{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T18:50:48Z","timestamp":1789757448859,"version":"4.0.1"},"reference-count":65,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2023,10,5]],"date-time":"2023-10-05T00:00:00Z","timestamp":1696464000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Bright Focus Foundation","award":["R03 NS114731"],"award-info":[{"award-number":["R03 NS114731"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Mitochondrial dysfunction has been reported in many Huntington\u2019s disease (HD) models; however, it is unclear how these defects occur. Here, we test the hypothesis that excess pathogenic huntingtin (HTT) impairs mitochondrial homeostasis, using Drosophila genetics and pharmacological inhibitors in HD and polyQ-expansion disease models and in a mechanical stress-induced traumatic brain injury (TBI) model. Expression of pathogenic HTT caused fragmented mitochondria compared to normal HTT, but HTT did not co-localize with mitochondria under normal or pathogenic conditions. Expression of pathogenic polyQ (127Q) alone or in the context of Machado Joseph Disease (MJD) caused fragmented mitochondria. While mitochondrial fragmentation was not dependent on the cellular location of polyQ accumulations, the expression of a chaperone protein, excess of mitofusin (MFN), or depletion of dynamin-related protein 1 (DRP1) rescued fragmentation. Intriguingly, a higher concentration of nitric oxide (NO) was observed in polyQ-expressing larval brains and inhibiting NO production rescued polyQ-mediated fragmented mitochondria, postulating that DRP1 nitrosylation could contribute to excess fission. Furthermore, while excess PI3K, which suppresses polyQ-induced cell death, did not rescue polyQ-mediated fragmentation, it did rescue fragmentation caused by mechanical stress\/TBI. Together, our observations suggest that pathogenic polyQ alone is sufficient to cause DRP1-dependent mitochondrial fragmentation upstream of cell death, uncovering distinct physiological mechanisms for mitochondrial dysfunction in polyQ disease and mechanical stress.<\/jats:p>","DOI":"10.3390\/cells12192406","type":"journal-article","created":{"date-parts":[[2023,10,5]],"date-time":"2023-10-05T09:14:22Z","timestamp":1696497262000},"page":"2406","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["PolyQ-Expansion Causes Mitochondria Fragmentation Independent of Huntingtin and Is Distinct from Traumatic Brain Injury (TBI)\/Mechanical Stress-Mediated Fragmentation Which Results from Cell Death"],"prefix":"10.3390","volume":"12","author":[{"given":"Kelsey","family":"Swinter","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dania","family":"Salah","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rasika","family":"Rathnayake","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8776-9397","authenticated-orcid":false,"given":"Shermali","family":"Gunawardena","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1126\/science.1219855","article-title":"Mitochondrial Fission, Fusion, and Stress","volume":"337","author":"Youle","year":"2012","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"24","DOI":"10.3389\/fncel.2016.00024","article-title":"Alterations in Mitochondrial Quality Control in Alzheimer\u2019s Disease","volume":"10","author":"Cai","year":"2016","journal-title":"Front. Cell. Neurosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1126\/science.1171091","article-title":"S-nitrosylation of Drp1 mediates \u03b2-amyloid-related mitochondrial fission and neuronal injury","volume":"324","author":"Cho","year":"2009","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1089\/ars.2012.4928","article-title":"S-nitrosylation of dynamin-related protein 1 mediates mutant huntingtin-induced mitochondrial fragmentation and neuronal injury in Huntington\u2019s disease","volume":"19","author":"Haun","year":"2013","journal-title":"Antioxid. Redox Signal"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1038\/nrm3013","article-title":"Mitochondrial fusion and fission in cell life and death","volume":"11","author":"Westermann","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1002\/emmm.201000102","article-title":"Mitochondrial fission and cristae disruption increase the response of cell models of Huntington\u2019s disease to apoptotic stimuli","volume":"2","author":"Costa","year":"2010","journal-title":"EMBO Mol. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/nm.2313","article-title":"Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity","volume":"17","author":"Song","year":"2011","journal-title":"Nat. Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1042\/BST20191283","article-title":"Exaggerated mitophagy: A weapon of striatal destruction in the brain?","volume":"48","author":"Subramaniam","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Czeredys, M. (2020). Dysregulation of Neuronal Calcium Signaling via Store-Operated Channels in Huntington\u2019s Disease. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.611735"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5780","DOI":"10.1074\/jbc.M704704200","article-title":"Calcium Homeostasis and Mitochondrial Dysfunction in Striatal Neurons of Huntington Disease","volume":"283","author":"Lim","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1038\/ng.2732","article-title":"Glutathione peroxidase activity is neuroprotective in models of Huntington\u2019s disease","volume":"45","author":"Mason","year":"2013","journal-title":"Nat. Genet."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1093\/hmg\/ddq253","article-title":"Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease","volume":"19","author":"Underwood","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1534\/genetics.111.133710","article-title":"Huntingtin Aggregation Kinetics and Their Pathological Role in a Drosophila Huntington\u2019s Disease Model","volume":"190","author":"Weiss","year":"2012","journal-title":"Genetics"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.neuron.2007.11.025","article-title":"Suppression of Neurodegeneration and Increased Neurotransmission Caused by Expanded Full-Length Huntingtin Accumulating in the Cytoplasm","volume":"57","author":"Romero","year":"2008","journal-title":"Neuron"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1534\/genetics.109.112516","article-title":"A Genomewide RNA Interference Screen for Modifiers of Aggregates Formation by Mutant Huntingtin in Drosophila","volume":"184","author":"Zhang","year":"2010","journal-title":"Genetics"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2657","DOI":"10.1093\/hmg\/11.21.2657","article-title":"Suppression of polyglutamine toxicity by a Drosophila homolog of myeloid leukemia factor 1","volume":"11","author":"Benzer","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1098\/rstb.1999.0458","article-title":"A genetic model for human polyglutamine-repeat disease in Drosophila melanogaster","volume":"354","author":"Bonini","year":"1999","journal-title":"Philos. Trans. R. Soc. B Biol. Sci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0896-6273(03)00594-4","article-title":"Disruption of Axonal Transport by Loss of Huntingtin or Expression of Pathogenic PolyQ Proteins in Drosophila","volume":"40","author":"Gunawardena","year":"2003","journal-title":"Neuron"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1038\/s41419-021-04046-3","article-title":"Differential mitochondrial roles for \u03b1-synuclein in DRP1-dependent fission and PINK1\/Parkin-mediated oxidation","volume":"12","author":"Krzystek","year":"2021","journal-title":"Cell Death Dis."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"13614","DOI":"10.1038\/s41598-021-92738-3","article-title":"Drosophila tubulin polymerization promoting protein mutants reveal pathological correlates relevant to human Parkinson\u2019s disease","volume":"11","author":"Xie","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.mito.2015.11.005","article-title":"Analysis of mitochondrial structure and function in the Drosophila larval musculature","volume":"26","author":"Wang","year":"2016","journal-title":"Mitochondrion"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1083\/jcb.130.1.157","article-title":"Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis","volume":"130","author":"Petit","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1016\/j.bbadis.2011.08.012","article-title":"Brain aging, Alzheimer\u2019s disease, and mitochondria","volume":"1812","author":"Swerdlow","year":"2011","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.1073\/pnas.0913485107","article-title":"Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin","volume":"107","author":"Ziviani","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"103702","DOI":"10.1016\/j.isci.2021.103702","article-title":"Transposable element activation promotes neurodegeneration in a Drosophila model of Huntington\u2019s disease","volume":"25","author":"Casale","year":"2022","journal-title":"iScience"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s10495-019-01520-4","article-title":"Excess active P13K rescues huntingtin-mediated neuronal cell deathbut has no effect on axonal transport defects","volume":"24","author":"Hansen","year":"2019","journal-title":"Apoptosis"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1093\/hmg\/ddu504","article-title":"Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington\u2019s disease","volume":"24","author":"Barbaro","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1080\/15548627.2022.2119351","article-title":"HTT (huntingtin) and RAB7 co-migrate retrogradely on a signaling LAMP1-containing late endosome during axonal injury","volume":"19","author":"Krzystek","year":"2023","journal-title":"Autophagy"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1093\/hmg\/2.10.1535","article-title":"Molecular analysis of juvenile Huntington disease: The major influence on (CAG) n repeat length is the sex of the affected parent","volume":"2","author":"Telenius","year":"1993","journal-title":"Hum. Mol. Genet."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"3231","DOI":"10.1083\/jcb.201612106","article-title":"Mitochondrial fission facilitates the selective mitophagy of protein aggregates","volume":"216","author":"Burman","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"34460","DOI":"10.1074\/jbc.M113.513903","article-title":"Ubiquitination regulates the neuroprotective function of the deubiquitinase ataxin-3 in vivo","volume":"288","author":"Tsou","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/70532","article-title":"Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70","volume":"23","author":"Warrick","year":"1999","journal-title":"Nat. Genet."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1126\/science.1067389","article-title":"Chaperone suppression of \u03b1-synuclein toxicity in a Drosophila model for Parkinson\u2019s disease","volume":"295","author":"Auluck","year":"2002","journal-title":"Science"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/502","article-title":"Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1","volume":"19","author":"Cummings","year":"1998","journal-title":"Nat. Genet."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1083\/jcb.200212059","article-title":"Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol","volume":"160","author":"Breckenridge","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Hemmings, B.A., and Restuccia, D.F. (2012). PI3K-PKB\/Akt Pathway. Cold Spring Harb. Perspect. Biol., 4.","DOI":"10.1101\/cshperspect.a011189"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"e03558","DOI":"10.7554\/eLife.03558","article-title":"Mitochondrial fusion but not fission regulates larval growth and synaptic development through steroid hormone production","volume":"3","author":"Sandoval","year":"2014","journal-title":"eLife"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"19777","DOI":"10.1073\/pnas.0605907103","article-title":"Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking","volume":"103","author":"Iwakiri","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"25252","DOI":"10.1038\/srep25252","article-title":"Using Drosophila as an integrated model to study mild repetitive traumatic brain injury","volume":"6","author":"Barekat","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1111\/j.1469-7793.2000.00057.x","article-title":"Mitochondria and calcium: From cell signalling to cell death","volume":"529","author":"Duchen","year":"2000","journal-title":"Physiol. J."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/sj.emboj.7601963","article-title":"Fission and selective fusion govern mitochondrial segregation and elimination by autophagy","volume":"27","author":"Twig","year":"2008","journal-title":"EMBO J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"7862","DOI":"10.1523\/JNEUROSCI.22-18-07862.2002","article-title":"Caspase Cleavage of Mutant Huntingtin Precedes Neurodegeneration in Huntington\u2019s Disease","volume":"22","author":"Wellington","year":"2002","journal-title":"J. Neurosci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/j.cell.2006.04.026","article-title":"Cleavage at the Caspase-6 Site Is Required for Neuronal Dysfunction and Degeneration Due to Mutant Huntingtin","volume":"125","author":"Graham","year":"2006","journal-title":"Cell"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1093\/hmg\/ddh162","article-title":"Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release","volume":"13","author":"Choo","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2783","DOI":"10.1523\/JNEUROSCI.0106-08.2008","article-title":"N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking","volume":"28","author":"Orr","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"36464","DOI":"10.1074\/jbc.M503672200","article-title":"Huntingtin associates with acidic phospholipids at the plasma membrane","volume":"280","author":"Kegel","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"e1617","DOI":"10.1038\/cddis.2014.581","article-title":"PINK1-induced mitophagy promotes neuroprotection in Huntington\u2019s disease","volume":"6","author":"Khalil","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.cell.2006.09.015","article-title":"Transcriptional repression of PGC-1\u03b1 by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration","volume":"127","author":"Cui","year":"2006","journal-title":"Cell"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"749","DOI":"10.4103\/1673-5374.249218","article-title":"Mitophagy links oxidative stress conditions and neurodegenerative diseases","volume":"14","author":"Shefa","year":"2019","journal-title":"Neural Regen. Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"329","DOI":"10.3389\/fnmol.2018.00329","article-title":"A mitochondria-associated oxidative stress perspective on Huntington\u2019s disease","volume":"11","author":"Zheng","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.bbrc.2006.01.007","article-title":"Polyglutamine expansion inhibits respiration by increasing reactive oxygen species in isolated mitochondria","volume":"341","author":"Puranam","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.mito.2017.03.001","article-title":"Evidence of oxidative stress and mitochondrial dysfunction in spinocerebellar ataxia type 2 (SCA2) patient fibroblasts: Effect of coenzyme Q10 supplementation on these parameters","volume":"34","author":"Cornelius","year":"2017","journal-title":"Mitochondrion"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1016\/j.celrep.2017.10.097","article-title":"Spatiotemporal proteomic profiling of Huntington\u2019s disease inclusions reveals widespread loss of protein function","volume":"21","author":"Hosp","year":"2017","journal-title":"Cell Rep."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1002\/jnr.24263","article-title":"Purkinje cell COX deficiency and mtDNA depletion in an animal model of spinocerebellar ataxia type 1","volume":"96","author":"Ripolone","year":"2018","journal-title":"J. Neurosci. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5418","DOI":"10.1038\/s41598-020-62308-0","article-title":"Hippocampal mitochondrial dysfunction and psychiatric-relevant behavioral deficits in spinocerebellar ataxia 1 mouse model","volume":"10","author":"Tichanek","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/j.celrep.2019.01.028","article-title":"Metabolic and organelle morphology defects in mice and human patients define spinocerebellar ataxia type 7 as a mitochondrial disease","volume":"26","author":"Ward","year":"2019","journal-title":"Cell Rep."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"196","DOI":"10.3389\/fnmol.2017.00196","article-title":"The truncated C-terminal fragment of mutant ATXN3 disrupts mitochondria dynamics in spinocerebellar ataxia type 3 models","volume":"10","author":"Hsu","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/S0006-8993(02)02550-7","article-title":"Altered neuronal nitric oxide synthase expression contributes to disease progression in Huntington\u2019s disease transgenic mice","volume":"939","author":"Deckel","year":"2002","journal-title":"Brain Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1750-3639.2004.tb00053.x","article-title":"Nitric Oxide in Traumatic Brain Injury","volume":"14","author":"Cherian","year":"2004","journal-title":"Brain Pathol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"e001474","DOI":"10.1161\/JAHA.114.001474","article-title":"Traumatic brain injury disrupts cerebrovascular tone through endothelial inducible nitric oxide synthase expression and nitric oxide gain of function","volume":"3","author":"Villalba","year":"2014","journal-title":"J. Am. Heart Assoc."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/ncb1268","article-title":"S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding","volume":"7","author":"Hara","year":"2005","journal-title":"Nat. Cell Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1046\/j.1471-4159.1999.0721843.x","article-title":"Analysis of the neuroprotective effects of various nitric oxide donor compounds in murine mixed cortical cell culture","volume":"72","author":"Vidwans","year":"1999","journal-title":"J. Neurochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1096\/fj.09-148601","article-title":"Suppression of polyglutamine-induced cytotoxicity in Saccharomyces cerevisiae by enhancement of mitochondrial biogenesis","volume":"24","author":"Ocampo","year":"2010","journal-title":"FASEB J."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Poole, A.C., Thomas, R.E., Yu, S., Vincow, E.S., and Pallanck, L. (2010). The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1\/parkin pathway. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010054"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 years of image analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/19\/2406\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:01:30Z","timestamp":1760130090000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/19\/2406"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10,5]]},"references-count":65,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2023,10]]}},"alternative-id":["cells12192406"],"URL":"https:\/\/doi.org\/10.3390\/cells12192406","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,10,5]]}}}