{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T08:44:01Z","timestamp":1794300241896,"version":"4.9.0"},"reference-count":210,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2025,4,1]],"date-time":"2025-04-01T00:00:00Z","timestamp":1743465600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,4,1]],"date-time":"2025-04-01T00:00:00Z","timestamp":1743465600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,7]],"date-time":"2025-01-07T00:00:00Z","timestamp":1736208000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["R01NS115903"],"award-info":[{"award-number":["R01NS115903"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01AG065240"],"award-info":[{"award-number":["R01AG065240"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01AG076051"],"award-info":[{"award-number":["R01AG076051"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["RF1AG074346"],"award-info":[{"award-number":["RF1AG074346"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["neurotherapeuticsjournal.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neurotherapeutics"],"published-print":{"date-parts":[[2025,4]]},"DOI":"10.1016\/j.neurot.2025.e00525","type":"journal-article","created":{"date-parts":[[2025,1,18]],"date-time":"2025-01-18T09:59:58Z","timestamp":1737194398000},"page":"e00525","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":65,"title":["Mitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies"],"prefix":"10.1016","volume":"22","author":[{"given":"Kyle C.","family":"McGill Percy","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zunren","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin","family":"Qi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib1","doi-asserted-by":"crossref","first-page":"3708","DOI":"10.1002\/alz.13809","article-title":"2024 Alzheimer's disease facts and figures","volume":"20","year":"2024","journal-title":"Alzheimers Dement"},{"issue":"24","key":"10.1016\/j.neurot.2025.e00525_bib2","doi-asserted-by":"crossref","DOI":"10.3390\/molecules25245789","article-title":"Comprehensive review on Alzheimer's disease: causes and treatment","volume":"25","author":"Breijyeh","year":"2020","journal-title":"Molecules"},{"issue":"5580","key":"10.1016\/j.neurot.2025.e00525_bib3","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00525_bib4","article-title":"Tau post-translational modifications: dynamic transformers of tau function, degradation, and aggregation","volume":"11","author":"Alquezar","year":"2020","journal-title":"Front Neurol"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib5","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1186\/s13024-020-00376-6","article-title":"Mitochondria dysfunction in the pathogenesis of Alzheimer's disease: recent advances","volume":"15","author":"Wang","year":"2020","journal-title":"Mol Neurodegener"},{"issue":"43","key":"10.1016\/j.neurot.2025.e00525_bib6","doi-asserted-by":"crossref","first-page":"18670","DOI":"10.1073\/pnas.1006586107","article-title":"Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model","volume":"107","author":"Du","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"issue":"34","key":"10.1016\/j.neurot.2025.e00525_bib7","doi-asserted-by":"crossref","first-page":"14670","DOI":"10.1073\/pnas.0903563106","article-title":"Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease","volume":"106","author":"Yao","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib8","doi-asserted-by":"crossref","DOI":"10.3390\/antiox13020240","article-title":"Mitochondria dysfunction and neuroinflammation in neurodegeneration: who comes first?","volume":"13","author":"Peggion","year":"2024","journal-title":"Antioxidants"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib9","first-page":"R203","article-title":"Ratio of central nervous system to body metabolism in vertebrates: its constancy and functional basis","volume":"241","author":"Mink","year":"1981","journal-title":"Am J Physiol"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib10","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1097\/00004647-200110000-00001","article-title":"An energy budget for signaling in the grey matter of the brain","volume":"21","author":"Attwell","year":"2001","journal-title":"J\u00a0Cerebr Blood Flow Metabol"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib11","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1089\/ars.2011.4085","article-title":"Mitochondrial regulation of cell cycle and proliferation","volume":"16","author":"Antico Arciuch","year":"2012","journal-title":"Antioxidants Redox Signal"},{"issue":"11","key":"10.1016\/j.neurot.2025.e00525_bib12","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"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib13","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1124\/jpet.112.192138","article-title":"Mitochondrial dysfunction in neurodegenerative diseases","volume":"342","author":"Johri","year":"2012","journal-title":"J\u00a0Pharmacol Exp Therapeut"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib14","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.molcel.2015.02.008","article-title":"Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPR(mt)","volume":"58","author":"Nargund","year":"2015","journal-title":"Mol Cell"},{"key":"10.1016\/j.neurot.2025.e00525_bib15","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1146\/annurev-pathmechdis-012419-032711","article-title":"Mitochondrial dynamics and its involvement in disease","volume":"15","author":"Chan","year":"2020","journal-title":"Annu Rev Pathol"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib16","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/s41580-020-0210-7","article-title":"The cell biology of mitochondrial membrane dynamics","volume":"21","author":"Giacomello","year":"2020","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib17","doi-asserted-by":"crossref","first-page":"R170","DOI":"10.1016\/j.cub.2018.01.004","article-title":"Mitophagy and quality control mechanisms in mitochondrial maintenance","volume":"28","author":"Pickles","year":"2018","journal-title":"Curr Biol"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib18","doi-asserted-by":"crossref","DOI":"10.3390\/cells10123528","article-title":"Role of mitochondrial protein import in age-related neurodegenerative and cardiovascular diseases","volume":"10","author":"Bogorodskiy","year":"2021","journal-title":"Cells"},{"key":"10.1016\/j.neurot.2025.e00525_bib19","doi-asserted-by":"crossref","first-page":"568","DOI":"10.3389\/fncel.2019.00568","article-title":"Activation of mitochondrial unfolded protein response in SHSY5Y expressing APP cells and APP\/PS1 mice","volume":"13","author":"Shen","year":"2019","journal-title":"Front Cell Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib20","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2020.581849","article-title":"The mitochondrial unfolded protein response: a hinge between healthy and pathological aging","volume":"12","author":"Mu\u00f1oz-Carvajal","year":"2020","journal-title":"Front Aging Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib21","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2021.617588","article-title":"Mitochondrial dysfunction and oxidative stress in Alzheimer's disease","volume":"13","author":"Misrani","year":"2021","journal-title":"Front Aging Neurosci"},{"issue":"13","key":"10.1016\/j.neurot.2025.e00525_bib22","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23136954","article-title":"Role of impaired mitochondrial dynamics processes in the pathogenesis of Alzheimer's disease","volume":"23","author":"Blagov","year":"2022","journal-title":"Int J Mol Sci"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib23","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/s41380-022-01631-6","article-title":"Mitophagy in Alzheimer's disease: molecular defects and therapeutic approaches","volume":"28","author":"Mary","year":"2023","journal-title":"Mol Psychiatr"},{"issue":"31","key":"10.1016\/j.neurot.2025.e00525_bib24","doi-asserted-by":"crossref","first-page":"3474","DOI":"10.2174\/138161211798072517","article-title":"Targeting mitochondrial bioenergetics for Alzheimer's prevention and treatment","volume":"17","author":"Yao","year":"2011","journal-title":"Curr Pharmaceut Des"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib25","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1186\/s13024-021-00495-8","article-title":"Characterization of mitochondrial DNA quantity and quality in the human aged and Alzheimer's disease brain","volume":"16","author":"Klein","year":"2021","journal-title":"Mol Neurodegener"},{"key":"10.1016\/j.neurot.2025.e00525_bib26","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1146\/annurev-genom-082509-141720","article-title":"The mitochondrial proteome and human disease","volume":"11","author":"Calvo","year":"2010","journal-title":"Annu Rev Genom Hum Genet"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib27","doi-asserted-by":"crossref","DOI":"10.3390\/cells9010017","article-title":"Mitochondrial gene expression and beyond-novel aspects of cellular physiology","volume":"9","author":"Kotrys","year":"2019","journal-title":"Cells"},{"issue":"7604","key":"10.1016\/j.neurot.2025.e00525_bib28","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nature18015","article-title":"Synchronized mitochondrial and cytosolic translation programs","volume":"533","author":"Couvillion","year":"2016","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib29","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/s13059-022-02732-9","article-title":"Balanced mitochondrial and cytosolic translatomes underlie the biogenesis of human respiratory complexes","volume":"23","author":"Soto","year":"2022","journal-title":"Genome Biol"},{"key":"10.1016\/j.neurot.2025.e00525_bib30","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1146\/annurev.biochem.66.1.863","article-title":"Protein import into mitochondria","volume":"66","author":"Neupert","year":"1997","journal-title":"Annu Rev Biochem"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib31","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/s41580-018-0092-0","article-title":"Mitochondrial proteins: from biogenesis to functional networks","volume":"20","author":"Pfanner","year":"2019","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib32","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.cmet.2014.01.010","article-title":"The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease","volume":"19","author":"Harbauer","year":"2014","journal-title":"Cell Metabol"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib33","doi-asserted-by":"crossref","DOI":"10.3390\/ijms24032479","article-title":"The journey of mitochondrial protein import and the roadmap to follow","volume":"24","author":"Haastrup","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.neurot.2025.e00525_bib34","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.freeradbiomed.2021.11.015","article-title":"Mitochondrial chaperones in human health and disease","volume":"179","author":"Bahr","year":"2022","journal-title":"Free Radic Biol Med"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib35","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1083\/jcb.126.2.305","article-title":"Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria","volume":"126","author":"H\u00f6hfeld","year":"1994","journal-title":"J\u00a0Cell Biol"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib36","doi-asserted-by":"crossref","first-page":"606","DOI":"10.2174\/092986609788490159","article-title":"Heat shock protein 40: structural studies and their functional implications","volume":"16","author":"Li","year":"2009","journal-title":"Protein Pept Lett"},{"issue":"6300","key":"10.1016\/j.neurot.2025.e00525_bib37","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/348455a0","article-title":"The mitochondrial chaperonin hsp60 is required for its own assembly","volume":"348","author":"Cheng","year":"1990","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib38","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1007\/s00018-004-4464-6","article-title":"Hsp70 chaperones: cellular functions and molecular mechanism","volume":"62","author":"Mayer","year":"2005","journal-title":"Cell Mol Life Sci"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib39","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1038\/nrm3658","article-title":"Chaperone machines for protein folding, unfolding and disaggregation","volume":"14","author":"Saibil","year":"2013","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"9","key":"10.1016\/j.neurot.2025.e00525_bib40","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19092560","article-title":"The HSP90 family: structure, regulation, function, and implications in health and disease","volume":"19","author":"Hoter","year":"2018","journal-title":"Int J Mol Sci"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib41","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0167-4889(02)00264-1","article-title":"Molecular chaperones as essential mediators of mitochondrial biogenesis","volume":"1592","author":"Voos","year":"2002","journal-title":"Biochim Biophys Acta"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib42","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41556-022-01074-9","article-title":"Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space","volume":"25","author":"Adriaenssens","year":"2023","journal-title":"Nat Cell Biol"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib43","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1038\/s42003-021-02498-z","article-title":"Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix","volume":"4","author":"Matsushima","year":"2021","journal-title":"Commun Biol"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib44","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.drudis.2021.01.007","article-title":"Human ClpP protease, a promising therapy target for diseases of mitochondrial dysfunction","volume":"26","author":"Luo","year":"2021","journal-title":"Drug Discov Today"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102119","article-title":"Protease OMA1 modulates mitochondrial bioenergetics and ultrastructure through dynamic association with MICOS complex","volume":"24","author":"Viana","year":"2021","journal-title":"iScience"},{"issue":"19","key":"10.1016\/j.neurot.2025.e00525_bib46","doi-asserted-by":"crossref","first-page":"12681","DOI":"10.1074\/jbc.C800036200","article-title":"Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi","volume":"283","author":"Radke","year":"2008","journal-title":"J\u00a0Biol Chem"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib47","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1038\/cr.2018.17","article-title":"m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration","volume":"28","author":"Patron","year":"2018","journal-title":"Cell Res"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib48","doi-asserted-by":"crossref","DOI":"10.3390\/cells7100163","article-title":"AAA proteases: guardians of mitochondrial function and homeostasis","volume":"7","author":"Opali\u0144ska","year":"2018","journal-title":"Cells"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib49","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/nrm.2017.110","article-title":"The mitochondrial UPR: mechanisms, physiological functions and implications in ageing","volume":"19","author":"Shpilka","year":"2018","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"17","key":"10.1016\/j.neurot.2025.e00525_bib50","doi-asserted-by":"crossref","first-page":"4411","DOI":"10.1093\/emboj\/cdf445","article-title":"A\u00a0mitochondrial specific stress response in mammalian cells","volume":"21","author":"Zhao","year":"2002","journal-title":"EMBO J"},{"issue":"8","key":"10.1016\/j.neurot.2025.e00525_bib51","doi-asserted-by":"crossref","first-page":"18224","DOI":"10.3390\/ijms160818224","article-title":"Mitochondria retrograde signaling and the UPR mt: where are we in mammals?","volume":"16","author":"Arnould","year":"2015","journal-title":"Int J Mol Sci"},{"issue":"Pt 1","key":"10.1016\/j.neurot.2025.e00525_bib52","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1242\/jeb.090738","article-title":"The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease","volume":"217","author":"Jovaisaite","year":"2014","journal-title":"J\u00a0Exp Biol"},{"key":"10.1016\/j.neurot.2025.e00525_bib53","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.freeradbiomed.2013.05.002","article-title":"SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage","volume":"63","author":"Tseng","year":"2013","journal-title":"Free Radic Biol Med"},{"issue":"33","key":"10.1016\/j.neurot.2025.e00525_bib54","doi-asserted-by":"crossref","first-page":"13500","DOI":"10.1074\/jbc.R117.791061","article-title":"The mitochondrial unfolded protein response: signaling from the powerhouse","volume":"292","author":"Qureshi","year":"2017","journal-title":"J\u00a0Biol Chem"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib55","doi-asserted-by":"crossref","first-page":"613","DOI":"10.2174\/1570159X18666200123165002","article-title":"A\u00a0new vision of mitochondrial unfolded protein response to the sirtuin family","volume":"18","author":"Weng","year":"2020","journal-title":"Curr Neuropharmacol"},{"issue":"31","key":"10.1016\/j.neurot.2025.e00525_bib56","doi-asserted-by":"crossref","first-page":"4393","DOI":"10.1038\/onc.2017.52","article-title":"Selected mitochondrial DNA landscapes activate the SIRT3 axis of the UPR(mt) to promote metastasis","volume":"36","author":"Kenny","year":"2017","journal-title":"Oncogene"},{"issue":"21","key":"10.1016\/j.neurot.2025.e00525_bib57","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1091\/mbc.E16-05-0313","article-title":"Amyloid \u03b2-peptides interfere with mitochondrial preprotein import competence by a coaggregation process","volume":"27","author":"Cenini","year":"2016","journal-title":"Mol Biol Cell"},{"issue":"35","key":"10.1016\/j.neurot.2025.e00525_bib58","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":"Hansson Petersen","year":"2008","journal-title":"Proc Natl Acad Sci USA"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib59","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1083\/jcb.200207030","article-title":"Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells","volume":"161","author":"Anandatheerthavarada","year":"2003","journal-title":"J\u00a0Cell Biol"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib60","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1515\/revneuro.2007.18.5.343","article-title":"Mitochondrial translocation of amyloid precursor protein and its cleaved products: relevance to mitochondrial dysfunction in Alzheimer's disease","volume":"18","author":"Anandatheerthavarada","year":"2007","journal-title":"Rev Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib61","doi-asserted-by":"crossref","DOI":"10.1038\/srep21734","article-title":"Interplay of histidine residues of the Alzheimer's disease A\u03b2 peptide governs its Zn-induced oligomerization","volume":"6","author":"Istrate","year":"2016","journal-title":"Sci Rep"},{"issue":"39","key":"10.1016\/j.neurot.2025.e00525_bib62","doi-asserted-by":"crossref","first-page":"29096","DOI":"10.1074\/jbc.M602532200","article-title":"Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome","volume":"281","author":"Falkevall","year":"2006","journal-title":"PreP. J Biol Chem."},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib63","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.cmet.2014.07.024","article-title":"Amyloid-\u03b2 peptide induces mitochondrial dysfunction by inhibition of preprotein maturation","volume":"20","author":"Mossmann","year":"2014","journal-title":"Cell Metabol"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib64","doi-asserted-by":"crossref","first-page":"610","DOI":"10.2174\/1567205013666151221145445","article-title":"Evidence for mitochondrial UPR gene activation in familial and sporadic Alzheimer's disease","volume":"13","author":"Beck","year":"2016","journal-title":"Curr Alzheimer Res"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib65","doi-asserted-by":"crossref","first-page":"5733","DOI":"10.1038\/s41380-020-0807-4","article-title":"Loss of function of the mitochondrial peptidase PITRM1 induces proteotoxic stress and Alzheimer's disease-like pathology in human cerebral organoids","volume":"26","author":"P\u00e9rez","year":"2021","journal-title":"Mol Psychiatr"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib66","doi-asserted-by":"crossref","first-page":"9936","DOI":"10.1038\/s41598-024-59998-1","article-title":"Mitochondrial dynamics: updates and perspectives","volume":"14","author":"Zhang","year":"2024","journal-title":"Sci Rep"},{"issue":"6-7","key":"10.1016\/j.neurot.2025.e00525_bib67","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1515\/hsz-2020-0103","article-title":"The MICOS complex, a structural element of mitochondria with versatile functions","volume":"401","author":"Khosravi","year":"2020","journal-title":"Biol Chem"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib68","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/s00441-016-2433-7","article-title":"The MICOS complex of human mitochondria","volume":"367","author":"Kozjak-Pavlovic","year":"2017","journal-title":"Cell Tissue Res"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib69","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1007\/s10495-016-1295-5","article-title":"Mitochondrial dynamics during cell cycling","volume":"21","author":"Horbay","year":"2016","journal-title":"Apoptosis"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib70","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.bbrc.2017.06.094","article-title":"Mitochondrial dynamics coordinate cell differentiation","volume":"500","author":"Noguchi","year":"2018","journal-title":"Biochem Biophys Res Commun"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib71","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1083\/jcb.200211046","article-title":"Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development","volume":"160","author":"Chen","year":"2003","journal-title":"J\u00a0Cell Biol"},{"issue":"5-6","key":"10.1016\/j.neurot.2025.e00525_bib72","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.ijmm.2014.03.006","article-title":"Dynamin-related protein Drp1 and mitochondria are important for Shigella flexneri infection","volume":"304","author":"Lum","year":"2014","journal-title":"International journal of medical microbiology : IJMM"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib73","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003722","article-title":"Hepatitis B virus disrupts mitochondrial dynamics: induces fission and mitophagy to attenuate apoptosis","volume":"9","author":"Kim","year":"2013","journal-title":"PLoS Pathog"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib74","doi-asserted-by":"crossref","DOI":"10.1096\/fj.202100067R","article-title":"Mitochondrial fusion and fission: the fine-tune balance for cellular homeostasis","volume":"35","author":"Adebayo","year":"2021","journal-title":"Faseb J"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib75","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1083\/jcb.143.2.351","article-title":"A\u00a0human dynamin-related protein controls the distribution of mitochondria","volume":"143","author":"Smirnova","year":"1998","journal-title":"J\u00a0Cell Biol"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib76","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1083\/jcb.151.2.367","article-title":"Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p","volume":"151","author":"Mozdy","year":"2000","journal-title":"J\u00a0Cell Biol"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib77","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1038\/embor.2011.54","article-title":"MiD49 and MiD51, new components of the mitochondrial fission machinery","volume":"12","author":"Palmer","year":"2011","journal-title":"EMBO Rep"},{"issue":"6","key":"10.1016\/j.neurot.2025.e00525_bib78","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1091\/mbc.e07-12-1287","article-title":"The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells","volume":"19","author":"Gandre-Babbe","year":"2008","journal-title":"Mol Biol Cell"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib79","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1038\/sj.embor.7401062","article-title":"Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death","volume":"8","author":"Cribbs","year":"2007","journal-title":"EMBO Rep"},{"issue":"1-2","key":"10.1016\/j.neurot.2025.e00525_bib80","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.cell.2011.11.030","article-title":"The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways","volume":"148","author":"Wang","year":"2012","journal-title":"Cell"},{"issue":"15","key":"10.1016\/j.neurot.2025.e00525_bib81","doi-asserted-by":"crossref","first-page":"11521","DOI":"10.1074\/jbc.M607279200","article-title":"Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission","volume":"282","author":"Taguchi","year":"2007","journal-title":"J\u00a0Biol Chem"},{"issue":"8","key":"10.1016\/j.neurot.2025.e00525_bib82","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201948686","article-title":"PINK1 phosphorylates Drp1(S616) to regulate mitophagy-independent mitochondrial dynamics","volume":"21","author":"Han","year":"2020","journal-title":"EMBO Rep"},{"key":"10.1016\/j.neurot.2025.e00525_bib83","doi-asserted-by":"crossref","DOI":"10.1016\/j.taap.2019.114874","article-title":"p38 MAPK-DRP1 signaling is involved in mitochondrial dysfunction and cell death in mutant A53T \u03b1-synuclein model of Parkinson's disease","volume":"388","author":"Gui","year":"2020","journal-title":"Toxicol Appl Pharmacol"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib84","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/79944","article-title":"OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28","volume":"26","author":"Alexander","year":"2000","journal-title":"Nat Genet"},{"key":"10.1016\/j.neurot.2025.e00525_bib85","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2023.1268883","article-title":"Mitochondrial transport in neurons and evidence for its involvement in acute neurological disorders","volume":"17","author":"Lu","year":"2023","journal-title":"Front Neurosci"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib86","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1091\/mbc.e05-06-0526","article-title":"Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons","volume":"17","author":"Pilling","year":"2006","journal-title":"Mol Biol Cell"},{"issue":"11","key":"10.1016\/j.neurot.2025.e00525_bib87","doi-asserted-by":"crossref","first-page":"3717","DOI":"10.1091\/mbc.10.11.3717","article-title":"Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport","volume":"10","author":"Martin","year":"1999","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.neurot.2025.e00525_bib88","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0074-7696(00)00005-X","article-title":"Regulation and expression of metazoan unconventional myosins","volume":"200","author":"Sokac","year":"2000","journal-title":"Int Rev Cytol"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib89","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1083\/jcb.200405100","article-title":"Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway","volume":"167","author":"Frederick","year":"2004","journal-title":"J\u00a0Cell Biol"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib90","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.neuron.2012.11.027","article-title":"TRAK\/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites","volume":"77","author":"van Spronsen","year":"2013","journal-title":"Neuron"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib91","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.cell.2007.11.024","article-title":"Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation","volume":"132","author":"Kang","year":"2008","journal-title":"Cell."},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib92","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/s41467-020-20346-2","article-title":"Metaxins are core components of mitochondrial transport adaptor complexes","volume":"12","author":"Zhao","year":"2021","journal-title":"Nat Commun"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib93","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-023-46106-y","article-title":"Author Correction: amyloid-\u03b2 impairs mitochondrial dynamics and autophagy in Alzheimer's disease experimental models","volume":"13","author":"de la Cueva","year":"2023","journal-title":"Sci Rep"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib94","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.3233\/JAD-220884","article-title":"Early mitochondrial defects in the 5xFAD mouse model of Alzheimer's disease","volume":"91","author":"Sharma","year":"2023","journal-title":"J\u00a0Alzheimers Dis"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib95","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1007\/s12035-017-0385-x","article-title":"Caspase-cleaved tau impairs mitochondrial dynamics in Alzheimer's disease","volume":"55","author":"P\u00e9rez","year":"2018","journal-title":"Mol Neurobiol"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib96","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.3233\/JAD-215175","article-title":"Mitochondrial fusion suppresses tau pathology-induced neurodegeneration and cognitive decline","volume":"84","author":"Wang","year":"2021","journal-title":"J\u00a0Alzheimers Dis"},{"issue":"13","key":"10.1016\/j.neurot.2025.e00525_bib97","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1093\/hmg\/ddr139","article-title":"Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage","volume":"20","author":"Manczak","year":"2011","journal-title":"Hum Mol Genet"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib98","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.neurobiolaging.2014.08.005","article-title":"Blockage of GSK3\u03b2-mediated Drp1 phosphorylation provides neuroprotection in neuronal and mouse models of Alzheimer's disease","volume":"36","author":"Yan","year":"2015","journal-title":"Neurobiol Aging"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib99","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1007\/s00401-022-02499-0","article-title":"A\u00a0CHCHD6-APP axis connects amyloid and mitochondrial pathology in Alzheimer's disease","volume":"144","author":"Shang","year":"2022","journal-title":"Acta Neuropathol"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib100","doi-asserted-by":"crossref","first-page":"195","DOI":"10.3233\/JAD-2006-9211","article-title":"Peri-nuclear clustering of mitochondria is triggered during aluminum maltolate induced apoptosis","volume":"9","author":"Dewitt","year":"2006","journal-title":"J\u00a0Alzheimers Dis"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib101","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.bbadis.2011.01.007","article-title":"Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons","volume":"1812","author":"Calkins","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.neurot.2025.e00525_bib102","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.neurobiolaging.2020.09.011","article-title":"Stabilization of microtubules improves cognitive functions and axonal transport of mitochondria in Alzheimer's disease model mice","volume":"96","author":"Guo","year":"2020","journal-title":"Neurobiol Aging"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib103","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1007\/s13760-020-01359-6","article-title":"Blocking retrograde axonal transport of autophagosomes contributes to sevoflurane-induced neuron apoptosis in APP\/PS1 mice","volume":"121","author":"Xu","year":"2021","journal-title":"Acta Neurol Belg"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib104","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/s13024-017-0164-1","article-title":"Increased acetylation of Peroxiredoxin1 by HDAC6 inhibition leads to recovery of A\u03b2-induced impaired axonal transport","volume":"12","author":"Choi","year":"2017","journal-title":"Mol Neurodegener"},{"key":"10.1016\/j.neurot.2025.e00525_bib105","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2022.927195","article-title":"Decreased anterograde transport coupled with sustained retrograde transport contributes to reduced axonal mitochondrial density in tauopathy neurons","volume":"15","author":"Sabui","year":"2022","journal-title":"Front Mol Neurosci"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib106","doi-asserted-by":"crossref","first-page":"3010","DOI":"10.1038\/s41380-022-01538-2","article-title":"Caspase-cleaved tau is senescence-associated and induces a toxic gain of function by putting a brake on axonal transport","volume":"27","author":"Conze","year":"2022","journal-title":"Mol Psychiatr"},{"issue":"6001","key":"10.1016\/j.neurot.2025.e00525_bib107","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1126\/science.1194653","article-title":"Tau reduction prevents Abeta-induced defects in axonal transport","volume":"330","author":"Vossel","year":"2010","journal-title":"Science"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib108","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.1016\/j.ajpath.2011.07.004","article-title":"Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain","volume":"179","author":"Kopeikina","year":"2011","journal-title":"Am J Pathol"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib109","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.1523\/JNEUROSCI.5927-11.2012","article-title":"Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease","volume":"32","author":"Shahpasand","year":"2012","journal-title":"J\u00a0Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib110","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2022.852368","article-title":"Hyperphosphorylated human tau accumulates at the synapse, localizing on synaptic mitochondrial outer membranes and disrupting respiration in a mouse model of tauopathy","volume":"15","author":"Trease","year":"2022","journal-title":"Front Mol Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib111","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2021.730604","article-title":"Mitochondrial protein PGAM5 emerges as a new regulator in neurological diseases","volume":"14","author":"Liang","year":"2021","journal-title":"Front Mol Neurosci"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib112","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/s41392-023-01503-7","article-title":"The mitophagy pathway and its implications in human diseases","volume":"8","author":"Wang","year":"2023","journal-title":"Signal Transduct Targeted Ther"},{"key":"10.1016\/j.neurot.2025.e00525_bib113","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2021.746873","article-title":"Mitochondrial quality control strategies: potential therapeutic targets for neurodegenerative diseases?","volume":"15","author":"Hu","year":"2021","journal-title":"Front Neurosci"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib114","doi-asserted-by":"crossref","first-page":"4182","DOI":"10.1080\/15548627.2021.1907167","article-title":"The role of mitophagy in the regulation of mitochondrial energetic status in neurons","volume":"17","author":"Han","year":"2021","journal-title":"Autophagy"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib115","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13024-020-00367-7","article-title":"PINK1 and Parkin mitochondrial quality control: a source of regional vulnerability in Parkinson's disease","volume":"15","author":"Ge","year":"2020","journal-title":"Mol Neurodegener"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib116","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1186\/s40478-020-01062-w","article-title":"PINK1\/PARKIN signalling in neurodegeneration and neuroinflammation","volume":"8","author":"Quinn","year":"2020","journal-title":"Acta Neuropathologica Communications"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib117","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2313540121","article-title":"Tom20 gates PINK1 activity and mediates its tethering of the TOM and TIM23 translocases upon mitochondrial stress","volume":"121","author":"Eldeeb","year":"2024","journal-title":"Proc Natl Acad Sci USA"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib118","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.neuron.2014.12.007","article-title":"The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease","volume":"85","author":"Pickrell","year":"2015","journal-title":"Neuron"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib119","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1111\/febs.13127","article-title":"PINK1 and Parkin \u2013 mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease","volume":"282","author":"Kazlauskaite","year":"2015","journal-title":"FEBS J"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib120","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1004279","article-title":"PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix","volume":"10","author":"Thomas","year":"2014","journal-title":"PLoS Genet"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib121","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.devcel.2011.12.014","article-title":"Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin","volume":"22","author":"Lazarou","year":"2012","journal-title":"Dev Cell"},{"issue":"9","key":"10.1016\/j.neurot.2025.e00525_bib122","doi-asserted-by":"crossref","DOI":"10.1111\/acel.13211","article-title":"Dependence of PINK1 accumulation on mitochondrial redox system","volume":"19","author":"Gao","year":"2020","journal-title":"Aging Cell"},{"issue":"11","key":"10.1016\/j.neurot.2025.e00525_bib123","doi-asserted-by":"crossref","first-page":"2076","DOI":"10.1111\/febs.13249","article-title":"Parkin structure and function","volume":"282","author":"Seirafi","year":"2015","journal-title":"FEBS J"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib124","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s00441-016-2485-8","article-title":"Mitochondrial quality control by the Pink1\/Parkin system","volume":"367","author":"R\u00fcb","year":"2017","journal-title":"Cell Tissue Res"},{"issue":"7445","key":"10.1016\/j.neurot.2025.e00525_bib125","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/nature12043","article-title":"Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization","volume":"496","author":"Sarraf","year":"2013","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib126","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.cels.2016.08.009","article-title":"Highly multiplexed quantitative mass spectrometry analysis of ubiquitylomes","volume":"3","author":"Rose","year":"2016","journal-title":"Cell Syst"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib127","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/ncb2012","article-title":"PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1","volume":"12","author":"Geisler","year":"2010","journal-title":"Nat Cell Biol"},{"issue":"15","key":"10.1016\/j.neurot.2025.e00525_bib128","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1073\/pnas.1523926113","article-title":"Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria","volume":"113","author":"Richter","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib129","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.immuni.2017.02.018","article-title":"The ubiquitin binding protein TAX1BP1 mediates autophagasome induction and the metabolic transition of activated T cells","volume":"46","author":"Whang","year":"2017","journal-title":"Immunity"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib130","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/s41419-021-04469-y","article-title":"BNIP3L\/NIX-mediated mitophagy: molecular mechanisms and implications for human disease","volume":"13","author":"Li","year":"2021","journal-title":"Cell Death Dis"},{"key":"10.1016\/j.neurot.2025.e00525_bib131","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.788634","article-title":"FUNDC1: a promising mitophagy regulator at the mitochondria-associated membrane for cardiovascular diseases","volume":"9","author":"Li","year":"2021","journal-title":"Front Cell Dev Biol"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib132","doi-asserted-by":"crossref","first-page":"7527","DOI":"10.1038\/ncomms8527","article-title":"Bcl-2-like protein 13 is a mammalian Atg32 homologue that mediates mitophagy and mitochondrial fragmentation","volume":"6","author":"Murakawa","year":"2015","journal-title":"Nat Commun"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib133","doi-asserted-by":"crossref","first-page":"2944","DOI":"10.1096\/fj.201901735R","article-title":"FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions","volume":"34","author":"Yoo","year":"2020","journal-title":"Faseb J"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib134","doi-asserted-by":"crossref","DOI":"10.1111\/acel.12860","article-title":"Disrupted-in-schizophrenia-1 protects synaptic plasticity in a transgenic mouse model of Alzheimer's disease as a mitophagy receptor","volume":"18","author":"Wang","year":"2019","journal-title":"Aging Cell"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib135","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1038\/cdd.2014.139","article-title":"AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62\/SQSTM1","volume":"22","author":"Strappazzon","year":"2015","journal-title":"Cell Death Differ"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib136","doi-asserted-by":"crossref","first-page":"5731","DOI":"10.1038\/s41467-020-19547-6","article-title":"Pharmacological targeting of MCL-1 promotes mitophagy and improves disease pathologies in an Alzheimer's disease mouse model","volume":"11","author":"Cen","year":"2020","journal-title":"Nat Commun"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib137","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1038\/ncb2837","article-title":"Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells","volume":"15","author":"Chu","year":"2013","journal-title":"Nat Cell Biol"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib138","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1038\/s41419-022-04906-6","article-title":"Mitochondrial autophagy: molecular mechanisms and implications for cardiovascular disease","volume":"13","author":"Li","year":"2022","journal-title":"Cell Death Dis"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib139","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020104705","article-title":"Molecular mechanisms and physiological functions of mitophagy","volume":"40","author":"Onishi","year":"2021","journal-title":"EMBO J"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib140","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1093\/hmg\/ddv616","article-title":"PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer's disease","volume":"25","author":"Mart\u00edn-Maestro","year":"2016","journal-title":"Hum Mol Genet"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib141","doi-asserted-by":"crossref","first-page":"3233","DOI":"10.1093\/brain\/awx258","article-title":"PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer's disease","volume":"140","author":"Du","year":"2017","journal-title":"Brain"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib142","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1038\/s41593-018-0332-9","article-title":"Mitophagy inhibits amyloid-\u03b2 and tau pathology and reverses cognitive deficits in models of Alzheimer's disease","volume":"22","author":"Fang","year":"2019","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib143","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/9302761","article-title":"Slower dynamics and aged mitochondria in sporadic Alzheimer's disease","volume":"2017","author":"Mart\u00edn-Maestro","year":"2017","journal-title":"Oxid Med Cell Longev"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib144","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s00401-020-02234-7","article-title":"Accumulation of amyloid precursor protein C-terminal fragments triggers mitochondrial structure, function, and mitophagy defects in Alzheimer's disease models and human brains","volume":"141","author":"Vaillant-Beuchot","year":"2021","journal-title":"Acta Neuropathol"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib145","doi-asserted-by":"crossref","first-page":"8220","DOI":"10.1007\/s12035-019-01665-y","article-title":"Autophagy induction by bexarotene promotes mitophagy in presenilin 1 familial Alzheimer's disease iPSC-derived neural stem cells","volume":"56","author":"Mart\u00edn-Maestro","year":"2019","journal-title":"Mol Neurobiol"},{"key":"10.1016\/j.neurot.2025.e00525_bib146","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.3389\/fphar.2019.01529","article-title":"\u03b2-Asarone inhibits amyloid-\u03b2 by promoting autophagy in a cell model of Alzheimer's disease","volume":"10","author":"Wang","year":"2019","journal-title":"Front Pharmacol"},{"key":"10.1016\/j.neurot.2025.e00525_bib147","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.toxlet.2017.10.021","article-title":"Resveratrol attenuates oxidative damage through activating mitophagy in an in vitro model of Alzheimer's disease","volume":"282","author":"Wang","year":"2018","journal-title":"Toxicol Lett"},{"key":"10.1016\/j.neurot.2025.e00525_bib148","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1016\/j.omtn.2021.02.010","article-title":"miR-204 silencing reduces mitochondrial autophagy and ROS production in a murine AD model via the TRPML1-activated STAT3 pathway","volume":"24","author":"Zhang","year":"2021","journal-title":"Mol Ther Nucleic Acids"},{"key":"10.1016\/j.neurot.2025.e00525_bib149","doi-asserted-by":"crossref","DOI":"10.1016\/j.lfs.2020.117322","article-title":"Parkin overexpression attenuates A\u03b2-induced mitochondrial dysfunction in HEK293 cells by restoring impaired mitophagy","volume":"244","author":"Wang","year":"2020","journal-title":"Life Sci"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib150","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1007\/s11011-020-00587-2","article-title":"\u03b2-Asarone improves learning and memory in A\u03b2(1-42)-induced Alzheimer's disease rats by regulating PINK1-Parkin-mediated mitophagy","volume":"35","author":"Han","year":"2020","journal-title":"Metab Brain Dis"},{"issue":"14","key":"10.1016\/j.neurot.2025.e00525_bib151","doi-asserted-by":"crossref","first-page":"17356","DOI":"10.18632\/oncotarget.7861","article-title":"Tau accumulation impairs mitophagy via increasing mitochondrial membrane potential and reducing mitochondrial Parkin","volume":"7","author":"Hu","year":"2016","journal-title":"Oncotarget"},{"issue":"17","key":"10.1016\/j.neurot.2025.e00525_bib152","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21176344","article-title":"Insights into disease-associated tau impact on mitochondria","volume":"21","author":"Szabo","year":"2020","journal-title":"Int J Mol Sci"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib153","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s13024-020-00410-7","article-title":"Tauopathy-associated tau modifications selectively impact neurodegeneration and mitophagy in a novel C. elegans single-copy transgenic model","volume":"15","author":"Guha","year":"2020","journal-title":"Mol Neurodegener"},{"key":"10.1016\/j.neurot.2025.e00525_bib154","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.nbd.2013.10.018","article-title":"AD-linked, toxic NH2 human tau affects the quality control of mitochondria in neurons","volume":"62","author":"Amadoro","year":"2014","journal-title":"Neurobiol Dis"},{"issue":"7975","key":"10.1016\/j.neurot.2025.e00525_bib155","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/s41586-023-06426-5","article-title":"Nuclear genetic control of mtDNA copy number and heteroplasmy in humans","volume":"620","author":"Gupta","year":"2023","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00525_bib156","article-title":"Mitochondrial DNA abundance in blood is associated with Alzheimer's disease- and dementia-risk","author":"Stocker","year":"2024","journal-title":"Mol Psychiatr"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib157","doi-asserted-by":"crossref","first-page":"1971","DOI":"10.3390\/antiox10121971","article-title":"Oxidative stress biomarkers and mitochondrial DNA copy number associated with APOE4 allele and cholinesterase inhibitor therapy in patients with Alzheimer\u2019s disease","volume":"10","author":"Liou","year":"2021","journal-title":"Antioxidants"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib158","doi-asserted-by":"crossref","first-page":"275","DOI":"10.3233\/JAD-2008-13305","article-title":"Mitochondrial transcription factor A (TFAM) gene variation and risk of late-onset Alzheimer's disease","volume":"13","author":"Alvarez","year":"2008","journal-title":"J\u00a0Alzheimers Dis"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib159","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1016\/j.bbrc.2016.11.135","article-title":"Overexpression of MTERF4 promotes the amyloidogenic processing of APP by inhibiting ADAM10","volume":"482","author":"Wang","year":"2017","journal-title":"Biochem Biophys Res Commun"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib160","doi-asserted-by":"crossref","DOI":"10.3390\/antiox10121917","article-title":"ROS-induced mtDNA release: the emerging messenger for communication between neurons and innate immune cells during neurodegenerative disorder progression","volume":"10","author":"Zhao","year":"2021","journal-title":"Antioxidants"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib161","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1007\/s11064-020-03192-y","article-title":"Hypermethylation of mitochondrial cytochrome b and cytochrome c oxidase II genes with decreased mitochondrial DNA copy numbers in the APP\/PS1 transgenic mouse model of Alzheimer's disease","volume":"46","author":"Xu","year":"2021","journal-title":"Neurochem Res"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib162","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.bbrc.2019.09.094","article-title":"Altered mitochondrial DNA methylation and mitochondrial DNA copy number in an APP\/PS1 transgenic mouse model of Alzheimer disease","volume":"520","author":"Xu","year":"2019","journal-title":"Biochem Biophys Res Commun"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib163","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1016\/j.cell.2014.11.036","article-title":"Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production","volume":"159","author":"White","year":"2014","journal-title":"Cell"},{"issue":"7","key":"10.1016\/j.neurot.2025.e00525_bib164","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/j.cell.2014.11.037","article-title":"Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA","volume":"159","author":"Rongvaux","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.neurot.2025.e00525_bib165","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/834502","article-title":"Exercise-induced neuroprotection of hippocampus in APP\/PS1 transgenic mice via upregulation of mitochondrial 8-oxoguanine DNA glycosylase","volume":"2014","author":"Bo","year":"2014","journal-title":"Oxid Med Cell Longev"},{"issue":"9","key":"10.1016\/j.neurot.2025.e00525_bib166","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102942","article-title":"BAD-mediated neuronal apoptosis and neuroinflammation contribute to Alzheimer's disease pathology","volume":"24","author":"Zhang","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.neurot.2025.e00525_bib167","doi-asserted-by":"crossref","first-page":"192.e1","DOI":"10.1016\/j.neurobiolaging.2016.12.009","article-title":"Cerebrospinal fluid mitochondrial DNA in the Alzheimer's disease continuum","volume":"53","author":"Cervera-Carles","year":"2017","journal-title":"Neurobiol Aging"},{"issue":"7973","key":"10.1016\/j.neurot.2025.e00525_bib168","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/s41586-023-06373-1","article-title":"cGAS-STING drives ageing-related inflammation and neurodegeneration","volume":"620","author":"Gulen","year":"2023","journal-title":"Nature"},{"issue":"9","key":"10.1016\/j.neurot.2025.e00525_bib169","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1007\/s11064-023-03945-5","article-title":"A\u03b2 induces neuroinflammation and microglial M1 polarization via cGAS-STING-IFITM3 signaling pathway in BV-2 cells","volume":"48","author":"Wu","year":"2023","journal-title":"Neurochem Res"},{"issue":"23","key":"10.1016\/j.neurot.2025.e00525_bib170","doi-asserted-by":"crossref","first-page":"E4612","DOI":"10.1073\/pnas.1705499114","article-title":"cGAS is essential for cellular senescence","volume":"114","author":"Yang","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"issue":"Pt 1","key":"10.1016\/j.neurot.2025.e00525_bib171","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.freeradbiomed.2022.09.032","article-title":"Altered glucose metabolism in Alzheimer's disease: role of mitochondrial dysfunction and oxidative stress","volume":"193","author":"Dewanjee","year":"2022","journal-title":"Free Radic Biol Med"},{"issue":"20","key":"10.1016\/j.neurot.2025.e00525_bib172","doi-asserted-by":"crossref","DOI":"10.3390\/ijms222011185","article-title":"ATP synthase and mitochondrial bioenergetics dysfunction in Alzheimer's disease","volume":"22","author":"Patro","year":"2021","journal-title":"Int J Mol Sci"},{"issue":"16","key":"10.1016\/j.neurot.2025.e00525_bib173","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23169212","article-title":"The role of bioenergetics in neurodegeneration","volume":"23","author":"Strope","year":"2022","journal-title":"Int J Mol Sci"},{"issue":"8","key":"10.1016\/j.neurot.2025.e00525_bib174","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1007\/s10571-021-01147-7","article-title":"Metabolic regulation of glia and their neuroinflammatory role in Alzheimer's disease","volume":"42","author":"Preeti","year":"2022","journal-title":"Cell Mol Neurobiol"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib175","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1186\/s12967-024-05571-3","article-title":"Gene therapy in A\u03b2-induced cell and mouse models of Alzheimer's disease through compensating defective mitochondrial complex I function","volume":"22","author":"Li","year":"2024","journal-title":"J\u00a0Transl Med"},{"issue":"11","key":"10.1016\/j.neurot.2025.e00525_bib176","first-page":"1028","article-title":"DJ1 ameliorates AD-like pathology in the Hippocampus of APP\/PS1 mice","volume":"36","author":"Peng","year":"2023","journal-title":"Biomed Environ Sci"},{"key":"10.1016\/j.neurot.2025.e00525_bib177","doi-asserted-by":"crossref","DOI":"10.1177\/17590914231159226","article-title":"Thioredoxin-1 promotes mitochondrial biogenesis through regulating AMPK\/Sirt1\/PGC1\u03b1 pathway in Alzheimer's disease","volume":"15","author":"Jia","year":"2023","journal-title":"ASN Neuro"},{"issue":"43","key":"10.1016\/j.neurot.2025.e00525_bib178","doi-asserted-by":"crossref","first-page":"12292","DOI":"10.1073\/pnas.1606171113","article-title":"PPAR\u03b3-coactivator-1\u03b1 gene transfer reduces neuronal loss and amyloid-\u03b2 generation by reducing \u03b2-secretase in an Alzheimer's disease model","volume":"113","author":"Katsouri","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"issue":"18","key":"10.1016\/j.neurot.2025.e00525_bib179","doi-asserted-by":"crossref","DOI":"10.3390\/cells11182849","article-title":"A\u00a0role for PGC-1a in the control of abnormal mitochondrial dynamics in Alzheimer's disease","volume":"11","author":"Wang","year":"2022","journal-title":"Cells"},{"issue":"12","key":"10.1016\/j.neurot.2025.e00525_bib180","doi-asserted-by":"crossref","first-page":"2417","DOI":"10.1038\/s41418-022-01027-7","article-title":"CEND1 deficiency induces mitochondrial dysfunction and cognitive impairment in Alzheimer's disease","volume":"29","author":"Xie","year":"2022","journal-title":"Cell Death Differ"},{"key":"10.1016\/j.neurot.2025.e00525_bib181","doi-asserted-by":"crossref","DOI":"10.1016\/j.intimp.2022.109614","article-title":"Mitochondrial calcium uptake 3 mitigates cerebral amyloid angiopathy-related neuronal death and glial inflammation by reducing mitochondrial dysfunction","volume":"117","author":"Zhou","year":"2023","journal-title":"Int Immunopharm"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib182","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1038\/npp.2015.164","article-title":"Disrupted-in-Schizophrenia-1 attenuates amyloid-\u03b2 generation and cognitive deficits in APP\/PS1 transgenic mice by reduction of \u03b2-site APP-cleaving enzyme 1 levels","volume":"41","author":"Deng","year":"2016","journal-title":"Neuropsychopharmacology"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib183","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/s41392-024-01780-w","article-title":"Adeno-associated virus as a delivery vector for gene therapy of human diseases","volume":"9","author":"Wang","year":"2024","journal-title":"Signal Transduct Targeted Ther"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib184","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/s10020-022-00456-x","article-title":"Gene therapy of yeast NDI1 on mitochondrial complex I dysfunction in rotenone-induced Parkinson's disease models in vitro and vivo","volume":"28","author":"Li","year":"2022","journal-title":"Mol Med"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib185","doi-asserted-by":"crossref","DOI":"10.3390\/cells10020347","article-title":"The role of DJ-1 in cellular metabolism and pathophysiological implications for Parkinson's disease","volume":"10","author":"Mencke","year":"2021","journal-title":"Cells"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib186","doi-asserted-by":"crossref","DOI":"10.3390\/antiox12051078","article-title":"The importance of thioredoxin-1 in health and disease","volume":"12","author":"Oberacker","year":"2023","journal-title":"Antioxidants"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib187","doi-asserted-by":"crossref","first-page":"5496","DOI":"10.1038\/s41467-023-41304-8","article-title":"The master energy homeostasis regulator PGC-1\u03b1 exhibits an mRNA nuclear export function","volume":"14","author":"Mihaylov","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00525_bib188","article-title":"Cend1, a story with many tales: from regulation of cell cycle progression\/exit of neural stem cells to brain structure and function","volume":"2019","author":"Gaitanou","year":"2019","journal-title":"Stem Cell Int"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib189","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/s41418-018-0113-8","article-title":"MICU3 is a tissue-specific enhancer of mitochondrial calcium uptake","volume":"26","author":"Patron","year":"2019","journal-title":"Cell Death Differ"},{"issue":"22","key":"10.1016\/j.neurot.2025.e00525_bib190","article-title":"Therapeutic potential of targeting mitochondria for Alzheimer's disease treatment","volume":"11","author":"Atlante","year":"2022","journal-title":"J\u00a0Clin Med"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib191","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.apsb.2021.06.014","article-title":"Targeting whole body metabolism and mitochondrial bioenergetics in the drug development for Alzheimer's disease","volume":"12","author":"Austad","year":"2022","journal-title":"Acta Pharm Sin B"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib192","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.bj.2022.05.002","article-title":"Targeting mitochondrial bioenergetics as a promising therapeutic strategy in metabolic and neurodegenerative diseases","volume":"45","author":"Bhatti","year":"2022","journal-title":"Biomed J"},{"issue":"2","key":"10.1016\/j.neurot.2025.e00525_bib193","doi-asserted-by":"crossref","DOI":"10.3390\/antiox12020453","article-title":"Mitochondrial-targeted antioxidant MitoQ-mediated autophagy: a novel strategy for precise radiation protection","volume":"12","author":"Bao","year":"2023","journal-title":"Antioxidants"},{"issue":"21","key":"10.1016\/j.neurot.2025.e00525_bib194","doi-asserted-by":"crossref","DOI":"10.3390\/ijms222111520","article-title":"Disentangling mitochondria in Alzheimer's disease","volume":"22","author":"Johri","year":"2021","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.neurot.2025.e00525_bib195","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.mcn.2019.03.001","article-title":"Small molecules as therapeutic drugs for Alzheimer's disease","volume":"96","author":"Oliver","year":"2019","journal-title":"Mol Cell Neurosci"},{"issue":"3","key":"10.1016\/j.neurot.2025.e00525_bib196","doi-asserted-by":"crossref","first-page":"297","DOI":"10.2174\/1567205013666151218150004","article-title":"SS31, a small molecule antioxidant peptide, attenuates \u03b2-amyloid elevation, mitochondrial\/synaptic deterioration and cognitive deficit in SAMP8 mice","volume":"13","author":"Jia","year":"2016","journal-title":"Curr Alzheimer Res"},{"issue":"8","key":"10.1016\/j.neurot.2025.e00525_bib197","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1093\/hmg\/ddx129","article-title":"Mitochondria-targeted small molecule SS31: a potential candidate for the treatment of Alzheimer's disease","volume":"26","author":"Reddy","year":"2017","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.neurot.2025.e00525_bib198","doi-asserted-by":"crossref","DOI":"10.1016\/j.arres.2022.100037","article-title":"Pharmacological significance of MitoQ in ameliorating mitochondria-related diseases","volume":"5","author":"Sulaimon","year":"2022","journal-title":"Advances in Redox Research."},{"key":"10.1016\/j.neurot.2025.e00525_bib199","doi-asserted-by":"crossref","DOI":"10.1016\/j.mcn.2019.103409","article-title":"The mitochondria-targeted antioxidant MitoQ inhibits memory loss, neuropathology, and extends lifespan in aged 3xTg-AD mice","volume":"101","author":"Young","year":"2019","journal-title":"Mol Cell Neurosci"},{"key":"10.1016\/j.neurot.2025.e00525_bib200","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.bbrc.2023.02.076","article-title":"The mitochondria-targeted small molecule SS31 delays progression of behavioral deficits by attenuating \u03b2-amyloid plaque formation and mitochondrial\/synaptic deterioration in APP\/PS1 mice","volume":"658","author":"Jia","year":"2023","journal-title":"Biochem Biophys Res Commun"},{"issue":"37","key":"10.1016\/j.neurot.2025.e00525_bib201","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2011226118","article-title":"NAD(+) supplementation reduces neuroinflammation and cell senescence in a transgenic mouse model of Alzheimer's disease via cGAS-STING","volume":"118","author":"Hou","year":"2021","journal-title":"Proc Natl Acad Sci USA"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib202","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1038\/s41467-019-09291-x","article-title":"ATAD3A oligomerization causes neurodegeneration by coupling mitochondrial fragmentation and bioenergetics defects","volume":"10","author":"Zhao","year":"2019","journal-title":"Nat Commun"},{"issue":"1","key":"10.1016\/j.neurot.2025.e00525_bib203","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1038\/s41467-022-28769-9","article-title":"ATAD3A oligomerization promotes neuropathology and cognitive deficits in Alzheimer's disease models","volume":"13","author":"Zhao","year":"2022","journal-title":"Nat Commun"},{"issue":"10","key":"10.1016\/j.neurot.2025.e00525_bib204","doi-asserted-by":"crossref","first-page":"2740","DOI":"10.1002\/2211-5463.13273","article-title":"Activation of ERK-Drp1 signaling promotes hypoxia-induced A\u03b2 accumulation by upregulating mitochondrial fission and BACE1 activity","volume":"11","author":"Yuan","year":"2021","journal-title":"FEBS Open Bio"},{"issue":"4","key":"10.1016\/j.neurot.2025.e00525_bib205","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.3233\/JAD-170988","article-title":"Synergistic protective effects of mitochondrial division inhibitor 1 and mitochondria-targeted small peptide SS31 in Alzheimer's disease","volume":"62","author":"Reddy","year":"2018","journal-title":"J\u00a0Alzheimers Dis"},{"issue":"20","key":"10.1016\/j.neurot.2025.e00525_bib206","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1523\/JNEUROSCI.2385-16.2017","article-title":"Inhibition of Drp1 ameliorates synaptic depression, A\u03b2 deposition, and cognitive impairment in an Alzheimer's disease model","volume":"37","author":"Baek","year":"2017","journal-title":"J\u00a0Neurosci"},{"issue":"Pt 3","key":"10.1016\/j.neurot.2025.e00525_bib207","first-page":"789","article-title":"A\u00a0novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity","volume":"126","author":"Qi","year":"2013","journal-title":"J\u00a0Cell Sci"},{"issue":"11","key":"10.1016\/j.neurot.2025.e00525_bib208","doi-asserted-by":"crossref","DOI":"10.3390\/life13112156","article-title":"Therapeutic potential of P110 peptide: new insights into treatment of Alzheimer's disease","volume":"13","author":"Srivastava","year":"2023","journal-title":"Life"},{"issue":"5","key":"10.1016\/j.neurot.2025.e00525_bib209","doi-asserted-by":"crossref","first-page":"6128","DOI":"10.18632\/oncotarget.23640","article-title":"Drp1\/Fis1 interaction mediates mitochondrial dysfunction, bioenergetic failure and cognitive decline in Alzheimer's disease","volume":"9","author":"Joshi","year":"2018","journal-title":"Oncotarget"},{"key":"10.1016\/j.neurot.2025.e00525_bib210","doi-asserted-by":"crossref","DOI":"10.1016\/j.jep.2023.116455","article-title":"Loganin alleviated cognitive impairment in 3\u00d7Tg-AD mice through promoting mitophagy mediated by optineurin","volume":"312","author":"Zhou","year":"2023","journal-title":"J\u00a0Ethnopharmacol"}],"container-title":["Neurotherapeutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1878747925000030?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1878747925000030?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,4,15]],"date-time":"2025-04-15T09:26:30Z","timestamp":1744709190000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1878747925000030"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,4]]},"references-count":210,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2025,4]]}},"alternative-id":["S1878747925000030"],"URL":"https:\/\/doi.org\/10.1016\/j.neurot.2025.e00525","relation":{},"ISSN":["1878-7479"],"issn-type":[{"value":"1878-7479","type":"print"}],"subject":[],"published":{"date-parts":[[2025,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies","name":"articletitle","label":"Article Title"},{"value":"Neurotherapeutics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.neurot.2025.e00525","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Inc. on behalf of American Society for Experimental NeuroTherapeutics.","name":"copyright","label":"Copyright"}],"article-number":"e00525"}}