPase in aging and neurodegenerative disease","volume":"32","author":"Colacurcio","year":"2016","journal-title":"Ageing. Res. Rev."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"E6640","DOI":"10.1073\/pnas.1801612115","article-title":"Amyloid clearance defect in ApoE4 astrocytes is reversed by epigenetic correction of endosomal pH","volume":"115","author":"Prasad","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"5255","DOI":"10.1523\/JNEUROSCI.0578-19.2019","article-title":"Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-\u03b2CTF (C99)","volume":"39","author":"Jiang","year":"2019","journal-title":"J. Neurosci."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1007\/s12035-022-02863-x","article-title":"The amyloid precursor protein: A converging point in Alzheimer\u2019s disease","volume":"59","author":"Delport","year":"2022","journal-title":"Mol. Neurobiol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1016\/j.cell.2010.05.008","article-title":"Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations","volume":"141","author":"Lee","year":"2010","journal-title":"Cell"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1016\/j.celrep.2015.07.050","article-title":"Presenilin 1 Maintains Lysosomal Ca2+ Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification","volume":"12","author":"Lee","year":"2015","journal-title":"Cell Rep."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"533","DOI":"10.3389\/fnins.2018.00533","article-title":"Dysregulation of Neuronal Iron Homeostasis as an Alternative Unifying Effect of Mutations Causing Familial Alzheimer\u2019s Disease","volume":"12","author":"Lumsden","year":"2018","journal-title":"Front. Neurosci."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1111\/jnc.13935","article-title":"Endo-lysosomal and autophagic dysfunction: A driving factor in Alzheimer\u2019s disease?","volume":"140","author":"Whyte","year":"2017","journal-title":"J. Neurochem."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.tins.2017.01.002","article-title":"Mitophagy and Alzheimer\u2019s Disease: Cellular and Molecular Mechanisms","volume":"40","author":"Kerr","year":"2017","journal-title":"Trends Neurosci."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.redox.2017.08.015","article-title":"Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis","volume":"14","author":"Masaldan","year":"2018","journal-title":"Redox Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"983623","DOI":"10.3389\/fphar.2022.983623","article-title":"Iron dyshomeostasis and ferroptosis in Alzheimer\u2019s disease: Molecular mechanisms of cell death and novel therapeutic drugs and targets for AD","volume":"13","author":"Zhang","year":"2022","journal-title":"Front. Pharmacol."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Pergande, M.R., Cougnoux, A., Rathnayake, R.A.C., Porter, F.D., and Cologna, S.M. (2019). Differential Proteomics Reveals miR-155 as a Novel Indicator of Liver and Spleen Pathology in the Symptomatic Niemann-Pick Disease, Type C1 Mouse Model. Molecules, 24.","DOI":"10.3390\/molecules24050994"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"11153","DOI":"10.1073\/pnas.0404349101","article-title":"A role for heme in Alzheimer\u2019s disease: Heme binds amyloid beta and has altered metabolism","volume":"101","author":"Atamna","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_184","doi-asserted-by":"crossref","unstructured":"Dwyer, B.E., Stone, M.L., Zhu, X., Perry, G., and Smith, M.A. (2006). Heme deficiency in Alzheimer\u2019s disease: A possible connection to porphyria. J. Biomed. Biotechnol., 2006.","DOI":"10.1155\/JBB\/2006\/24038"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1002\/prot.25075","article-title":"Fe2+ binding on amyloid \u03b2-peptide promotes aggregation","volume":"84","author":"Boopathi","year":"2016","journal-title":"Proteins"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"276","DOI":"10.3389\/fnmol.2018.00276","article-title":"Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration","volume":"11","author":"Rao","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.stemcr.2015.07.002","article-title":"Alpha-Synuclein Expression in the Oligodendrocyte Lineage: An In Vitro and In Vivo Study Using Rodent and Human Models","volume":"5","author":"Djelloul","year":"2015","journal-title":"Stem Cell Rep."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.tins.2022.11.007","article-title":"\u03b1-Synuclein in synaptic function and dysfunction","volume":"46","author":"Sharma","year":"2023","journal-title":"Trends Neurosci."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"3965","DOI":"10.1002\/alz.13088","article-title":"Associations of blood cell indices and anemia with risk of incident dementia: A prospective cohort study of 313,448 participants","volume":"19","author":"Qiang","year":"2023","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"2633105520935104","DOI":"10.1177\/2633105520935104","article-title":"The Effects of Early-Life Iron Deficiency on Brain Energy Metabolism","volume":"15","author":"Bastian","year":"2020","journal-title":"Neurosci. Insights"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1021\/acschemneuro.8b00194","article-title":"Increased Iron Deposition on Brain Quantitative Susceptibility Mapping Correlates with Decreased Cognitive Function in Alzheimer\u2019s Disease","volume":"9","author":"Du","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1093\/brain\/awaa089","article-title":"Relationship between cortical iron and tau aggregation in Alzheimer\u2019s disease","volume":"143","author":"Spotorno","year":"2020","journal-title":"Brain"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1148\/radiol.2020192541","article-title":"Cross-sectional and Longitudinal Assessment of Brain Iron Level in Alzheimer Disease Using 3-T MRI","volume":"296","author":"Damulina","year":"2020","journal-title":"Radiology"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.21037\/qims-22-7","article-title":"Associations of cortical iron accumulation with cognition and cerebral atrophy in Alzheimer\u2019s disease","volume":"12","author":"Yang","year":"2022","journal-title":"Quant. Imaging Med. Surg."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"3072","DOI":"10.1002\/hbm.26263","article-title":"Magnetic resonance evidence of increased iron content in subcortical brain regions in asymptomatic Alzheimer\u2019s disease","volume":"44","author":"Lin","year":"2023","journal-title":"Hum. Brain Mapp."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1042\/BST0361267","article-title":"The role of iron in neurodevelopment: Fetal iron deficiency and the developing hippocampus","volume":"36","author":"Georgieff","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1002\/ejhf.1154","article-title":"Iron deficiency impairs contractility of human cardiomyocytes through decreased mitochondrial function","volume":"20","author":"Hoes","year":"2018","journal-title":"Eur. J. Heart Fail."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1111\/bpa.12402","article-title":"Alzheimer\u2019s Disease: From Mitochondrial Perturbations to Mitochondrial Medicine","volume":"26","author":"Cardoso","year":"2016","journal-title":"Brain Pathol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1111\/bph.14585","article-title":"Mitochondrial dysfunction in Alzheimer\u2019s disease: Role in pathogenesis and novel therapeutic opportunities","volume":"176","author":"Swerdlow","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1203\/PDR.0b013e31819d90a1","article-title":"Long-term reduction of hippocampal brain-derived neurotrophic factor activity after fetal-neonatal iron deficiency in adult rats","volume":"65","author":"Tran","year":"2009","journal-title":"Pediatr. Res."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1159\/000314341","article-title":"Gestational and neonatal iron deficiency alters apical dendrite structure of CA1 pyramidal neurons in adult rat hippocampus","volume":"32","author":"Brunette","year":"2010","journal-title":"Dev. Neurosci."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1093\/jn\/nxz237","article-title":"Postweaning Iron Deficiency in Male Rats Leads to Long-Term Hyperactivity and Decreased Reelin Gene Expression in the Nucleus Accumbens","volume":"150","author":"Nishikura","year":"2020","journal-title":"J. Nutr."},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Barks, A.K., Liu, S.X., Georgieff, M.K., Hallstrom, T.C., and Tran, P.V. (2021). Early-Life Iron Deficiency Anemia Programs the Hippocampal Epigenomic Landscape. Nutrients, 13.","DOI":"10.3390\/nu13113857"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/B978-0-444-64150-2.00009-5","article-title":"Critical periods of brain development","volume":"173","author":"Voss","year":"2020","journal-title":"Handb. Clin. Neurol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"13382","DOI":"10.1074\/jbc.M110.213785","article-title":"Iron mediates N-methyl-D-aspartate receptor-dependent stimulation of calcium-induced pathways and hippocampal synaptic plasticity","volume":"286","author":"Humeres","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1007\/s10534-012-9550-x","article-title":"Iron deficiency on neuronal function","volume":"25","author":"Humeres","year":"2012","journal-title":"Biometals"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1098\/rstb.2003.1276","article-title":"Neurobiology and cellular pathogenesis of glycolipid storage diseases","volume":"358","author":"Walkley","year":"2003","journal-title":"Philos. Trans. R. Soc. B"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1016\/j.nbd.2006.03.009","article-title":"Multivariate neurocognitive and emotional profile of a mannosidosis murine model for therapy assessment","volume":"23","author":"Caeyenberghs","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.bbr.2011.03.059","article-title":"Telencephalic histopathology and changes in behavioural and neural plasticity in a murine model for metachromatic leukodystrophy","volume":"222","author":"Faldini","year":"2011","journal-title":"Behav. Brain Res."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"735","DOI":"10.3389\/fnins.2019.00735","article-title":"Targeting the Synapse in Alzheimer\u2019s Disease","volume":"13","author":"Jackson","year":"2019","journal-title":"Front. Neurosci."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1515\/revneuro-2019-0058","article-title":"Synaptic plasticity in Alzheimer\u2019s disease and healthy aging","volume":"31","author":"Cardenas","year":"2020","journal-title":"Rev. Neurosci."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/B978-0-12-819410-2.00027-8","article-title":"Alzheimer disease and neuroplasticity","volume":"184","author":"Koch","year":"2022","journal-title":"Handb. Clin. Neurol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"118267","DOI":"10.1016\/j.neuroimage.2021.118267","article-title":"Investigation of the association between cerebral iron content and myelin content in normative aging using quantitative magnetic resonance neuroimaging","volume":"239","author":"Khattar","year":"2021","journal-title":"Neuroimage"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"C1117","DOI":"10.1152\/ajpcell.00444.2004","article-title":"Iron alters glutamate secretion by regulating cytosolic aconitase activity","volume":"288","author":"McGahan","year":"2005","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.3389\/fnins.2019.01443","article-title":"Iron Metabolism, Ferroptosis, and the Links with Alzheimer\u2019s Disease","volume":"13","author":"Yan","year":"2020","journal-title":"Front. Neurosci."},{"key":"ref_216","doi-asserted-by":"crossref","unstructured":"Chavoshinezhad, S., Beirami, E., Izadpanah, E., Feligioni, M., and Hassanzadeh, K. (2023). Molecular mechanism and potential therapeutic targets of necroptosis and ferroptosis in Alzheimer\u2019s disease. Biomed. Pharmacother., 168.","DOI":"10.1016\/j.biopha.2023.115656"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1038\/s41583-021-00535-8","article-title":"Energy matters: Presynaptic metabolism and the maintenance of synaptic transmission","volume":"23","author":"Li","year":"2022","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.mito.2023.09.003","article-title":"Understanding the neuronal synapse and challenges associated with the mitochondrial dysfunction in mild cognitive impairment and Alzheimer\u2019s disease","volume":"73","author":"Verma","year":"2023","journal-title":"Mitochondrion"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1146\/annurev-neuro-080317-061804","article-title":"Lysosomes and Brain Health","volume":"41","author":"Sharma","year":"2018","journal-title":"Annu. Rev. Neurosci."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/22\/2641\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:24:17Z","timestamp":1760131457000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/22\/2641"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11,16]]},"references-count":219,"journal-issue":{"issue":"22","published-online":{"date-parts":[[2023,11]]}},"alternative-id":["cells12222641"],"URL":"https:\/\/doi.org\/10.3390\/cells12222641","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,11,16]]}}}