{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T03:04:41Z","timestamp":1792033481621,"version":"4.4.0"},"reference-count":229,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2022,10,29]],"date-time":"2022-10-29T00:00:00Z","timestamp":1667001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2022,10,29]],"date-time":"2022-10-29T00:00:00Z","timestamp":1667001600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["129584"],"award-info":[{"award-number":["129584"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell. Mol. Life Sci."],"published-print":{"date-parts":[[2022,11]]},"DOI":"10.1007\/s00018-022-04604-8","type":"journal-article","created":{"date-parts":[[2022,10,29]],"date-time":"2022-10-29T15:04:06Z","timestamp":1667055846000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Mitochondrial proteotoxicity: implications and ubiquitin-dependent quality control mechanisms"],"prefix":"10.1007","volume":"79","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4336-5187","authenticated-orcid":false,"given":"Mariusz","family":"Karbowski","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yumiko","family":"Oshima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolas","family":"Verhoeven","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,10,29]]},"reference":[{"key":"4604_CR1","first-page":"3","volume":"44","author":"RZ Zhao","year":"2019","unstructured":"Zhao RZ, Jiang S, Zhang L, Yu ZB (2019) Mitochondrial electron transport chain, ROS generation and uncoupling (review). Int J Mol Med 44:3\u201315","journal-title":"Int J Mol Med"},{"key":"4604_CR2","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1038\/s42255-019-0126-8","volume":"1","author":"AP Wescott","year":"2019","unstructured":"Wescott AP, Kao JPY, Lederer WJ, Boyman L (2019) Voltage-energized calcium-sensitive ATP production by mitochondria. Nat Metab 1:975\u2013984","journal-title":"Nat Metab"},{"key":"4604_CR3","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.3390\/cells10051164","volume":"10","author":"AS Pitt","year":"2021","unstructured":"Pitt AS, Buchanan SK (2021) A biochemical and structural understanding of TOM complex interactions and implications for human health and disease. Cells 10:1164","journal-title":"Cells"},{"key":"4604_CR4","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1091\/mbc.e12-10-0721","volume":"24","author":"OC Loson","year":"2013","unstructured":"Loson OC, Song Z, Chen H, Chan DC (2013) Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol Biol Cell 24:659\u2013667","journal-title":"Mol Biol Cell"},{"key":"4604_CR5","doi-asserted-by":"publisher","first-page":"1141","DOI":"10.1083\/jcb.201007152","volume":"191","author":"H Otera","year":"2010","unstructured":"Otera H, Wang C, Cleland MM, Setoguchi K, Yokota S, Youle RJ, Mihara K (2010) Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J Cell Biol 191:1141\u20131158","journal-title":"J Cell Biol"},{"key":"4604_CR6","doi-asserted-by":"publisher","first-page":"27584","DOI":"10.1074\/jbc.M113.479873","volume":"288","author":"CS Palmer","year":"2013","unstructured":"Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT (2013) Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission. J Biol Chem 288:27584\u201327593","journal-title":"J Biol Chem"},{"key":"4604_CR7","doi-asserted-by":"publisher","first-page":"3177","DOI":"10.1038\/onc.2011.497","volume":"31","author":"C Wang","year":"2012","unstructured":"Wang C, Youle RJ (2012) Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1\u2019s inhibitory effect on Bak. Oncogene 31:3177\u20133189","journal-title":"Oncogene"},{"key":"4604_CR8","doi-asserted-by":"publisher","first-page":"957","DOI":"10.1038\/bjc.2015.85","volume":"112","author":"J Lopez","year":"2015","unstructured":"Lopez J, Tait SW (2015) Mitochondrial apoptosis: killing cancer using the enemy within. Br J Cancer 112:957\u2013962","journal-title":"Br J Cancer"},{"key":"4604_CR9","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1038\/cdd.2017.186","volume":"25","author":"J Kale","year":"2018","unstructured":"Kale J, Osterlund EJ, Andrews DW (2018) BCL-2 family proteins: changing partners in the dance towards death. Cell Death Differ 25:65\u201380","journal-title":"Cell Death Differ"},{"key":"4604_CR10","doi-asserted-by":"publisher","first-page":"13057","DOI":"10.3390\/ijms222313057","volume":"22","author":"W Kang","year":"2021","unstructured":"Kang W, Suzuki M, Saito T, Miyado K (2021) Emerging role of TCA cycle-related enzymes in human diseases. Int J Mol Sci 22:13057","journal-title":"Int J Mol Sci"},{"issue":"Pt 2","key":"4604_CR11","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1042\/bj3200345","volume":"320","author":"S Eaton","year":"1996","unstructured":"Eaton S, Bartlett K, Pourfarzam M (1996) Mammalian mitochondrial beta-oxidation. Biochem J 320(Pt 2):345\u2013357","journal-title":"Biochem J"},{"key":"4604_CR12","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/j.bbabio.2009.09.005","volume":"1797","author":"HA Tuppen","year":"2010","unstructured":"Tuppen HA, Blakely EL, Turnbull DM, Taylor RW (2010) Mitochondrial DNA mutations and human disease. Biochim Biophys Acta 1797:113\u2013128","journal-title":"Biochim Biophys Acta"},{"key":"4604_CR13","doi-asserted-by":"publisher","first-page":"100","DOI":"10.3389\/fcell.2019.00100","volume":"7","author":"E Vringer","year":"2019","unstructured":"Vringer E, Tait SWG (2019) Mitochondria and inflammation: cell death heats up. Front Cell Dev Biol 7:100","journal-title":"Front Cell Dev Biol"},{"key":"4604_CR14","doi-asserted-by":"publisher","first-page":"1062","DOI":"10.1126\/science.1219855","volume":"337","author":"RJ Youle","year":"2012","unstructured":"Youle RJ, van der Bliek AM (2012) Mitochondrial fission, fusion, and stress. Science 337:1062\u20131065","journal-title":"Science"},{"key":"4604_CR15","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1038\/nature12985","volume":"505","author":"JR Friedman","year":"2014","unstructured":"Friedman JR, Nunnari J (2014) Mitochondrial form and function. Nature 505:335\u2013343","journal-title":"Nature"},{"key":"4604_CR16","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.58041","author":"SM Nowinski","year":"2020","unstructured":"Nowinski SM, Solmonson A, Rusin SF, Maschek JA, Bensard CL, Fogarty S, Jeong MY, Lettlova S, Berg JA, Morgan JT, Ouyang Y, Naylor BC, Paulo JA, Funai K, Cox JE, Gygi SP, Winge DR, DeBerardinis RJ, Rutter J (2020) Mitochondrial fatty acid synthesis coordinates oxidative metabolism in mammalian mitochondria. Elife. https:\/\/doi.org\/10.7554\/eLife.58041","journal-title":"Elife"},{"key":"4604_CR17","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1146\/annurev-biochem-013118-111540","volume":"89","author":"R Lill","year":"2020","unstructured":"Lill R, Freibert SA (2020) Mechanisms of mitochondrial iron-sulfur protein biogenesis. Annu Rev Biochem 89:471\u2013499","journal-title":"Annu Rev Biochem"},{"key":"4604_CR18","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1083\/jcb.201606069","volume":"214","author":"B Mesmin","year":"2016","unstructured":"Mesmin B (2016) Mitochondrial lipid transport and biosynthesis: a complex balance. J Cell Biol 214:9\u201311","journal-title":"J Cell Biol"},{"key":"4604_CR19","doi-asserted-by":"publisher","first-page":"8220","DOI":"10.1007\/s12035-019-01665-y","volume":"56","author":"P Martin-Maestro","year":"2019","unstructured":"Martin-Maestro P, Sproul A, Martinez H, Paquet D, Gerges M, Noggle S, Starkov AA (2019) Autophagy induction by bexarotene promotes mitophagy in presenilin 1 familial Alzheimer\u2019s disease iPSC-derived neural stem cells. Mol Neurobiol 56:8220\u20138236","journal-title":"Mol Neurobiol"},{"key":"4604_CR20","doi-asserted-by":"publisher","first-page":"5993","DOI":"10.1016\/S0021-9258(18)62653-5","volume":"245","author":"JA Watson","year":"1970","unstructured":"Watson JA, Lowenstein JM (1970) Citrate and the conversion of carbohydrate into fat. Fatty acid synthesis by a combination of cytoplasm and mitochondria. J Biol Chem 245:5993\u20136002","journal-title":"J Biol Chem"},{"key":"4604_CR21","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1038\/35004029","volume":"2","author":"JC Goldstein","year":"2000","unstructured":"Goldstein JC, Waterhouse NJ, Juin P, Evan GI, Green DR (2000) The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat Cell Biol 2:156\u2013162","journal-title":"Nat Cell Biol"},{"key":"4604_CR22","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1007\/978-1-4419-6706-0_8","volume":"687","author":"M Karbowski","year":"2010","unstructured":"Karbowski M (2010) Mitochondria on guard: role of mitochondrial fusion and fission in the regulation of apoptosis. Adv Exp Med Biol 687:131\u2013142","journal-title":"Adv Exp Med Biol"},{"key":"4604_CR23","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/S1534-5807(01)00116-2","volume":"2","author":"L Scorrano","year":"2002","unstructured":"Scorrano L, Ashiya M, Buttle K, Weiler S, Oakes SA, Mannella CA, Korsmeyer SJ (2002) A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev Cell 2:55\u201367","journal-title":"Dev Cell"},{"key":"4604_CR24","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1016\/j.neurobiolaging.2021.07.017","volume":"107","author":"J Burtscher","year":"2021","unstructured":"Burtscher J, Syed MMK, Keller MA, Lashuel HA, Millet GP (2021) Fatal attraction: the role of hypoxia when alpha-synuclein gets intimate with mitochondria. Neurobiol Aging 107:128\u2013141","journal-title":"Neurobiol Aging"},{"key":"4604_CR25","doi-asserted-by":"publisher","first-page":"9832","DOI":"10.3390\/ijms22189832","volume":"22","author":"M Jankovic","year":"2021","unstructured":"Jankovic M, Novakovic I, Gamil ADP, Gamil ADA, Drinic A, Abdel Motaleb FI, Ducic S, Nikolic D (2021) Current concepts on genetic aspects of mitochondrial dysfunction in amyotrophic lateral sclerosis. Int J Mol Sci 22:9832","journal-title":"Int J Mol Sci"},{"key":"4604_CR26","doi-asserted-by":"publisher","first-page":"11520","DOI":"10.3390\/ijms222111520","volume":"22","author":"A Johri","year":"2021","unstructured":"Johri A (2021) Disentangling mitochondria in Alzheimer\u2019s disease. Int J Mol Sci 22:11520","journal-title":"Int J Mol Sci"},{"key":"4604_CR27","doi-asserted-by":"publisher","DOI":"10.1007\/s12035-021-02556-x","author":"N Sawant","year":"2021","unstructured":"Sawant N, Morton H, Kshirsagar S, Reddy AP, Reddy PH (2021) Mitochondrial abnormalities and synaptic damage in Huntington\u2019s disease: a focus on defective mitophagy and mitochondria-targeted therapeutics. Mol Neurobiol. https:\/\/doi.org\/10.1007\/s12035-021-02556-x","journal-title":"Mol Neurobiol"},{"key":"4604_CR28","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuint.2021.105147","volume":"149","author":"I Sonsky","year":"2021","unstructured":"Sonsky I, Vodicka P, Vodickova Kepkova K, Hansikova H (2021) Mitophagy in Huntington\u2019s disease. Neurochem Int 149:105147","journal-title":"Neurochem Int"},{"key":"4604_CR29","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1038\/nm.4130","volume":"22","author":"W Wang","year":"2016","unstructured":"Wang W, Wang L, Lu J, Siedlak SL, Fujioka H, Liang J, Jiang S, Ma X, Jiang Z, da Rocha EL, Sheng M, Choi H, Lerou PH, Li H, Wang X (2016) The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity. Nat Med 22:869\u2013878","journal-title":"Nat Med"},{"key":"4604_CR30","doi-asserted-by":"publisher","DOI":"10.1038\/emm.2014.117","volume":"47","author":"A Ciechanover","year":"2015","unstructured":"Ciechanover A, Kwon YT (2015) Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp Mol Med 47:e147","journal-title":"Exp Mol Med"},{"key":"4604_CR31","doi-asserted-by":"publisher","first-page":"1097","DOI":"10.1038\/s41467-018-03509-0","volume":"9","author":"TA Thibaudeau","year":"2018","unstructured":"Thibaudeau TA, Anderson RT, Smith DM (2018) A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers. Nat Commun 9:1097","journal-title":"Nat Commun"},{"key":"4604_CR32","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1159\/000367694","volume":"14","author":"C Zheng","year":"2014","unstructured":"Zheng C, Geetha T, Babu JR (2014) Failure of ubiquitin proteasome system: risk for neurodegenerative diseases. Neurodegener Dis 14:161\u2013175","journal-title":"Neurodegener Dis"},{"key":"4604_CR33","doi-asserted-by":"publisher","first-page":"303","DOI":"10.3389\/fnagi.2016.00303","volume":"8","author":"Q Zheng","year":"2016","unstructured":"Zheng Q, Huang T, Zhang L, Zhou Y, Luo H, Xu H, Wang X (2016) Dysregulation of ubiquitin-proteasome system in neurodegenerative diseases. Front Aging Neurosci 8:303","journal-title":"Front Aging Neurosci"},{"key":"4604_CR34","doi-asserted-by":"publisher","first-page":"5789","DOI":"10.3390\/molecules25245789","volume":"25","author":"Z Breijyeh","year":"2020","unstructured":"Breijyeh Z, Karaman R (2020) Comprehensive review on Alzheimer\u2019s disease: causes and treatment. Molecules 25:5789","journal-title":"Molecules"},{"key":"4604_CR35","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1038\/s41572-021-00269-y","volume":"7","author":"DS Knopman","year":"2021","unstructured":"Knopman DS, Amieva H, Petersen RC, Chetelat G, Holtzman DM, Hyman BT, Nixon RA, Jones DT (2021) Alzheimer disease. Nat Rev Dis Primers 7:33","journal-title":"Nat Rev Dis Primers"},{"key":"4604_CR36","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1212\/WNL.0000000000011415","volume":"96","author":"DS Knopman","year":"2021","unstructured":"Knopman DS, Jagust WJ (2021) Alzheimer disease spectrum: syndrome and etiology from clinical and PET imaging perspectives. Neurology 96:299\u2013300","journal-title":"Neurology"},{"key":"4604_CR37","doi-asserted-by":"publisher","first-page":"3017","DOI":"10.1523\/JNEUROSCI.21-09-03017.2001","volume":"21","author":"K Hirai","year":"2001","unstructured":"Hirai K, Aliev G, Nunomura A, Fujioka H, Russell RL, Atwood CS, Johnson AB, Kress Y, Vinters HV, Tabaton M, Shimohama S, Cash AD, Siedlak SL, Harris PL, Jones PK, Petersen RB, Perry G, Smith MA (2001) Mitochondrial abnormalities in Alzheimer\u2019s disease. J Neurosci 21:3017\u20133023","journal-title":"J Neurosci"},{"key":"4604_CR38","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1042\/BST20170501","volume":"46","author":"R Macdonald","year":"2018","unstructured":"Macdonald R, Barnes K, Hastings C, Mortiboys H (2018) Mitochondrial abnormalities in Parkinson\u2019s disease and Alzheimer\u2019s disease: can mitochondria be targeted therapeutically? Biochem Soc Trans 46:891\u2013909","journal-title":"Biochem Soc Trans"},{"key":"4604_CR39","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.mito.2020.08.003","volume":"55","author":"P Pantiya","year":"2020","unstructured":"Pantiya P, Thonusin C, Chattipakorn N, Chattipakorn SC (2020) Mitochondrial abnormalities in neurodegenerative models and possible interventions: focus on Alzheimer\u2019s disease, Parkinson\u2019s disease, Huntington\u2019s disease. Mitochondrion 55:14\u201347","journal-title":"Mitochondrion"},{"key":"4604_CR40","doi-asserted-by":"publisher","first-page":"1403","DOI":"10.3233\/JAD-170585","volume":"62","author":"RH Swerdlow","year":"2018","unstructured":"Swerdlow RH (2018) Mitochondria and mitochondrial cascades in Alzheimer\u2019s disease. J Alzheimers Dis 62:1403\u20131416","journal-title":"J Alzheimers Dis"},{"key":"4604_CR41","doi-asserted-by":"publisher","first-page":"9090","DOI":"10.1523\/JNEUROSCI.1357-09.2009","volume":"29","author":"X Wang","year":"2009","unstructured":"Wang X, Su B, Lee HG, Li X, Perry G, Smith MA, Zhu X (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer\u2019s disease. J Neurosci 29:9090\u20139103","journal-title":"J Neurosci"},{"key":"4604_CR42","doi-asserted-by":"publisher","first-page":"1324","DOI":"10.1111\/ene.15246","volume":"29","author":"T Terada","year":"2022","unstructured":"Terada T, Therriault J, Kang MS, Savard M, Pascoal TA, Lussier F, Tissot C, Wang YT, Benedet A, Poltronetti NM, Ottoy J, Arias JF, Bezgin G, Matsudaira T, Bunai T, Obi T, Tsukada H, Ouchi Y, Rosa-Neto P (2022) Mitochondrial complex I abnormalities underlie neurodegeneration and cognitive decline in Alzheimer\u2019s disease. Eur J Neurol 29:1324\u20131334","journal-title":"Eur J Neurol"},{"key":"4604_CR43","doi-asserted-by":"publisher","first-page":"1587","DOI":"10.3390\/biomedicines9111587","volume":"9","author":"PJ Yao","year":"2021","unstructured":"Yao PJ, Eren E, Goetzl EJ, Kapogiannis D (2021) Mitochondrial electron transport chain protein abnormalities detected in plasma extracellular vesicles in Alzheimer\u2019s disease. Biomedicines. 9:1587","journal-title":"Biomedicines."},{"key":"4604_CR44","doi-asserted-by":"publisher","first-page":"2040","DOI":"10.1096\/fj.05-3735fje","volume":"19","author":"C Caspersen","year":"2005","unstructured":"Caspersen C, Wang N, Yao J, Sosunov A, Chen X, Lustbader JW, Xu HW, Stern D, McKhann G, Yan SD (2005) Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer\u2019s disease. FASEB J 19:2040\u20132041","journal-title":"FASEB J"},{"key":"4604_CR45","doi-asserted-by":"publisher","first-page":"1437","DOI":"10.1093\/hmg\/ddl066","volume":"15","author":"M Manczak","year":"2006","unstructured":"Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, Reddy PH (2006) Mitochondria are a direct site of A beta accumulation in Alzheimer\u2019s disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15:1437\u20131449","journal-title":"Hum Mol Genet"},{"key":"4604_CR46","doi-asserted-by":"publisher","first-page":"13145","DOI":"10.1073\/pnas.0806192105","volume":"105","author":"CA Hansson Petersen","year":"2008","unstructured":"Hansson Petersen CA, Alikhani N, Behbahani H, Wiehager B, Pavlov PF, Alafuzoff I, Leinonen V, Ito A, Winblad B, Glaser E, Ankarcrona M (2008) The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci USA 105:13145\u201313150","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR47","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1038\/nature12748","volume":"504","author":"SA Hasson","year":"2013","unstructured":"Hasson SA, Kane LA, Yamano K, Huang CH, Sliter DA, Buehler E, Wang C, Heman-Ackah SM, Hessa T, Guha R, Martin SE, Youle RJ (2013) High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy. Nature 504:291\u2013295","journal-title":"Nature"},{"key":"4604_CR48","doi-asserted-by":"publisher","first-page":"12681","DOI":"10.1074\/jbc.RA118.002713","volume":"293","author":"W Hu","year":"2018","unstructured":"Hu W, Wang Z, Zheng H (2018) Mitochondrial accumulation of amyloid beta (Abeta) peptides requires TOMM22 as a main Abeta receptor in yeast. J Biol Chem 293:12681\u201312689","journal-title":"J Biol Chem"},{"key":"4604_CR49","doi-asserted-by":"publisher","first-page":"9057","DOI":"10.1523\/JNEUROSCI.1469-06.2006","volume":"26","author":"L Devi","year":"2006","unstructured":"Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK (2006) Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer\u2019s disease brain is associated with mitochondrial dysfunction. J Neurosci 26:9057\u20139068","journal-title":"J Neurosci"},{"key":"4604_CR50","doi-asserted-by":"publisher","first-page":"3257","DOI":"10.1091\/mbc.E16-05-0313","volume":"27","author":"G Cenini","year":"2016","unstructured":"Cenini G, Rub C, Bruderek M, Voos W (2016) Amyloid beta-peptides interfere with mitochondrial preprotein import competence by a coaggregation process. Mol Biol Cell 27:3257\u20133272","journal-title":"Mol Biol Cell"},{"key":"4604_CR51","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1126\/science.1091230","volume":"304","author":"JW Lustbader","year":"2004","unstructured":"Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, Caspersen C, Chen X, Pollak S, Chaney M, Trinchese F, Liu S, Gunn-Moore F, Lue LF, Walker DG, Kuppusamy P, Zewier ZL, Arancio O, Stern D, Yan SS, Wu H (2004) ABAD directly links Abeta to mitochondrial toxicity in Alzheimer\u2019s disease. Science 304:448\u2013452","journal-title":"Science"},{"key":"4604_CR52","doi-asserted-by":"publisher","first-page":"19318","DOI":"10.1073\/pnas.0804871105","volume":"105","author":"X Wang","year":"2008","unstructured":"Wang X, Su B, Siedlak SL, Moreira PI, Fujioka H, Wang Y, Casadesus G, Zhu X (2008) Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission\/fusion proteins. Proc Natl Acad Sci USA 105:19318\u201319323","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR53","doi-asserted-by":"publisher","first-page":"1874","DOI":"10.1212\/WNL.0b013e3182929fc3","volume":"80","author":"M Benatar","year":"2013","unstructured":"Benatar M, Wuu J, Fernandez C, Weihl CC, Katzen H, Steele J, Oskarsson B, Taylor JP (2013) Motor neuron involvement in multisystem proteinopathy: implications for ALS. Neurology 80:1874\u20131880","journal-title":"Neurology"},{"key":"4604_CR54","doi-asserted-by":"publisher","first-page":"835","DOI":"10.1016\/j.neuron.2010.05.024","volume":"66","author":"L Chakrabarti","year":"2010","unstructured":"Chakrabarti L, Zahra R, Jackson SM, Kazemi-Esfarjani P, Sopher BL, Mason AG, Toneff T, Ryu S, Shaffer S, Kansy JW, Eng J, Merrihew G, MacCoss MJ, Murphy A, Goodlett DR, Hook V, Bennett CL, Pallanck LJ, La Spada AR (2010) Mitochondrial dysfunction in NnaD mutant flies and Purkinje cell degeneration mice reveals a role for Nna proteins in neuronal bioenergetics. Neuron 66:835\u2013847","journal-title":"Neuron"},{"key":"4604_CR55","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1038\/nature10353","volume":"477","author":"HX Deng","year":"2011","unstructured":"Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, Yang Y, Fecto F, Shi Y, Zhai H, Jiang H, Hirano M, Rampersaud E, Jansen GH, Donkervoort S, Bigio EH, Brooks BR, Ajroud K, Sufit RL, Haines JL, Mugnaini E, Pericak-Vance MA, Siddique T (2011) Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS\/dementia. Nature 477:211\u2013215","journal-title":"Nature"},{"key":"4604_CR56","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1016\/j.neuron.2010.11.036","volume":"68","author":"JO Johnson","year":"2010","unstructured":"Johnson JO, Mandrioli J, Benatar M, Abramzon Y, Van Deerlin VM, Trojanowski JQ, Gibbs JR, Brunetti M, Gronka S, Wuu J, Ding J, McCluskey L, Martinez-Lage M, Falcone D, Hernandez DG, Arepalli S, Chong S, Schymick JC, Rothstein J, Landi F, Wang YD, Calvo A, Mora G, Sabatelli M, Monsurro MR, Battistini S, Salvi F, Spataro R, Sola P, Borghero G, Consortium I, Galassi G, Scholz SW, Taylor JP, Restagno G, Chio A, Traynor BJ (2010) Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron 68:857\u2013864","journal-title":"Neuron"},{"key":"4604_CR57","doi-asserted-by":"publisher","first-page":"1230","DOI":"10.1093\/hmg\/ddab116","volume":"30","author":"BC Lin","year":"2021","unstructured":"Lin BC, Phung TH, Higgins NR, Greenslade JE, Prado MA, Finley D, Karbowski M, Polster BM, Monteiro MJ (2021) ALS\/FTD mutations in UBQLN2 are linked to mitochondrial dysfunction through loss-of-function in mitochondrial protein import. Hum Mol Genet 30:1230\u20131246","journal-title":"Hum Mol Genet"},{"issue":"636\u2013649","key":"4604_CR58","volume":"183","author":"CH Yu","year":"2020","unstructured":"Yu CH, Davidson S, Harapas CR, Hilton JB, Mlodzianoski MJ, Laohamonthonkul P, Louis C, Low RRJ, Moecking J, De Nardo D, Balka KR, Calleja DJ, Moghaddas F, Ni E, McLean CA, Samson AL, Tyebji S, Tonkin CJ, Bye CR, Turner BJ, Pepin G, Gantier MP, Rogers KL, McArthur K, Crouch PJ, Masters SL (2020) TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate cGAS\/STING in ALS. Cell 183(636\u2013649):e18","journal-title":"Cell"},{"key":"4604_CR59","doi-asserted-by":"publisher","first-page":"1652","DOI":"10.1038\/s12276-020-00513-7","volume":"52","author":"M Jo","year":"2020","unstructured":"Jo M, Lee S, Jeon YM, Kim S, Kwon Y, Kim HJ (2020) The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies. Exp Mol Med 52:1652\u20131662","journal-title":"Exp Mol Med"},{"key":"4604_CR60","doi-asserted-by":"publisher","first-page":"851","DOI":"10.1007\/s00439-016-1683-5","volume":"135","author":"T Geuens","year":"2016","unstructured":"Geuens T, Bouhy D, Timmerman V (2016) The hnRNP family: insights into their role in health and disease. Hum Genet 135:851\u2013867","journal-title":"Hum Genet"},{"key":"4604_CR61","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","volume":"351","author":"T Arai","year":"2006","unstructured":"Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, Mann D, Tsuchiya K, Yoshida M, Hashizume Y, Oda T (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351:602\u2013611","journal-title":"Biochem Biophys Res Commun"},{"key":"4604_CR62","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.neulet.2018.04.053","volume":"678","author":"SA Davis","year":"2018","unstructured":"Davis SA, Itaman S, Khalid-Janney CM, Sherard JA, Dowell JA, Cairns NJ, Gitcho MA (2018) TDP-43 interacts with mitochondrial proteins critical for mitophagy and mitochondrial dynamics. Neurosci Lett 678:8\u201315","journal-title":"Neurosci Lett"},{"key":"4604_CR63","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1007947","volume":"15","author":"P Wang","year":"2019","unstructured":"Wang P, Deng J, Dong J, Liu J, Bigio EH, Mesulam M, Wang T, Sun L, Wang L, Lee AY, McGee WA, Chen X, Fushimi K, Zhu L, Wu JY (2019) TDP-43 induces mitochondrial damage and activates the mitochondrial unfolded protein response. PLoS Genet 15:e1007947","journal-title":"PLoS Genet"},{"key":"4604_CR64","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1016\/j.celrep.2013.06.007","volume":"4","author":"T Nonaka","year":"2013","unstructured":"Nonaka T, Masuda-Suzukake M, Arai T, Hasegawa Y, Akatsu H, Obi T, Yoshida M, Murayama S, Mann DM, Akiyama H, Hasegawa M (2013) Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 4:124\u2013134","journal-title":"Cell Rep"},{"key":"4604_CR65","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1016\/j.bbrc.2020.01.099","volume":"524","author":"T Shimizu","year":"2020","unstructured":"Shimizu T, Kozuka Y, Kusano M, Nagane M, Yamashita T, Hachiya N (2020) PrP (122\u2013139) is a covert mitochondrial targeting signal of prion protein and it specifically triggers the perinuclear clustering of mitochondria in neuronal culture cells. Biochem Biophys Res Commun 524:301\u2013307","journal-title":"Biochem Biophys Res Commun"},{"key":"4604_CR66","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.bbrc.2021.09.040","volume":"578","author":"DV Laurents","year":"2021","unstructured":"Laurents DV, Stuani C, Pantoja-Uceda D, Buratti E, Mompean M (2021) Aromatic and aliphatic residues of the disordered region of TDP-43 are on a fast track for self-assembly. Biochem Biophys Res Commun 578:110\u2013114","journal-title":"Biochem Biophys Res Commun"},{"key":"4604_CR67","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1091\/mbc.e10-09-0748","volume":"22","author":"S Xu","year":"2011","unstructured":"Xu S, Peng G, Wang Y, Fang S, Karbowski M (2011) The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Mol Biol Cell 22:291\u2013300","journal-title":"Mol Biol Cell"},{"key":"4604_CR68","doi-asserted-by":"publisher","first-page":"1367","DOI":"10.1083\/jcb.201007013","volume":"191","author":"A Tanaka","year":"2010","unstructured":"Tanaka A, Cleland MM, Xu S, Narendra DP, Suen DF, Karbowski M, Youle RJ (2010) Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J Cell Biol 191:1367\u20131380","journal-title":"J Cell Biol"},{"key":"4604_CR69","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/j.biocel.2014.02.018","volume":"50","author":"KY Zhang","year":"2014","unstructured":"Zhang KY, Yang S, Warraich ST, Blair IP (2014) Ubiquilin 2: a component of the ubiquitin-proteasome system with an emerging role in neurodegeneration. Int J Biochem Cell Biol 50:123\u2013126","journal-title":"Int J Biochem Cell Biol"},{"key":"4604_CR70","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/j.molcel.2016.05.020","volume":"63","author":"E Itakura","year":"2016","unstructured":"Itakura E, Zavodszky E, Shao S, Wohlever ML, Keenan RJ, Hegde RS (2016) Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation. Mol Cell 63:21\u201333","journal-title":"Mol Cell"},{"key":"4604_CR71","doi-asserted-by":"publisher","first-page":"1642","DOI":"10.1016\/S0140-6736(03)13304-1","volume":"361","author":"G Bates","year":"2003","unstructured":"Bates G (2003) Huntingtin aggregation and toxicity in Huntington\u2019s disease. Lancet 361:1642\u20131644","journal-title":"Lancet"},{"key":"4604_CR72","doi-asserted-by":"publisher","first-page":"a007476","DOI":"10.1101\/cshperspect.a007476","volume":"3","author":"S Finkbeiner","year":"2011","unstructured":"Finkbeiner S (2011) Huntington\u2019s disease. Cold Spring Harb Perspect Biol 3:a007476","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"4604_CR73","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.neuron.2012.05.024","volume":"75","author":"DI Shirasaki","year":"2012","unstructured":"Shirasaki DI, Greiner ER, Al-Ramahi I, Gray M, Boontheung P, Geschwind DH, Botas J, Coppola G, Horvath S, Loo JA, Yang XW (2012) Network organization of the huntingtin proteomic interactome in mammalian brain. Neuron 75:41\u201357","journal-title":"Neuron"},{"key":"4604_CR74","doi-asserted-by":"publisher","first-page":"9895","DOI":"10.1523\/JNEUROSCI.6223-10.2011","volume":"31","author":"AM Pickrell","year":"2011","unstructured":"Pickrell AM, Fukui H, Wang X, Pinto M, Moraes CT (2011) The striatum is highly susceptible to mitochondrial oxidative phosphorylation dysfunctions. J Neurosci 31:9895\u20139904","journal-title":"J Neurosci"},{"key":"4604_CR75","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1093\/hmg\/ddn404","volume":"18","author":"H Wang","year":"2009","unstructured":"Wang H, Lim PJ, Karbowski M, Monteiro MJ (2009) Effects of overexpression of huntingtin proteins on mitochondrial integrity. Hum Mol Genet 18:737\u2013752","journal-title":"Hum Mol Genet"},{"key":"4604_CR76","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1038\/nm.2313","volume":"17","author":"W Song","year":"2011","unstructured":"Song W, Chen J, Petrilli A, Liot G, Klinglmayr E, Zhou Y, Poquiz P, Tjong J, Pouladi MA, Hayden MR, Masliah E, Ellisman M, Rouiller I, Schwarzenbacher R, Bossy B, Perkins G, Bossy-Wetzel E (2011) Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat Med 17:377\u2013382","journal-title":"Nat Med"},{"key":"4604_CR77","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1007\/s00702-009-0328-4","volume":"117","author":"F Squitieri","year":"2010","unstructured":"Squitieri F, Falleni A, Cannella M, Orobello S, Fulceri F, Lenzi P, Fornai F (2010) Abnormal morphology of peripheral cell tissues from patients with Huntington disease. J Neural Transm (Vienna) 117:77\u201383","journal-title":"J Neural Transm (Vienna)"},{"key":"4604_CR78","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1471-4159.2010.06741.x","volume":"114","author":"JM Oliveira","year":"2010","unstructured":"Oliveira JM (2010) Nature and cause of mitochondrial dysfunction in Huntington\u2019s disease: focusing on huntingtin and the striatum. J Neurochem 114:1\u201312","journal-title":"J Neurochem"},{"key":"4604_CR79","doi-asserted-by":"publisher","first-page":"16593","DOI":"10.1073\/pnas.1904101116","volume":"116","author":"S Yablonska","year":"2019","unstructured":"Yablonska S, Ganesan V, Ferrando LM, Kim J, Pyzel A, Baranova OV, Khattar NK, Larkin TM, Baranov SV, Chen N, Strohlein CE, Stevens DA, Wang X, Chang YF, Schurdak ME, Carlisle DL, Minden JS, Friedlander RM (2019) Mutant huntingtin disrupts mitochondrial proteostasis by interacting with TIM23. Proc Natl Acad Sci USA 116:16593\u201316602","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR80","doi-asserted-by":"publisher","first-page":"2484","DOI":"10.1016\/j.bbadis.2015.08.012","volume":"1852","author":"P Guedes-Dias","year":"2015","unstructured":"Guedes-Dias P, de Proenca J, Soares TR, Leitao-Rocha A, Pinho BR, Duchen MR, Oliveira JM (2015) HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons. Biochim Biophys Acta 1852:2484\u20132493","journal-title":"Biochim Biophys Acta"},{"key":"4604_CR81","doi-asserted-by":"publisher","first-page":"652","DOI":"10.1111\/jnc.13165","volume":"134","author":"JJ Pellman","year":"2015","unstructured":"Pellman JJ, Hamilton J, Brustovetsky T, Brustovetsky N (2015) Ca(2+) handling in isolated brain mitochondria and cultured neurons derived from the YAC128 mouse model of Huntington\u2019s disease. J Neurochem 134:652\u2013667","journal-title":"J Neurochem"},{"key":"4604_CR82","doi-asserted-by":"publisher","first-page":"8314","DOI":"10.3390\/ijms21218314","volume":"21","author":"M Bozzi","year":"2020","unstructured":"Bozzi M, Sciandra F (2020) Molecular mechanisms underlying muscle wasting in Huntington\u2019s disease. Int J Mol Sci 21:8314","journal-title":"Int J Mol Sci"},{"key":"4604_CR83","doi-asserted-by":"publisher","first-page":"3719","DOI":"10.3390\/ijms21103719","volume":"21","author":"S Stanga","year":"2020","unstructured":"Stanga S, Caretto A, Boido M, Vercelli A (2020) Mitochondrial dysfunctions: a red thread across neurodegenerative diseases. Int J Mol Sci 21:3719","journal-title":"Int J Mol Sci"},{"key":"4604_CR84","doi-asserted-by":"publisher","first-page":"650","DOI":"10.1038\/s41586-021-04059-0","volume":"599","author":"P Gonzalez-Rodriguez","year":"2021","unstructured":"Gonzalez-Rodriguez P, Zampese E, Stout KA, Guzman JN, Ilijic E, Yang B, Tkatch T, Stavarache MA, Wokosin DL, Gao L, Kaplitt MG, Lopez-Barneo J, Schumacker PT, Surmeier DJ (2021) Disruption of mitochondrial complex I induces progressive parkinsonism. Nature 599:650\u2013656","journal-title":"Nature"},{"key":"4604_CR85","doi-asserted-by":"publisher","first-page":"1508","DOI":"10.3390\/biom11101508","volume":"11","author":"A Picca","year":"2021","unstructured":"Picca A, Guerra F, Calvani R, Romano R, Coelho-Junior HJ, Bucci C, Marzetti E (2021) Mitochondrial dysfunction, protein misfolding and neuroinflammation in Parkinson\u2019s disease: roads to biomarker discovery. Biomolecules 11:1508","journal-title":"Biomolecules"},{"key":"4604_CR86","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1038\/nature14893","volume":"524","author":"M Lazarou","year":"2015","unstructured":"Lazarou M, Sliter DA, Kane LA, Sarraf SA, Wang C, Burman JL, Sideris DP, Fogel AI, Youle RJ (2015) The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy. Nature 524:309\u2013314","journal-title":"Nature"},{"key":"4604_CR87","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1083\/jcb.200809125","volume":"183","author":"D Narendra","year":"2008","unstructured":"Narendra D, Tanaka A, Suen DF, Youle RJ (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183:795\u2013803","journal-title":"J Cell Biol"},{"key":"4604_CR88","doi-asserted-by":"publisher","first-page":"706","DOI":"10.4161\/auto.5.5.8505","volume":"5","author":"D Narendra","year":"2009","unstructured":"Narendra D, Tanaka A, Suen DF, Youle RJ (2009) Parkin-induced mitophagy in the pathogenesis of Parkinson disease. Autophagy 5:706\u2013708","journal-title":"Autophagy"},{"key":"4604_CR89","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/j.conb.2021.09.005","volume":"72","author":"S Agarwal","year":"2021","unstructured":"Agarwal S, Muqit MMK (2021) PTEN-induced kinase 1 (PINK1) and Parkin: unlocking a mitochondrial quality control pathway linked to Parkinson\u2019s disease. Curr Opin Neurobiol 72:111\u2013119","journal-title":"Curr Opin Neurobiol"},{"key":"4604_CR90","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1016\/j.ceb.2011.05.007","volume":"23","author":"M Karbowski","year":"2011","unstructured":"Karbowski M, Youle RJ (2011) Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr Opin Cell Biol 23:476\u2013482","journal-title":"Curr Opin Cell Biol"},{"key":"4604_CR91","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.636506","volume":"9","author":"V Nicoletti","year":"2021","unstructured":"Nicoletti V, Palermo G, Del Prete E, Mancuso M, Ceravolo R (2021) Understanding the multiple role of mitochondria in Parkinson\u2019s disease and related disorders: lesson from genetics and protein-interaction network. Front Cell Dev Biol 9:636506","journal-title":"Front Cell Dev Biol"},{"key":"4604_CR92","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1038\/s41556-018-0176-2","volume":"20","author":"K Palikaras","year":"2018","unstructured":"Palikaras K, Lionaki E, Tavernarakis N (2018) Mechanisms of mitophagy in cellular homeostasis, physiology and pathology. Nat Cell Biol 20:1013\u20131022","journal-title":"Nat Cell Biol"},{"key":"4604_CR93","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1161\/CIRCULATIONAHA.118.037417","volume":"139","author":"C Hofmann","year":"2019","unstructured":"Hofmann C, Katus HA, Doroudgar S (2019) Protein misfolding in cardiac disease. Circulation 139:2085\u20132088","journal-title":"Circulation"},{"key":"4604_CR94","doi-asserted-by":"publisher","first-page":"821","DOI":"10.4161\/auto.6502","volume":"4","author":"JS Pattison","year":"2008","unstructured":"Pattison JS, Robbins J (2008) Protein misfolding and cardiac disease: establishing cause and effect. Autophagy 4:821\u2013823","journal-title":"Autophagy"},{"key":"4604_CR95","doi-asserted-by":"publisher","first-page":"H1220","DOI":"10.1152\/ajpheart.00601.2011","volume":"301","author":"PM McLendon","year":"2011","unstructured":"McLendon PM, Robbins J (2011) Desmin-related cardiomyopathy: an unfolding story. Am J Physiol Heart Circ Physiol 301:H1220\u2013H1228","journal-title":"Am J Physiol Heart Circ Physiol"},{"key":"4604_CR96","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1111\/j.1750-3639.2009.00289.x","volume":"19","author":"R Schroder","year":"2009","unstructured":"Schroder R, Schoser B (2009) Myofibrillar myopathies: a clinical and myopathological guide. Brain Pathol 19:483\u2013492","journal-title":"Brain Pathol"},{"key":"4604_CR97","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.yexcr.2004.08.004","volume":"301","author":"D Paulin","year":"2004","unstructured":"Paulin D, Li Z (2004) Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp Cell Res 301:1\u20137","journal-title":"Exp Cell Res"},{"key":"4604_CR98","doi-asserted-by":"publisher","first-page":"16835","DOI":"10.1073\/pnas.1908263116","volume":"116","author":"N Kedia","year":"2019","unstructured":"Kedia N, Arhzaouy K, Pittman SK, Sun Y, Batchelor M, Weihl CC, Bieschke J (2019) Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibers. Proc Natl Acad Sci USA 116:16835\u201316840","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR99","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1007\/s00401-016-1592-7","volume":"132","author":"L Winter","year":"2016","unstructured":"Winter L, Wittig I, Peeva V, Eggers B, Heidler J, Chevessier F, Kley RA, Barkovits K, Strecker V, Berwanger C, Herrmann H, Marcus K, Kornblum C, Kunz WS, Schroder R, Clemen CS (2016) Mutant desmin substantially perturbs mitochondrial morphology, function and maintenance in skeletal muscle tissue. Acta Neuropathol 132:453\u2013473","journal-title":"Acta Neuropathol"},{"key":"4604_CR100","doi-asserted-by":"publisher","DOI":"10.1161\/JAHA.118.009289","author":"S Alam","year":"2018","unstructured":"Alam S, Abdullah CS, Aishwarya R, Miriyala S, Panchatcharam M, Peretik JM, Orr AW, James J, Robbins J, Bhuiyan MS (2018) Aberrant mitochondrial fission is maladaptive in desmin mutation-induced cardiac proteotoxicity. J Am Heart Assoc. https:\/\/doi.org\/10.1161\/JAHA.118.009289","journal-title":"J Am Heart Assoc"},{"key":"4604_CR101","doi-asserted-by":"publisher","first-page":"5284","DOI":"10.1172\/JCI70877","volume":"123","author":"MS Bhuiyan","year":"2013","unstructured":"Bhuiyan MS, Pattison JS, Osinska H, James J, Gulick J, McLendon PM, Hill JA, Sadoshima J, Robbins J (2013) Enhanced autophagy ameliorates cardiac proteinopathy. J Clin Invest 123:5284\u20135297","journal-title":"J Clin Invest"},{"key":"4604_CR102","doi-asserted-by":"publisher","first-page":"8122","DOI":"10.3390\/ijms21218122","volume":"21","author":"AA Dayal","year":"2020","unstructured":"Dayal AA, Medvedeva NV, Nekrasova TM, Duhalin SD, Surin AK, Minin AA (2020) Desmin interacts directly with mitochondria. Int J Mol Sci 21:8122","journal-title":"Int J Mol Sci"},{"key":"4604_CR103","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1161\/CIRCULATIONAHA.119.044948","volume":"141","author":"JH Park","year":"2020","unstructured":"Park JH, Kim DH, Park YG, Kwon DY, Choi M, Jung JH, Han K (2020) Association of Parkinson disease with risk of cardiovascular disease and all-cause mortality: a nationwide, population-based cohort study. Circulation 141:1205\u20131207","journal-title":"Circulation"},{"key":"4604_CR104","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jocn.2018.04.031","volume":"53","author":"FA Scorza","year":"2018","unstructured":"Scorza FA, Fiorini AC, Scorza CA, Finsterer J (2018) Cardiac abnormalities in Parkinson\u2019s disease and Parkinsonism. J Clin Neurosci 53:1\u20135","journal-title":"J Clin Neurosci"},{"key":"4604_CR105","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1080\/01616412.2017.1390933","volume":"40","author":"J Piqueras-Flores","year":"2018","unstructured":"Piqueras-Flores J, Lopez-Garcia A, Moreno-Reig A, Gonzalez-Martinez A, Hernandez-Gonzalez A, Vaamonde-Gamo J, Jurado-Roman A (2018) Structural and functional alterations of the heart in Parkinson\u2019s disease. Neurol Res 40:53\u201361","journal-title":"Neurol Res"},{"key":"4604_CR106","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1074\/jbc.M112.411363","volume":"288","author":"DA Kubli","year":"2013","unstructured":"Kubli DA, Zhang X, Lee Y, Hanna RA, Quinsay MN, Nguyen CK, Jimenez R, Petrosyan S, Murphy AN, Gustafsson AB (2013) Parkin protein deficiency exacerbates cardiac injury and reduces survival following myocardial infarction. J Biol Chem 288:915\u2013926","journal-title":"J Biol Chem"},{"key":"4604_CR107","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1161\/CIRCRESAHA.117.306859","volume":"117","author":"M Song","year":"2015","unstructured":"Song M, Gong G, Burelle Y, Gustafsson AB, Kitsis RN, Matkovich SJ, Dorn GW 2nd (2015) Interdependence of Parkin-mediated mitophagy and mitochondrial fission in adult mouse hearts. Circ Res 117:346\u2013351","journal-title":"Circ Res"},{"key":"4604_CR108","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.yjmcc.2015.11.023","volume":"95","author":"GW Dorn 2nd","year":"2016","unstructured":"Dorn GW 2nd (2016) Parkin-dependent mitophagy in the heart. J Mol Cell Cardiol 95:42\u201349","journal-title":"J Mol Cell Cardiol"},{"key":"4604_CR109","doi-asserted-by":"publisher","first-page":"3791","DOI":"10.1007\/s00018-021-03772-3","volume":"78","author":"RA Gottlieb","year":"2021","unstructured":"Gottlieb RA, Piplani H, Sin J, Sawaged S, Hamid SM, Taylor DJ, de Freitas Germano J (2021) At the heart of mitochondrial quality control: many roads to the top. Cell Mol Life Sci 78:3791\u20133801","journal-title":"Cell Mol Life Sci"},{"key":"4604_CR110","doi-asserted-by":"publisher","first-page":"15019","DOI":"10.1038\/nrdp.2015.19","volume":"1","author":"RA DeFronzo","year":"2015","unstructured":"DeFronzo RA, Ferrannini E, Groop L, Henry RR, Herman WH, Holst JJ, Hu FB, Kahn CR, Raz I, Shulman GI, Simonson DC, Testa MA, Weiss R (2015) Type 2 diabetes mellitus. Nat Rev Dis Primers 1:15019","journal-title":"Nat Rev Dis Primers"},{"key":"4604_CR111","doi-asserted-by":"publisher","first-page":"266","DOI":"10.3892\/etm.2020.9396","volume":"20","author":"W Sha","year":"2020","unstructured":"Sha W, Hu F, Bu S (2020) Mitochondrial dysfunction and pancreatic islet beta-cell failure (review). Exp Ther Med 20:266","journal-title":"Exp Ther Med"},{"key":"4604_CR112","doi-asserted-by":"publisher","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","volume":"84","author":"P Westermark","year":"1987","unstructured":"Westermark P, Wernstedt C, Wilander E, Hayden DW, O\u2019Brien TD, Johnson KH (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci USA 84:3881\u20133885","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR113","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1517\/03009734000000014","volume":"77","author":"P Westermark","year":"1972","unstructured":"Westermark P (1972) Quantitative studies on amyloid in the islets of Langerhans. Ups J Med Sci 77:91\u201394","journal-title":"Ups J Med Sci"},{"key":"4604_CR114","doi-asserted-by":"publisher","first-page":"3629","DOI":"10.1210\/jc.2004-0405","volume":"89","author":"RL Hull","year":"2004","unstructured":"Hull RL, Westermark GT, Westermark P, Kahn SE (2004) Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes. J Clin Endocrinol Metab 89:3629\u20133643","journal-title":"J Clin Endocrinol Metab"},{"key":"4604_CR115","doi-asserted-by":"publisher","first-page":"1621","DOI":"10.1002\/pmic.200900651","volume":"10","author":"YA Lim","year":"2010","unstructured":"Lim YA, Rhein V, Baysang G, Meier F, Poljak A, Raftery MJ, Guilhaus M, Ittner LM, Eckert A, Gotz J (2010) Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction. Proteomics 10:1621\u20131633","journal-title":"Proteomics"},{"key":"4604_CR116","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1080\/15548627.2018.1446627","volume":"14","author":"G Pearson","year":"2018","unstructured":"Pearson G, Soleimanpour SA (2018) A ubiquitin-dependent mitophagy complex maintains mitochondrial function and insulin secretion in beta cells. Autophagy 14:1160\u20131161","journal-title":"Autophagy"},{"key":"4604_CR117","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1038\/s41419-018-0533-x","volume":"9","author":"MG Hernandez","year":"2018","unstructured":"Hernandez MG, Aguilar AG, Burillo J, Oca RG, Manca MA, Novials A, Alcarraz-Vizan G, Guillen C, Benito M (2018) Pancreatic beta cells overexpressing hIAPP impaired mitophagy and unbalanced mitochondrial dynamics. Cell Death Dis 9:481","journal-title":"Cell Death Dis"},{"key":"4604_CR118","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1016\/j.ajhg.2009.07.009","volume":"85","author":"H Tyynismaa","year":"2009","unstructured":"Tyynismaa H, Ylikallio E, Patel M, Molnar MJ, Haller RG, Suomalainen A (2009) A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. Am J Hum Genet 85:290\u2013295","journal-title":"Am J Hum Genet"},{"key":"4604_CR119","doi-asserted-by":"publisher","first-page":"9103","DOI":"10.1073\/pnas.0402959101","volume":"101","author":"RM Canet-Aviles","year":"2004","unstructured":"Canet-Aviles RM, Wilson MA, Miller DW, Ahmad R, McLendon C, Bandyopadhyay S, Baptista MJ, Ringe D, Petsko GA, Cookson MR (2004) The Parkinson\u2019s disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci USA 101:9103\u20139108","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR120","doi-asserted-by":"publisher","DOI":"10.1155\/2010\/737385","volume":"2010","author":"P Smits","year":"2010","unstructured":"Smits P, Smeitink J, van den Heuvel L (2010) Mitochondrial translation and beyond: processes implicated in combined oxidative phosphorylation deficiencies. J Biomed Biotechnol 2010:737385","journal-title":"J Biomed Biotechnol"},{"key":"4604_CR121","doi-asserted-by":"publisher","DOI":"10.1038\/cddis.2014.112","volume":"5","author":"A Sheth","year":"2014","unstructured":"Sheth A, Escobar-Alvarez S, Gardner J, Ran L, Heaney ML, Scheinberg DA (2014) Inhibition of human mitochondrial peptide deformylase causes apoptosis in c-myc-overexpressing hematopoietic cancers. Cell Death Dis 5:e1152","journal-title":"Cell Death Dis"},{"key":"4604_CR122","doi-asserted-by":"publisher","first-page":"4331","DOI":"10.1242\/jcs.131888","volume":"126","author":"BJ Battersby","year":"2013","unstructured":"Battersby BJ, Richter U (2013) Why translation counts for mitochondria - retrograde signalling links mitochondrial protein synthesis to mitochondrial biogenesis and cell proliferation. J Cell Sci 126:4331\u20134338","journal-title":"J Cell Sci"},{"key":"4604_CR123","doi-asserted-by":"publisher","first-page":"1309","DOI":"10.1016\/j.cmet.2018.04.011","volume":"27","author":"T Suhm","year":"2018","unstructured":"Suhm T, Kaimal JM, Dawitz H, Peselj C, Masser AE, Hanzen S, Ambrozic M, Smialowska A, Bjorck ML, Brzezinski P, Nystrom T, Buttner S, Andreasson C, Ott M (2018) Mitochondrial translation efficiency controls cytoplasmic protein homeostasis. Cell Metab 27:1309-1322 e6","journal-title":"Cell Metab"},{"key":"4604_CR124","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1111\/1567-1364.12134","volume":"14","author":"M Breitenbach","year":"2014","unstructured":"Breitenbach M, Rinnerthaler M, Hartl J, Stincone A, Vowinckel J, Breitenbach-Koller H, Ralser M (2014) Mitochondria in ageing: there is metabolism beyond the ROS. FEMS Yeast Res 14:198\u2013212","journal-title":"FEMS Yeast Res"},{"key":"4604_CR125","doi-asserted-by":"publisher","first-page":"390","DOI":"10.1016\/j.molcel.2011.03.021","volume":"42","author":"A Caballero","year":"2011","unstructured":"Caballero A, Ugidos A, Liu B, Oling D, Kvint K, Hao X, Mignat C, Nachin L, Molin M, Nystrom T (2011) Absence of mitochondrial translation control proteins extends life span by activating sirtuin-dependent silencing. Mol Cell 42:390\u2013400","journal-title":"Mol Cell"},{"key":"4604_CR126","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1016\/j.ccr.2011.10.015","volume":"20","author":"M Skrtic","year":"2011","unstructured":"Skrtic M, Sriskanthadevan S, Jhas B, Gebbia M, Wang X, Wang Z, Hurren R, Jitkova Y, Gronda M, Maclean N, Lai CK, Eberhard Y, Bartoszko J, Spagnuolo P, Rutledge AC, Datti A, Ketela T, Moffat J, Robinson BH, Cameron JH, Wrana J, Eaves CJ, Minden MD, Wang JC, Dick JE, Humphries K, Nislow C, Giaever G, Schimmer AD (2011) Inhibition of mitochondrial translation as a therapeutic strategy for human acute myeloid leukemia. Cancer Cell 20:674\u2013688","journal-title":"Cancer Cell"},{"key":"4604_CR127","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1016\/j.cub.2013.02.019","volume":"23","author":"U Richter","year":"2013","unstructured":"Richter U, Lahtinen T, Marttinen P, Myohanen M, Greco D, Cannino G, Jacobs HT, Lietzen N, Nyman TA, Battersby BJ (2013) A mitochondrial ribosomal and RNA decay pathway blocks cell proliferation. Curr Biol 23:535\u2013541","journal-title":"Curr Biol"},{"key":"4604_CR128","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1083\/jcb.201504062","volume":"211","author":"U Richter","year":"2015","unstructured":"Richter U, Lahtinen T, Marttinen P, Suomi F, Battersby BJ (2015) Quality control of mitochondrial protein synthesis is required for membrane integrity and cell fitness. J Cell Biol 211:373\u2013389","journal-title":"J Cell Biol"},{"key":"4604_CR129","doi-asserted-by":"publisher","first-page":"3231","DOI":"10.1083\/jcb.201612106","volume":"216","author":"JL Burman","year":"2017","unstructured":"Burman JL, Pickles S, Wang C, Sekine S, Vargas JNS, Zhang Z, Youle AM, Nezich CL, Wu X, Hammer JA, Youle RJ (2017) Mitochondrial fission facilitates the selective mitophagy of protein aggregates. J Cell Biol 216:3231\u20133247","journal-title":"J Cell Biol"},{"key":"4604_CR130","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1038\/s41593-018-0332-9","volume":"22","author":"EF Fang","year":"2019","unstructured":"Fang EF, Hou Y, Palikaras K, Adriaanse BA, Kerr JS, Yang B, Lautrup S, Hasan-Olive MM, Caponio D, Dan X, Rocktaschel P, Croteau DL, Akbari M, Greig NH, Fladby T, Nilsen H, Cader MZ, Mattson MP, Tavernarakis N, Bohr VA (2019) Mitophagy inhibits amyloid-beta and tau pathology and reverses cognitive deficits in models of Alzheimer\u2019s disease. Nat Neurosci 22:401\u2013412","journal-title":"Nat Neurosci"},{"key":"4604_CR131","doi-asserted-by":"publisher","first-page":"106233","DOI":"10.18632\/oncotarget.22287","volume":"8","author":"FC Fiesel","year":"2017","unstructured":"Fiesel FC, James ED, Hudec R, Springer W (2017) Mitochondrial targeted HSP90 inhibitor Gamitrinib-TPP (G-TPP) induces PINK1\/Parkin-dependent mitophagy. Oncotarget 8:106233\u2013106248","journal-title":"Oncotarget"},{"key":"4604_CR132","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1038\/nature18302","volume":"534","author":"C Munch","year":"2016","unstructured":"Munch C, Harper JW (2016) Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation. Nature 534:710\u2013713","journal-title":"Nature"},{"key":"4604_CR133","doi-asserted-by":"publisher","first-page":"1349","DOI":"10.1172\/JCI44855","volume":"121","author":"MD Siegelin","year":"2011","unstructured":"Siegelin MD, Dohi T, Raskett CM, Orlowski GM, Powers CM, Gilbert CA, Ross AH, Plescia J, Altieri DC (2011) Exploiting the mitochondrial unfolded protein response for cancer therapy in mice and human cells. J Clin Invest 121:1349\u20131360","journal-title":"J Clin Invest"},{"key":"4604_CR134","doi-asserted-by":"publisher","first-page":"3321","DOI":"10.1182\/blood-2011-02-340075","volume":"119","author":"SH Bernstein","year":"2012","unstructured":"Bernstein SH, Venkatesh S, Li M, Lee J, Lu B, Hilchey SP, Morse KM, Metcalfe HM, Skalska J, Andreeff M, Brookes PS, Suzuki CK (2012) The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives. Blood 119:3321\u20133329","journal-title":"Blood"},{"key":"4604_CR135","doi-asserted-by":"publisher","DOI":"10.1038\/s41401-021-00782-6","author":"J Dong","year":"2021","unstructured":"Dong J, Zhang KJ, Li GC, Chen XR, Lin JJ, Li JW, Lv ZY, Deng ZZ, Dai J, Cao W, Jiang Q (2021) CDDO-Im ameliorates osteoarthritis and inhibits chondrocyte apoptosis in mice via enhancing Nrf2-dependent autophagy. Acta Pharmacol Sin. https:\/\/doi.org\/10.1038\/s41401-021-00782-6","journal-title":"Acta Pharmacol Sin"},{"key":"4604_CR136","doi-asserted-by":"publisher","first-page":"4411","DOI":"10.1093\/emboj\/cdf445","volume":"21","author":"Q Zhao","year":"2002","unstructured":"Zhao Q, Wang J, Levichkin IV, Stasinopoulos S, Ryan MT, Hoogenraad NJ (2002) A mitochondrial specific stress response in mammalian cells. EMBO J 21:4411\u20134419","journal-title":"EMBO J"},{"key":"4604_CR137","doi-asserted-by":"publisher","first-page":"17397","DOI":"10.1038\/srep17397","volume":"5","author":"A Bezawork-Geleta","year":"2015","unstructured":"Bezawork-Geleta A, Brodie EJ, Dougan DA, Truscott KN (2015) LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins. Sci Rep 5:17397","journal-title":"Sci Rep"},{"key":"4604_CR138","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1146\/annurev-biochem-061516-044916","volume":"86","author":"TET Mevissen","year":"2017","unstructured":"Mevissen TET, Komander D (2017) Mechanisms of deubiquitinase specificity and regulation. Annu Rev Biochem 86:159\u2013192","journal-title":"Annu Rev Biochem"},{"key":"4604_CR139","doi-asserted-by":"publisher","first-page":"2953","DOI":"10.1042\/BCJ20160783","volume":"474","author":"L Stach","year":"2017","unstructured":"Stach L, Freemont PS (2017) The AAA+ ATPase p97, a cellular multitool. Biochem J 474:2953\u20132976","journal-title":"Biochem J"},{"key":"4604_CR140","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1083\/jcb.200611064","volume":"178","author":"M Karbowski","year":"2007","unstructured":"Karbowski M, Neutzner A, Youle RJ (2007) The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J Cell Biol 178:71\u201384","journal-title":"J Cell Biol"},{"key":"4604_CR141","doi-asserted-by":"publisher","first-page":"3618","DOI":"10.1038\/sj.emboj.7601249","volume":"25","author":"R Yonashiro","year":"2006","unstructured":"Yonashiro R, Ishido S, Kyo S, Fukuda T, Goto E, Matsuki Y, Ohmura-Hoshino M, Sada K, Hotta H, Yamamura H, Inatome R, Yanagi S (2006) A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J 25:3618\u20133626","journal-title":"EMBO J"},{"key":"4604_CR142","doi-asserted-by":"publisher","first-page":"1458","DOI":"10.1038\/emboj.2010.39","volume":"29","author":"G Benard","year":"2010","unstructured":"Benard G, Neutzner A, Peng G, Wang C, Livak F, Youle RJ, Karbowski M (2010) IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO J 29:1458\u20131471","journal-title":"EMBO J"},{"key":"4604_CR143","doi-asserted-by":"publisher","first-page":"3755","DOI":"10.1038\/s41467-018-05722-3","volume":"9","author":"A Di Rita","year":"2018","unstructured":"Di Rita A, Peschiaroli A, D\u2019Acunzo P, Strobbe D, Hu Z, Gruber J, Nygaard M, Lambrughi M, Melino G, Papaleo E, Dengjel J, El Alaoui S, Campanella M, Dotsch V, Rogov VV, Strappazzon F, Cecconi F (2018) HUWE1 E3 ligase promotes PINK1\/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKalpha. Nat Commun 9:3755","journal-title":"Nat Commun"},{"key":"4604_CR144","doi-asserted-by":"publisher","first-page":"370","DOI":"10.1038\/nature13418","volume":"510","author":"B Bingol","year":"2014","unstructured":"Bingol B, Tea JS, Phu L, Reichelt M, Bakalarski CE, Song Q, Foreman O, Kirkpatrick DS, Sheng M (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510:370\u2013375","journal-title":"Nature"},{"key":"4604_CR145","doi-asserted-by":"publisher","first-page":"618","DOI":"10.15252\/embr.201439820","volume":"16","author":"JR Liang","year":"2015","unstructured":"Liang JR, Martinez A, Lane JD, Mayor U, Clague MJ, Urbe S (2015) USP30 deubiquitylates mitochondrial Parkin substrates and restricts apoptotic cell death. EMBO Rep 16:618\u2013627","journal-title":"EMBO Rep"},{"key":"4604_CR146","doi-asserted-by":"publisher","first-page":"1903","DOI":"10.1091\/mbc.e07-11-1103","volume":"19","author":"N Nakamura","year":"2008","unstructured":"Nakamura N, Hirose S (2008) Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane. Mol Biol Cell 19:1903\u20131911","journal-title":"Mol Biol Cell"},{"key":"4604_CR147","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1038\/nature08646","volume":"463","author":"M Schwickart","year":"2010","unstructured":"Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM, Maecker H, O\u2019Rourke K, Bazan F, Eastham-Anderson J, Yue P, Dornan D, Huang DC, Dixit VM (2010) Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463:103\u2013107","journal-title":"Nature"},{"key":"4604_CR148","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.32866","author":"GL McLelland","year":"2018","unstructured":"McLelland GL, Goiran T, Yi W, Dorval G, Chen CX, Lauinger ND, Krahn AI, Valimehr S, Rakovic A, Rouiller I, Durcan TM, Trempe JF, Fon EA (2018) Mfn2 ubiquitination by PINK1\/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy. Elife. https:\/\/doi.org\/10.7554\/eLife.32866","journal-title":"Elife"},{"key":"4604_CR149","doi-asserted-by":"publisher","first-page":"14970","DOI":"10.1073\/pnas.1920109117","volume":"117","author":"DT Castanzo","year":"2020","unstructured":"Castanzo DT, LaFrance B, Martin A (2020) The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity. Proc Natl Acad Sci USA 117:14970\u201314977","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR150","doi-asserted-by":"publisher","first-page":"1548","DOI":"10.15252\/embj.201487943","volume":"33","author":"YC Chen","year":"2014","unstructured":"Chen YC, Umanah GK, Dephoure N, Andrabi SA, Gygi SP, Dawson TM, Dawson VL, Rutter J (2014) Msp1\/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins. EMBO J 33:1548\u20131564","journal-title":"EMBO J"},{"key":"4604_CR151","doi-asserted-by":"publisher","first-page":"8019","DOI":"10.1073\/pnas.1405755111","volume":"111","author":"V Okreglak","year":"2014","unstructured":"Okreglak V, Walter P (2014) The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins. Proc Natl Acad Sci USA 111:8019\u20138024","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR152","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1038\/nature09732","volume":"471","author":"H Inuzuka","year":"2011","unstructured":"Inuzuka H, Shaik S, Onoyama I, Gao D, Tseng A, Maser RS, Zhai B, Wan L, Gutierrez A, Lau AW, Xiao Y, Christie AL, Aster J, Settleman J, Gygi SP, Kung AL, Look T, Nakayama KI, DePinho RA, Wei W (2011) SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature 471:104\u2013109","journal-title":"Nature"},{"key":"4604_CR153","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1016\/j.semcdb.2012.03.019","volume":"23","author":"A Neutzner","year":"2012","unstructured":"Neutzner A, Li S, Xu S, Karbowski M (2012) The ubiquitin\/proteasome system-dependent control of mitochondrial steps in apoptosis. Semin Cell Dev Biol 23:499\u2013508","journal-title":"Semin Cell Dev Biol"},{"key":"4604_CR154","doi-asserted-by":"publisher","first-page":"900","DOI":"10.1038\/cr.2008.75","volume":"18","author":"B Zhang","year":"2008","unstructured":"Zhang B, Huang J, Li HL, Liu T, Wang YY, Waterman P, Mao AP, Xu LG, Zhai Z, Liu D, Marrack P, Shu HB (2008) GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth. Cell Res 18:900\u2013910","journal-title":"Cell Res"},{"key":"4604_CR155","doi-asserted-by":"publisher","first-page":"748","DOI":"10.1038\/embor.2009.86","volume":"10","author":"E Braschi","year":"2009","unstructured":"Braschi E, Zunino R, McBride HM (2009) MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission. EMBO Rep 10:748\u2013754","journal-title":"EMBO Rep"},{"key":"4604_CR156","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1091\/mbc.e15-09-0678","volume":"27","author":"S Xu","year":"2016","unstructured":"Xu S, Cherok E, Das S, Li S, Roelofs BA, Ge SX, Polster BM, Boyman L, Lederer WJ, Wang C, Karbowski M (2016) Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein. Mol Biol Cell 27:349\u2013359","journal-title":"Mol Biol Cell"},{"key":"4604_CR157","doi-asserted-by":"publisher","first-page":"1726","DOI":"10.1093\/hmg\/ddr048","volume":"20","author":"NC Chan","year":"2011","unstructured":"Chan NC, Salazar AM, Pham AH, Sweredoski MJ, Kolawa NJ, Graham RL, Hess S, Chan DC (2011) Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet 20:1726\u20131737","journal-title":"Hum Mol Genet"},{"key":"4604_CR158","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1083\/jcb.201402104","volume":"205","author":"LA Kane","year":"2014","unstructured":"Kane LA, Lazarou M, Fogel AI, Li Y, Yamano K, Sarraf SA, Banerjee S, Youle RJ (2014) PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol 205:143\u2013153","journal-title":"J Cell Biol"},{"key":"4604_CR159","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1038\/nature13392","volume":"510","author":"F Koyano","year":"2014","unstructured":"Koyano F, Okatsu K, Kosako H, Tamura Y, Go E, Kimura M, Kimura Y, Tsuchiya H, Yoshihara H, Hirokawa T, Endo T, Fon EA, Trempe JF, Saeki Y, Tanaka K, Matsuda N (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510:162\u2013166","journal-title":"Nature"},{"key":"4604_CR160","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.RA118.006302","author":"F Koyano","year":"2019","unstructured":"Koyano F, Yamano K, Kosako H, Tanaka K, Matsuda N (2019) Parkin recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MITOL. J Biol Chem. https:\/\/doi.org\/10.1074\/jbc.RA118.006302","journal-title":"J Biol Chem"},{"key":"4604_CR161","doi-asserted-by":"publisher","first-page":"11364","DOI":"10.1073\/pnas.0802076105","volume":"105","author":"CA Gautier","year":"2008","unstructured":"Gautier CA, Kitada T, Shen J (2008) Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc Natl Acad Sci USA 105:11364\u201311369","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR162","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1000298","volume":"8","author":"DP Narendra","year":"2010","unstructured":"Narendra DP, Jin SM, Tanaka A, Suen DF, Gautier CA, Shen J, Cookson MR, Youle RJ (2010) PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol 8:e1000298","journal-title":"PLoS Biol"},{"key":"4604_CR163","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.180108","author":"TG McWilliams","year":"2018","unstructured":"McWilliams TG, Barini E, Pohjolan-Pirhonen R, Brooks SP, Singh F, Burel S, Balk K, Kumar A, Montava-Garriga L, Prescott AR, Hassoun SM, Mouton-Liger F, Ball G, Hills R, Knebel A, Ulusoy A, Di Monte DA, Tamjar J, Antico O, Fears K, Smith L, Brambilla R, Palin E, Valori M, Eerola-Rautio J, Tienari P, Corti O, Dunnett SB, Ganley IG, Suomalainen A, Muqit MMK (2018) Phosphorylation of Parkin at serine 65 is essential for its activation in vivo. Open Biol. https:\/\/doi.org\/10.1098\/rsob.180108","journal-title":"Open Biol"},{"key":"4604_CR164","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1126\/science.1231031","volume":"340","author":"Y Chen","year":"2013","unstructured":"Chen Y, Dorn GW 2nd (2013) PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 340:471\u2013475","journal-title":"Science"},{"key":"4604_CR165","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1083\/jcb.201401070","volume":"206","author":"G Ashrafi","year":"2014","unstructured":"Ashrafi G, Schlehe JS, LaVoie MJ, Schwarz TL (2014) Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin. J Cell Biol 206:655\u2013670","journal-title":"J Cell Biol"},{"key":"4604_CR166","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.ceb.2015.01.002","volume":"33","author":"A Eiyama","year":"2015","unstructured":"Eiyama A, Okamoto K (2015) PINK1\/Parkin-mediated mitophagy in mammalian cells. Curr Opin Cell Biol 33:95\u2013101","journal-title":"Curr Opin Cell Biol"},{"key":"4604_CR167","doi-asserted-by":"publisher","first-page":"2989","DOI":"10.1016\/j.celrep.2018.05.015","volume":"23","author":"F Jian","year":"2018","unstructured":"Jian F, Chen D, Chen L, Yan C, Lu B, Zhu Y, Chen S, Shi A, Chan DC, Song Z (2018) Sam50 regulates PINK1-Parkin-mediated mitophagy by controlling PINK1 stability and mitochondrial morphology. Cell Rep 23:2989\u20133005","journal-title":"Cell Rep"},{"key":"4604_CR168","doi-asserted-by":"publisher","first-page":"126","DOI":"10.1091\/mbc.e07-08-0796","volume":"19","author":"NC Chan","year":"2008","unstructured":"Chan NC, Lithgow T (2008) The peripheral membrane subunits of the SAM complex function codependently in mitochondrial outer membrane biogenesis. Mol Biol Cell 19:126\u2013136","journal-title":"Mol Biol Cell"},{"key":"4604_CR169","doi-asserted-by":"publisher","first-page":"e202009092","DOI":"10.1083\/jcb.202009092","volume":"220","author":"YP Abudu","year":"2021","unstructured":"Abudu YP, Shrestha BK, Zhang W, Palara A, Brenne HB, Larsen KB, Wolfson DL, Dumitriu G, Oie CI, Ahluwalia BS, Levy G, Behrends C, Tooze SA, Mouilleron S, Lamark T, Johansen T (2021) SAMM50 acts with p62 in piecemeal basal- and OXPHOS-induced mitophagy of SAM and MICOS components. J Cell Biol 220:e202009092","journal-title":"J Cell Biol"},{"key":"4604_CR170","doi-asserted-by":"publisher","first-page":"3237","DOI":"10.1242\/jcs.126128","volume":"126","author":"AB Birgisdottir","year":"2013","unstructured":"Birgisdottir AB, Lamark T, Johansen T (2013) The LIR motif - crucial for selective autophagy. J Cell Sci 126:3237\u20133247","journal-title":"J Cell Sci"},{"key":"4604_CR171","doi-asserted-by":"publisher","first-page":"1613","DOI":"10.1083\/jcb.201801044","volume":"217","author":"JJ Lee","year":"2018","unstructured":"Lee JJ, Sanchez-Martinez A, Zarate AM, Beninca C, Mayor U, Clague MJ, Whitworth AJ (2018) Basal mitophagy is widespread in Drosophila but minimally affected by loss of Pink1 or parkin. J Cell Biol 217:1613\u20131622","journal-title":"J Cell Biol"},{"issue":"439\u2013449","key":"4604_CR172","volume":"27","author":"TG McWilliams","year":"2018","unstructured":"McWilliams TG, Prescott AR, Montava-Garriga L, Ball G, Singh F, Barini E, Muqit MMK, Brooks SP, Ganley IG (2018) Basal mitophagy occurs independently of PINK1 in mouse tissues of high metabolic demand. Cell Metab 27(439\u2013449):e5","journal-title":"Cell Metab"},{"key":"4604_CR173","doi-asserted-by":"publisher","first-page":"2174","DOI":"10.1073\/pnas.0409598102","volume":"102","author":"FA Perez","year":"2005","unstructured":"Perez FA, Palmiter RD (2005) Parkin-deficient mice are not a robust model of Parkinsonism. Proc Natl Acad Sci USA 102:2174\u20132179","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR174","doi-asserted-by":"publisher","first-page":"2798","DOI":"10.15252\/embj.201488658","volume":"33","author":"Y Kageyama","year":"2014","unstructured":"Kageyama Y, Hoshijima M, Seo K, Bedja D, Sysa-Shah P, Andrabi SA, Chen W, Hoke A, Dawson VL, Dawson TM, Gabrielson K, Kass DA, Iijima M, Sesaki H (2014) Parkin-independent mitophagy requires Drp1 and maintains the integrity of mammalian heart and brain. EMBO J 33:2798\u20132813","journal-title":"EMBO J"},{"issue":"588\u2013604","key":"4604_CR175","volume":"28","author":"T Yamada","year":"2018","unstructured":"Yamada T, Murata D, Adachi Y, Itoh K, Kameoka S, Igarashi A, Kato T, Araki Y, Huganir RL, Dawson TM, Yanagawa T, Okamoto K, Iijima M, Sesaki H (2018) Mitochondrial stasis reveals p62-mediated ubiquitination in Parkin-independent mitophagy and mitigates nonalcoholic fatty liver disease. Cell Metab 28(588\u2013604):e5","journal-title":"Cell Metab"},{"key":"4604_CR176","doi-asserted-by":"publisher","first-page":"2245","DOI":"10.1091\/mbc.12.8.2245","volume":"12","author":"E Smirnova","year":"2001","unstructured":"Smirnova E, Griparic L, Shurland DL, van der Bliek AM (2001) Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12:2245\u20132256","journal-title":"Mol Biol Cell"},{"key":"4604_CR177","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1038\/sj.emboj.7601963","volume":"27","author":"G Twig","year":"2008","unstructured":"Twig G, Elorza A, Molina AJ, Mohamed H, Wikstrom JD, Walzer G, Stiles L, Haigh SE, Katz S, Las G, Alroy J, Wu M, Py BF, Yuan J, Deeney JT, Corkey BE, Shirihai OS (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 27:433\u2013446","journal-title":"EMBO J"},{"key":"4604_CR178","doi-asserted-by":"publisher","first-page":"5909","DOI":"10.4049\/jimmunol.0900441","volume":"183","author":"YT Zheng","year":"2009","unstructured":"Zheng YT, Shahnazari S, Brech A, Lamark T, Johansen T, Brumell JH (2009) The adaptor protein p62\/SQSTM1 targets invading bacteria to the autophagy pathway. J Immunol 183:5909\u20135916","journal-title":"J Immunol"},{"key":"4604_CR179","doi-asserted-by":"publisher","first-page":"e97858","DOI":"10.15252\/embj.201797858","volume":"37","author":"T Prabakaran","year":"2018","unstructured":"Prabakaran T, Bodda C, Krapp C, Zhang BC, Christensen MH, Sun C, Reinert L, Cai Y, Jensen SB, Skouboe MK, Nyengaard JR, Thompson CB, Lebbink RJ, Sen GC, van Loo G, Nielsen R, Komatsu M, Nejsum LN, Jakobsen MR, Gyrd-Hansen M, Paludan SR (2018) Attenuation of cGAS-STING signaling is mediated by a p62\/SQSTM1-dependent autophagy pathway activated by TBK1. EMBO J 37:e97858","journal-title":"EMBO J"},{"key":"4604_CR180","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1111\/febs.14712","volume":"286","author":"P Sanchez-Martin","year":"2019","unstructured":"Sanchez-Martin P, Saito T, Komatsu M (2019) p62\/SQSTM1: \u201cJack of all trades\u201d in health and cancer. FEBS J 286:8\u201323","journal-title":"FEBS J"},{"key":"4604_CR181","doi-asserted-by":"publisher","DOI":"10.1111\/febs.16317","author":"CT Tan","year":"2021","unstructured":"Tan CT, Soh NJH, Chang HC, Yu VC (2021) p62\/SQSTM1 in liver diseases: the usual suspect with multifarious identities. FEBS J. https:\/\/doi.org\/10.1111\/febs.16317","journal-title":"FEBS J"},{"key":"4604_CR182","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1038\/s41389-020-00251-5","volume":"9","author":"XH Lin","year":"2020","unstructured":"Lin XH, Qiu BQ, Ma M, Zhang R, Hsu SJ, Liu HH, Chen J, Gao DM, Cui JF, Ren ZG, Chen RX (2020) Suppressing DRP1-mediated mitochondrial fission and mitophagy increases mitochondrial apoptosis of hepatocellular carcinoma cells in the setting of hypoxia. Oncogenesis 9:67","journal-title":"Oncogenesis"},{"key":"4604_CR183","doi-asserted-by":"publisher","first-page":"e202006043","DOI":"10.1083\/jcb.202006043","volume":"220","author":"Y Oshima","year":"2021","unstructured":"Oshima Y, Cartier E, Boyman L, Verhoeven N, Polster BM, Huang W, Kane M, Lederer WJ, Karbowski M (2021) Parkin-independent mitophagy via Drp1-mediated outer membrane severing and inner membrane ubiquitination. J Cell Biol 220:e202006043","journal-title":"J Cell Biol"},{"key":"4604_CR184","doi-asserted-by":"publisher","first-page":"2846","DOI":"10.1016\/j.celrep.2017.08.087","volume":"20","author":"E Villa","year":"2017","unstructured":"Villa E, Proics E, Rubio-Patino C, Obba S, Zunino B, Bossowski JP, Rozier RM, Chiche J, Mondragon L, Riley JS, Marchetti S, Verhoeyen E, Tait SWG, Ricci JE (2017) Parkin-independent mitophagy controls chemotherapeutic response in cancer cells. Cell Rep 20:2846\u20132859","journal-title":"Cell Rep"},{"key":"4604_CR185","doi-asserted-by":"publisher","first-page":"372","DOI":"10.1038\/nature12043","volume":"496","author":"SA Sarraf","year":"2013","unstructured":"Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW (2013) Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 496:372\u2013376","journal-title":"Nature"},{"key":"4604_CR186","doi-asserted-by":"publisher","first-page":"19630","DOI":"10.1074\/jbc.M110.209338","volume":"286","author":"SR Yoshii","year":"2011","unstructured":"Yoshii SR, Kishi C, Ishihara N, Mizushima N (2011) Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem 286:19630\u201319640","journal-title":"J Biol Chem"},{"key":"4604_CR187","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1038\/cdd.2014.139","volume":"22","author":"F Strappazzon","year":"2015","unstructured":"Strappazzon F, Nazio F, Corrado M, Cianfanelli V, Romagnoli A, Fimia GM, Campello S, Nardacci R, Piacentini M, Campanella M, Cecconi F (2015) AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62\/SQSTM1. Cell Death Differ 22:419\u2013432","journal-title":"Cell Death Differ"},{"key":"4604_CR188","doi-asserted-by":"publisher","first-page":"1465","DOI":"10.1038\/s41598-020-58315-w","volume":"10","author":"R Igarashi","year":"2020","unstructured":"Igarashi R, Yamashita SI, Yamashita T, Inoue K, Fukuda T, Fukuchi T, Kanki T (2020) Gemcitabine induces Parkin-independent mitophagy through mitochondrial-resident E3 ligase MUL1-mediated stabilization of PINK1. Sci Rep 10:1465","journal-title":"Sci Rep"},{"key":"4604_CR189","doi-asserted-by":"publisher","DOI":"10.15252\/embr.202152584","volume":"22","author":"A Yamada","year":"2021","unstructured":"Yamada A, Hikichi M, Nozawa T, Nakagawa I (2021) FBXO2\/SCF ubiquitin ligase complex directs xenophagy through recognizing bacterial surface glycan. EMBO Rep 22:e52584","journal-title":"EMBO Rep"},{"key":"4604_CR190","doi-asserted-by":"publisher","first-page":"2041","DOI":"10.1080\/15548627.2017.1376160","volume":"13","author":"G Pei","year":"2017","unstructured":"Pei G, Buijze H, Liu H, Moura-Alves P, Goosmann C, Brinkmann V, Kawabe H, Dorhoi A, Kaufmann SHE (2017) The E3 ubiquitin ligase NEDD4 enhances killing of membrane-perturbing intracellular bacteria by promoting autophagy. Autophagy 13:2041\u20132055","journal-title":"Autophagy"},{"key":"4604_CR191","doi-asserted-by":"publisher","DOI":"10.1016\/j.cellsig.2022.110249","volume":"92","author":"H Ji","year":"2022","unstructured":"Ji H, Wang J, Muid D, Song W, Jiang Y, Zhou H (2022) FUNDC1 activates the mitochondrial unfolded protein response to preserve mitochondrial quality control in cardiac ischemia\/reperfusion injury. Cell Signal 92:110249","journal-title":"Cell Signal"},{"key":"4604_CR192","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.788634","volume":"9","author":"G Li","year":"2021","unstructured":"Li G, Li J, Shao R, Zhao J, Chen M (2021) FUNDC1: a promising mitophagy regulator at the mitochondria-associated membrane for cardiovascular diseases. Front Cell Dev Biol 9:788634","journal-title":"Front Cell Dev Biol"},{"key":"4604_CR193","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcp.2021.114891","volume":"197","author":"H Liu","year":"2022","unstructured":"Liu H, Zang C, Yuan F, Ju C, Shang M, Ning J, Yang Y, Ma J, Li G, Bao X, Zhang D (2022) The role of FUNDC1 in mitophagy, mitochondrial dynamics and human diseases. Biochem Pharmacol 197:114891","journal-title":"Biochem Pharmacol"},{"key":"4604_CR194","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1038\/ncb2422","volume":"14","author":"L Liu","year":"2012","unstructured":"Liu L, Feng D, Chen G, Chen M, Zheng Q, Song P, Ma Q, Zhu C, Wang R, Qi W, Huang L, Xue P, Li B, Wang X, Jin H, Wang J, Yang F, Liu P, Zhu Y, Sui S, Chen Q (2012) Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat Cell Biol 14:177\u2013185","journal-title":"Nat Cell Biol"},{"key":"4604_CR195","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2021.807654","volume":"12","author":"L Liu","year":"2021","unstructured":"Liu L, Li Y, Chen Q (2021) The emerging role of FUNDC1-mediated mitophagy in cardiovascular diseases. Front Physiol 12:807654","journal-title":"Front Physiol"},{"key":"4604_CR196","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2020.101792","volume":"38","author":"Y Cai","year":"2021","unstructured":"Cai Y, Yang E, Yao X, Zhang X, Wang Q, Wang Y, Liu J, Fan W, Yi K, Kang C, Wu J (2021) FUNDC1-dependent mitophagy induced by tPA protects neurons against cerebral ischemia-reperfusion injury. Redox Biol 38:101792","journal-title":"Redox Biol"},{"key":"4604_CR197","doi-asserted-by":"publisher","first-page":"1539","DOI":"10.1007\/s11064-018-2568-x","volume":"43","author":"L Wang","year":"2018","unstructured":"Wang L, Wang P, Dong H, Wang S, Chu H, Yan W, Zhang X (2018) Ulk1\/FUNDC1 prevents nerve cells from hypoxia-induced apoptosis by promoting cell autophagy. Neurochem Res 43:1539\u20131548","journal-title":"Neurochem Res"},{"key":"4604_CR198","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1016\/j.molcel.2014.02.034","volume":"54","author":"G Chen","year":"2014","unstructured":"Chen G, Han Z, Feng D, Chen Y, Chen L, Wu H, Huang L, Zhou C, Cai X, Fu C, Duan L, Wang X, Liu L, Liu X, Shen Y, Zhu Y, Chen Q (2014) A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy. Mol Cell 54:362\u2013377","journal-title":"Mol Cell"},{"key":"4604_CR199","doi-asserted-by":"publisher","first-page":"1697","DOI":"10.1016\/j.yexcr.2013.03.034","volume":"319","author":"D Feng","year":"2013","unstructured":"Feng D, Liu L, Zhu Y, Chen Q (2013) Molecular signaling toward mitophagy and its physiological significance. Exp Cell Res 319:1697\u20131705","journal-title":"Exp Cell Res"},{"key":"4604_CR200","doi-asserted-by":"publisher","first-page":"e98786","DOI":"10.15252\/embj.201798786","volume":"38","author":"Y Li","year":"2019","unstructured":"Li Y, Xue Y, Xu X, Wang G, Liu Y, Wu H, Li W, Wang Y, Chen Z, Zhang W, Zhu Y, Ji W, Xu T, Liu L, Chen Q (2019) A mitochondrial FUNDC1\/HSC70 interaction organizes the proteostatic stress response at the risk of cell morbidity. EMBO J 38:e98786","journal-title":"EMBO J"},{"key":"4604_CR201","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2020.103949","volume":"229","author":"P Sulkshane","year":"2020","unstructured":"Sulkshane P, Duek I, Ram J, Thakur A, Reis N, Ziv T, Glickman MH (2020) Inhibition of proteasome reveals basal mitochondrial ubiquitination. J Proteom 229:103949","journal-title":"J Proteom"},{"key":"4604_CR202","doi-asserted-by":"publisher","first-page":"12681","DOI":"10.1074\/jbc.C800036200","volume":"283","author":"S Radke","year":"2008","unstructured":"Radke S, Chander H, Schafer P, Meiss G, Kruger R, Schulz JB, Germain D (2008) Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi. J Biol Chem 283:12681\u201312685","journal-title":"J Biol Chem"},{"key":"4604_CR203","doi-asserted-by":"publisher","first-page":"7713","DOI":"10.1073\/pnas.1504615112","volume":"112","author":"P Bragoszewski","year":"2015","unstructured":"Bragoszewski P, Wasilewski M, Sakowska P, Gornicka A, Bottinger L, Qiu J, Wiedemann N, Chacinska A (2015) Retro-translocation of mitochondrial intermembrane space proteins. Proc Natl Acad Sci USA 112:7713\u20137718","journal-title":"Proc Natl Acad Sci USA"},{"key":"4604_CR204","doi-asserted-by":"publisher","first-page":"1759","DOI":"10.1016\/j.bbabio.2012.03.035","volume":"1817","author":"KJ Clarke","year":"2012","unstructured":"Clarke KJ, Adams AE, Manzke LH, Pearson TW, Borchers CH, Porter RK (2012) A role for ubiquitinylation and the cytosolic proteasome in turnover of mitochondrial uncoupling protein 1 (UCP1). Biochim Biophys Acta 1817:1759\u20131767","journal-title":"Biochim Biophys Acta"},{"key":"4604_CR205","doi-asserted-by":"publisher","first-page":"2136","DOI":"10.1128\/MCB.01579-12","volume":"33","author":"P Bragoszewski","year":"2013","unstructured":"Bragoszewski P, Gornicka A, Sztolsztener ME, Chacinska A (2013) The ubiquitin-proteasome system regulates mitochondrial intermembrane space proteins. Mol Cell Biol 33:2136\u20132148","journal-title":"Mol Cell Biol"},{"key":"4604_CR206","doi-asserted-by":"publisher","first-page":"e9561","DOI":"10.15252\/emmm.201809561","volume":"11","author":"K Mohanraj","year":"2019","unstructured":"Mohanraj K, Wasilewski M, Beninca C, Cysewski D, Poznanski J, Sakowska P, Bugajska Z, Deckers M, Dennerlein S, Fernandez-Vizarra E, Rehling P, Dadlez M, Zeviani M, Chacinska A (2019) Inhibition of proteasome rescues a pathogenic variant of respiratory chain assembly factor COA7. EMBO Mol Med 11:e9561","journal-title":"EMBO Mol Med"},{"key":"4604_CR207","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1038\/sj.cdd.4402291","volume":"15","author":"L Vande Walle","year":"2008","unstructured":"Vande Walle L, Lamkanfi M, Vandenabeele P (2008) The mitochondrial serine protease HtrA2\/Omi: an overview. Cell Death Differ 15:453\u2013460","journal-title":"Cell Death Differ"},{"key":"4604_CR208","doi-asserted-by":"publisher","first-page":"846","DOI":"10.1136\/jmedgenet-2016-104194","volume":"53","author":"A Martinez Lyons","year":"2016","unstructured":"Martinez Lyons A, Ardissone A, Reyes A, Robinson AJ, Moroni I, Ghezzi D, Fernandez-Vizarra E, Zeviani M (2016) COA7 (C1orf163\/RESA1) mutations associated with mitochondrial leukoencephalopathy and cytochrome c oxidase deficiency. J Med Genet 53:846\u2013849","journal-title":"J Med Genet"},{"key":"4604_CR209","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1038\/sj.embor.7400790","volume":"7","author":"N Nakamura","year":"2006","unstructured":"Nakamura N, Kimura Y, Tokuda M, Honda S, Hirose S (2006) MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep 7:1019\u20131022","journal-title":"EMBO Rep"},{"key":"4604_CR210","doi-asserted-by":"publisher","first-page":"4524","DOI":"10.1091\/mbc.e09-02-0112","volume":"20","author":"R Yonashiro","year":"2009","unstructured":"Yonashiro R, Sugiura A, Miyachi M, Fukuda T, Matsushita N, Inatome R, Ogata Y, Suzuki T, Dohmae N, Yanagi S (2009) Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol Biol Cell 20:4524\u20134530","journal-title":"Mol Biol Cell"},{"key":"4604_CR211","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.mito.2010.09.001","volume":"11","author":"A Sugiura","year":"2011","unstructured":"Sugiura A, Yonashiro R, Fukuda T, Matsushita N, Nagashima S, Inatome R, Yanagi S (2011) A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein. Mitochondrion 11:139\u2013146","journal-title":"Mitochondrion"},{"key":"4604_CR212","doi-asserted-by":"publisher","first-page":"938","DOI":"10.1038\/s41419-019-2175-z","volume":"10","author":"YS Yoo","year":"2019","unstructured":"Yoo YS, Park YJ, Lee HS, Oanh NTK, Cho MY, Heo J, Lee ES, Cho H, Park YY, Cho H (2019) Mitochondria ubiquitin ligase, MARCH5 resolves hepatitis B virus X protein aggregates in the liver pathogenesis. Cell Death Dis 10:938","journal-title":"Cell Death Dis"},{"key":"4604_CR213","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.3001139","volume":"19","author":"M Hussain","year":"2021","unstructured":"Hussain M, Mohammed A, Saifi S, Khan A, Kaur E, Priya S, Agarwal H, Sengupta S (2021) MITOL-dependent ubiquitylation negatively regulates the entry of PolgammaA into mitochondria. PLoS Biol 19:e3001139","journal-title":"PLoS Biol"},{"key":"4604_CR214","doi-asserted-by":"publisher","DOI":"10.15252\/embr.201949097","volume":"22","author":"I Shiiba","year":"2021","unstructured":"Shiiba I, Takeda K, Nagashima S, Ito N, Tokuyama T, Yamashita SI, Kanki T, Komatsu T, Urano Y, Fujikawa Y, Inatome R, Yanagi S (2021) MITOL promotes cell survival by degrading Parkin during mitophagy. EMBO Rep 22:e49097","journal-title":"EMBO Rep"},{"key":"4604_CR215","doi-asserted-by":"publisher","DOI":"10.15252\/embr.201947728","volume":"20","author":"F Koyano","year":"2019","unstructured":"Koyano F, Yamano K, Kosako H, Kimura Y, Kimura M, Fujiki Y, Tanaka K, Matsuda N (2019) Parkin-mediated ubiquitylation redistributes MITOL\/March5 from mitochondria to peroxisomes. EMBO Rep 20:e47728","journal-title":"EMBO Rep"},{"key":"4604_CR216","doi-asserted-by":"publisher","first-page":"3027","DOI":"10.3390\/molecules20023027","volume":"20","author":"E Chapman","year":"2015","unstructured":"Chapman E, Maksim N, de la Cruz F, La Clair JJ (2015) Inhibitors of the AAA+ chaperone p97. Molecules 20:3027\u20133049","journal-title":"Molecules"},{"key":"4604_CR217","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1016\/j.bbrc.2006.12.206","volume":"354","author":"JM Muller","year":"2007","unstructured":"Muller JM, Deinhardt K, Rosewell I, Warren G, Shima DT (2007) Targeted deletion of p97 (VCP\/CDC48) in mouse results in early embryonic lethality. Biochem Biophys Res Commun 354:459\u2013465","journal-title":"Biochem Biophys Res Commun"},{"key":"4604_CR218","doi-asserted-by":"publisher","first-page":"85","DOI":"10.3389\/fmolb.2018.00085","volume":"5","author":"J Shorter","year":"2018","unstructured":"Shorter J, Houry WA (2018) Editorial: the role of AAA+ proteins in protein repair and degradation. Front Mol Biosci 5:85","journal-title":"Front Mol Biosci"},{"key":"4604_CR219","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1083\/jcb.200302169","volume":"162","author":"Y Ye","year":"2003","unstructured":"Ye Y, Meyer HH, Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162:71\u201384","journal-title":"J Cell Biol"},{"key":"4604_CR220","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1097\/00125817-200007000-00006","volume":"2","author":"VE Kimonis","year":"2000","unstructured":"Kimonis VE, Kovach MJ, Waggoner B, Leal S, Salam A, Rimer L, Davis K, Khardori R, Gelber D (2000) Clinical and molecular studies in a unique family with autosomal dominant limb-girdle muscular dystrophy and Paget disease of bone. Genet Med 2:232\u2013241","journal-title":"Genet Med"},{"key":"4604_CR221","doi-asserted-by":"publisher","first-page":"2897","DOI":"10.1093\/brain\/awu224","volume":"137","author":"MA Gonzalez","year":"2014","unstructured":"Gonzalez MA, Feely SM, Speziani F, Strickland AV, Danzi M, Bacon C, Lee Y, Chou TF, Blanton SH, Weihl CC, Zuchner S, Shy ME (2014) A novel mutation in VCP causes charcot-marie-tooth type 2 disease. Brain 137:2897\u20132902","journal-title":"Brain"},{"key":"4604_CR222","doi-asserted-by":"publisher","first-page":"79","DOI":"10.3389\/fmolb.2016.00079","volume":"3","author":"WK Tang","year":"2016","unstructured":"Tang WK, Xia D (2016) Mutations in the human AAA(+) Chaperone p97 and related diseases. Front Mol Biosci 3:79","journal-title":"Front Mol Biosci"},{"key":"4604_CR223","doi-asserted-by":"publisher","first-page":"16","DOI":"10.3389\/fncel.2015.00016","volume":"9","author":"L Fang","year":"2015","unstructured":"Fang L, Hemion C, Pinho FB, Bippes CC, Flammer J, Neutzner A (2015) Mitochondrial function in neuronal cells depends on p97\/VCP\/Cdc48-mediated quality control. Front Cell Neurosci 9:16","journal-title":"Front Cell Neurosci"},{"key":"4604_CR224","doi-asserted-by":"publisher","first-page":"12415","DOI":"10.1038\/s41598-018-30963-z","volume":"8","author":"AC Bento","year":"2018","unstructured":"Bento AC, Bippes CC, Kohler C, Hemion C, Frank S, Neutzner A (2018) UBXD1 is a mitochondrial recruitment factor for p97\/VCP and promotes mitophagy. Sci Rep 8:12415","journal-title":"Sci Rep"},{"key":"4604_CR225","doi-asserted-by":"publisher","DOI":"10.1126\/science.aan4146","author":"H Weidberg","year":"2018","unstructured":"Weidberg H, Amon A (2018) MitoCPR-A surveillance pathway that protects mitochondria in response to protein import stress. Science. https:\/\/doi.org\/10.1126\/science.aan4146","journal-title":"Science"},{"key":"4604_CR226","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1091\/mbc.e04-06-0508","volume":"16","author":"CG Levine","year":"2005","unstructured":"Levine CG, Mitra D, Sharma A, Smith CL, Hegde RS (2005) The efficiency of protein compartmentalization into the secretory pathway. Mol Biol Cell 16:279\u2013291","journal-title":"Mol Biol Cell"},{"key":"4604_CR227","doi-asserted-by":"publisher","first-page":"1136","DOI":"10.1016\/j.cell.2009.03.042","volume":"137","author":"O Chakrabarti","year":"2009","unstructured":"Chakrabarti O, Hegde RS (2009) Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration. Cell 137:1136\u20131147","journal-title":"Cell"},{"key":"4604_CR228","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1038\/nature21375","volume":"542","author":"A Sugiura","year":"2017","unstructured":"Sugiura A, Mattie S, Prudent J, McBride HM (2017) Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes. Nature 542:251\u2013254","journal-title":"Nature"},{"key":"4604_CR229","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1172\/JCI71602","volume":"124","author":"NM Weathington","year":"2014","unstructured":"Weathington NM, Mallampalli RK (2014) Emerging therapies targeting the ubiquitin proteasome system in cancer. J Clin Invest 124:6\u201312","journal-title":"J Clin Invest"}],"container-title":["Cellular and Molecular Life Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-022-04604-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00018-022-04604-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-022-04604-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,29]],"date-time":"2023-11-29T19:33:31Z","timestamp":1701286411000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00018-022-04604-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10,29]]},"references-count":229,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2022,11]]}},"alternative-id":["4604"],"URL":"https:\/\/doi.org\/10.1007\/s00018-022-04604-8","relation":{},"ISSN":["1420-682X","1420-9071"],"issn-type":[{"value":"1420-682X","type":"print"},{"value":"1420-9071","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,10,29]]},"assertion":[{"value":"12 March 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 June 2022","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 October 2022","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 October 2022","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"N\/A; this is a review manuscript.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"The authors give their consent to publish this work in Cellular and Molecular Life Sciences.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}}],"article-number":"574"}}