{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T23:44:05Z","timestamp":1792712645029,"version":"4.5.0"},"reference-count":147,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2025,1,24]],"date-time":"2025-01-24T00:00:00Z","timestamp":1737676800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Ubiquitin\u2013proteasome-mediated proteolysis post-translationally regulates the amounts of many proteins that are critical for the normal physiology of the central nervous system. Research carried out over the last several years has revealed a role for components of the ubiquitin\u2013proteasome pathway (UPP) in many neurodegenerative diseases such as Parkinson\u2019s disease and Huntington\u2019s disease. Studies have also shown a role for the UPP in mental disorders such as schizophrenia and autism. Even though dysregulation of protein degradation by the UPP is a contributory factor to the pathology underlying many nervous system disorders, the association between the components of the UPP and these diseases is far from simple. In this review, we discuss the connections between the UPP and some of the major mental disorders and neurodegenerative diseases.<\/jats:p>","DOI":"10.3390\/ijms26030966","type":"journal-article","created":{"date-parts":[[2025,1,24]],"date-time":"2025-01-24T03:26:31Z","timestamp":1737689191000},"page":"966","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Ubiquitin-Proteasome-Mediated Protein Degradation and Disorders of the Central Nervous System"],"prefix":"10.3390","volume":"26","author":[{"given":"Ashok N.","family":"Hegde","sequence":"first","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Logan E.","family":"Timm","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Connor J.","family":"Sivley","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shrenik","family":"Ramiyaramcharankarthic","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivia J.","family":"Lowrimore","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brenna J.","family":"Hendrix","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teodora G.","family":"Grozdanov","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William J.","family":"Anderson","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences, Georgia College and State University, Milledgeville, GA 31061, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,1,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.pneurobio.2004.05.005","article-title":"Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity","volume":"73","author":"Hegde","year":"2004","journal-title":"Prog. Neurobiol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Spano, D., and Catara, G. (2023). Targeting the Ubiquitin-Proteasome System and Recent Advances in Cancer Therapy. Cells, 13.","DOI":"10.3390\/cells13010029"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.tins.2007.08.005","article-title":"The ubiquitin-proteasome pathway in health and disease of the nervous system","volume":"30","author":"Hegde","year":"2007","journal-title":"Trends Neurosci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/0304-3940(87)90698-7","article-title":"Ubiquitin-protein conjugates in Alzheimer\u2019s lesions","volume":"79","author":"Cole","year":"1987","journal-title":"Neurosci. Lett."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/349132a0","article-title":"Cyclin is degraded by the ubiquitin pathway","volume":"349","author":"Glotzer","year":"1991","journal-title":"Nature"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"5005","DOI":"10.1038\/onc.2012.522","article-title":"BRCA1 targets G2\/M cell cycle proteins for ubiquitination and proteasomal degradation","volume":"32","author":"Shabbeer","year":"2013","journal-title":"Oncogene"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Paccosi, E., Artemi, G., Filippi, S., Balzerano, A., Costanzo, F., Laghezza-Masci, V., Proietti, S., and Proietti-De-Santis, L. (2023). Cockayne syndrome group A protein localizes at centrosomes during mitosis and regulates Cyclin B1 ubiquitination. Eur. J. Cell Biol., 102.","DOI":"10.1016\/j.ejcb.2023.151325"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1038\/ng0197-70","article-title":"UBE3A\/E6-AP mutations cause Angelman syndrome","volume":"15","author":"Kishino","year":"1997","journal-title":"Nat. Genet."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/ng0197-74","article-title":"De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome","volume":"15","author":"Matsuura","year":"1997","journal-title":"Nat. Genet."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/S0896-6273(00)80596-6","article-title":"Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation","volume":"21","author":"Jiang","year":"1998","journal-title":"Neuron"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1101\/lm.1504010","article-title":"The ubiquitin-proteasome pathway and synaptic plasticity","volume":"17","author":"Hegde","year":"2010","journal-title":"Learn. Mem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"7096","DOI":"10.1093\/emboj\/20.24.7096","article-title":"Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome","volume":"20","author":"Fu","year":"2001","journal-title":"EMBO J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1218","DOI":"10.1073\/pnas.98.3.1218","article-title":"Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells","volume":"98","author":"Hengstermann","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.cellbio.15.1.435","article-title":"SCF and Cullin\/Ring H2-based ubiquitin ligases","volume":"15","author":"Deshaies","year":"1999","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1146\/annurev.biochem.68.1.583","article-title":"The anaphase-promoting complex: New subunits and regulators","volume":"68","author":"Page","year":"1999","journal-title":"Annu. Rev. Biochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/s41467-023-35871-z","article-title":"The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family","volume":"14","author":"Wang","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1982","DOI":"10.1038\/ncomms2982","article-title":"Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases","volume":"4","author":"Riley","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/s41586-018-0026-1","article-title":"Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity","volume":"556","author":"Pao","year":"2018","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"12","DOI":"10.2183\/pjab.85.12","article-title":"The proteasome: Overview of structure and functions","volume":"85","author":"Tanaka","year":"2009","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.braindev.2003.09.014","article-title":"Neurological aspects of the Angelman syndrome","volume":"27","author":"Williams","year":"2005","journal-title":"Brain Dev."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1038\/ng0997-75","article-title":"Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons","volume":"17","author":"Albrecht","year":"1997","journal-title":"Nat. Genet."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/ng0997-14","article-title":"The Angelman syndrome candidate gene, UBE3A\/E6-AP, is imprinted in brain","volume":"17","author":"Rougeulle","year":"1997","journal-title":"Nat. Genet."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"18785","DOI":"10.1074\/jbc.274.26.18785","article-title":"Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination","volume":"274","author":"Kumar","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"34302","DOI":"10.1074\/jbc.273.51.34302","article-title":"E3-ubiquitin ligase\/E6-AP links multicopy maintenance protein 7 to the ubiquitination pathway by a novel motif, the L2G box","volume":"273","author":"Banks","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1046\/j.1432-1327.1998.2540643.x","article-title":"The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate","volume":"254","author":"Nuber","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2634","DOI":"10.1523\/JNEUROSCI.23-07-02634.2003","article-title":"Derangements of hippocampal calcium\/calmodulin-dependent protein kinase II in a mouse model for Angelman mental retardation syndrome","volume":"23","author":"Weeber","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/nn1845","article-title":"Rescue of neurological deficits in a mouse model for Angelman syndrome by reduction of alphaCaMKII inhibitory phosphorylation","volume":"10","author":"Harris","year":"2007","journal-title":"Nat. Neurosci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/j.cell.2010.01.026","article-title":"The Angelman Syndrome protein Ube3A regulates synapse development by ubiquitinating arc","volume":"140","author":"Greer","year":"2010","journal-title":"Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.celrep.2015.06.023","article-title":"UBE3A Regulates Synaptic Plasticity and Learning and Memory by Controlling SK2 Channel Endocytosis","volume":"12","author":"Sun","year":"2015","journal-title":"Cell Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e37993","DOI":"10.7554\/eLife.37993","article-title":"UBE3A-mediated p18\/LAMTOR1 ubiquitination and degradation regulate mTORC1 activity and synaptic plasticity","volume":"7","author":"Sun","year":"2018","journal-title":"eLife"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2825","DOI":"10.1093\/hmg\/ddl225","article-title":"Expression of the Rho-GEF Pbl\/ECT2 is regulated by the UBE3A E3 ubiquitin ligase","volume":"15","author":"Reiter","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1172\/JCI80554","article-title":"Ube3a reinstatement identifies distinct developmental windows in a murine Angelman syndrome model","volume":"125","author":"Bruinsma","year":"2015","journal-title":"J. Clin. Investig."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/2040-2392-5-45","article-title":"Ubiquitin-proteasome dependent degradation of GABAA\u03b11 in autism spectrum disorder","volume":"5","author":"Crider","year":"2014","journal-title":"Mol. Autism"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1016\/j.cell.2012.11.040","article-title":"Multiple autism-linked genes mediate synapse elimination via proteasomal degradation of a synaptic scaffold PSD-95","volume":"151","author":"Tsai","year":"2012","journal-title":"Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/nature07953","article-title":"Autism genome-wide copy number variation reveals ubiquitin and neuronal genes","volume":"459","author":"Glessner","year":"2009","journal-title":"Nature"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1038\/s41398-023-02702-0","article-title":"A novel autism-associated UBLCP1 mutation impacts proteasome regulation\/activity","volume":"13","author":"Soueid","year":"2023","journal-title":"Transl. Psychiatry"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3995","DOI":"10.1093\/hmg\/ddx289","article-title":"Neuronal overexpression of Ube3a isoform 2 causes behavioral impairments and neuroanatomical pathology relevant to 15q11.2-q13.3 duplication syndrome","volume":"26","author":"Copping","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.cell.2015.06.045","article-title":"An Autism-Linked Mutation Disables Phosphorylation Control of UBE3A","volume":"162","author":"Yi","year":"2015","journal-title":"Cell"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"112706","DOI":"10.1016\/j.celrep.2023.112706","article-title":"Autism-linked UBE3A gain-of-function mutation causes interneuron and behavioral phenotypes when inherited maternally or paternally in mice","volume":"42","author":"Xing","year":"2023","journal-title":"Cell Rep."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1007\/s00439-017-1763-1","article-title":"Haploinsufficiency of the E3 ubiquitin-protein ligase gene TRIP12 causes intellectual disability with or without autism spectrum disorders, speech delay, and dysmorphic features","volume":"136","author":"Zhang","year":"2017","journal-title":"Hum. Genet."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/s41398-021-01529-x","article-title":"Genome wide analysis implicates upregulation of proteasome pathway in major depressive disorder","volume":"11","author":"Belaish","year":"2021","journal-title":"Transl. Psychiatry"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e687","DOI":"10.1038\/tp.2015.180","article-title":"Proteasome system dysregulation and treatment resistance mechanisms in major depressive disorder","volume":"5","author":"Minelli","year":"2015","journal-title":"Transl. Psychiatry"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4562","DOI":"10.1523\/JNEUROSCI.6458-11.2012","article-title":"MAGE-D1 regulates expression of depression-like behavior through serotonin transporter ubiquitylation","volume":"32","author":"Mouri","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.jad.2011.04.020","article-title":"Possible association between ubiquitin-specific peptidase 46 gene and major depressive disorders in the Japanese population","volume":"133","author":"Fukuo","year":"2011","journal-title":"J. Affect. Disord."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0140-6736(90)91520-K","article-title":"Association within a family of a balanced autosomal translocation with major mental illness","volume":"336","author":"Blackwood","year":"1990","journal-title":"Lancet"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"7746","DOI":"10.1021\/bi900901e","article-title":"Oligomer assembly of the C-terminal DISC1 domain (640\u2013854) is controlled by self-association motifs and disease-associated polymorphism S704C","volume":"48","author":"Leliveld","year":"2009","journal-title":"Biochemistry"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1093\/hmg\/ddl407","article-title":"DISC1-NDEL1\/NUDEL protein interaction, an essential component for neurite outgrowth, is modulated by genetic variations of DISC1","volume":"15","author":"Kamiya","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1038\/mp.2017.138","article-title":"FBXW7 regulates DISC1 stability via the ubiquitin-proteosome system","volume":"23","author":"Yalla","year":"2018","journal-title":"Mol. Psychiatry"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.cell.2008.12.044","article-title":"Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3beta\/beta-catenin signaling","volume":"136","author":"Mao","year":"2009","journal-title":"Cell"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.celrep.2014.03.022","article-title":"Dendrite development regulated by the schizophrenia-associated gene FEZ1 involves the ubiquitin proteasome system","volume":"7","author":"Watanabe","year":"2014","journal-title":"Cell Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1038\/s41398-018-0281-9","article-title":"Convergence of independent DISC1 mutations on impaired neurite growth via decreased UNC5D expression","volume":"8","author":"Srikanth","year":"2018","journal-title":"Transl. Psychiatry"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4128","DOI":"10.1016\/j.cub.2020.08.002","article-title":"Synaptic Protein Degradation Controls Sexually Dimorphic Circuits through Regulation of DCC\/UNC-40","volume":"30","author":"Salzberg","year":"2020","journal-title":"Curr. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.jpsychires.2018.03.013","article-title":"Gene expression profile associated with postnatal development of pyramidal neurons in the human prefrontal cortex implicates ubiquitin ligase E3 in the pathophysiology of schizophrenia onset","volume":"102","author":"Kohlbrenner","year":"2018","journal-title":"J. Psychiatr. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1038\/mp.2014.171","article-title":"Distinctive transcriptome alterations of prefrontal pyramidal neurons in schizophrenia and schizoaffective disorder","volume":"20","author":"Arion","year":"2015","journal-title":"Mol. Psychiatry"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.jpsychires.2017.01.009","article-title":"Alterations of ubiquitin related proteins in the pathology and development of schizophrenia: Evidence from human and animal studies","volume":"90","author":"Andrews","year":"2017","journal-title":"J. Psychiatr. Res."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Bi, Y., Ren, D., Yuan, F., Zhang, Z., Zhou, D., Yi, X., Ji, L., Li, K., Yang, F., and Wu, X. (2023). TULP4, a novel E3 ligase gene, participates in neuronal migration as a candidate in schizophrenia. CNS Neurosci. Ther.","DOI":"10.1111\/cns.14423"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S0361-9230(01)00522-6","article-title":"Application of cDNA microarrays to examine gene expression differences in schizophrenia","volume":"55","author":"Vawter","year":"2001","journal-title":"Brain Res. Bull."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2718","DOI":"10.1523\/JNEUROSCI.22-07-02718.2002","article-title":"Gene expression profiling reveals alterations of specific metabolic pathways in schizophrenia","volume":"22","author":"Middleton","year":"2002","journal-title":"J. Neurosci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.nbd.2006.02.002","article-title":"Identification of protein biomarkers for schizophrenia and bipolar disorder in the postmortem prefrontal cortex using SELDI-TOF-MS ProteinChip profiling combined with MALDI-TOF-PSD-MS analysis","volume":"23","author":"Novikova","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1038\/npp.2015.219","article-title":"Protein Expression of Proteasome Subunits in Elderly Patients with Schizophrenia","volume":"41","author":"Scott","year":"2016","journal-title":"Neuropsychopharmacology"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1093\/schbul\/sbaa160","article-title":"Comprehensive Gene Expression Analysis Detects Global Reduction of Proteasome Subunits in Schizophrenia","volume":"47","author":"Hertzberg","year":"2021","journal-title":"Schizophr. Bull."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Bousman, C.A., Luza, S., Mancuso, S.G., Kang, D., Opazo, C.M., Mostaid, M.S., Cropley, V., McGorry, P., Shannon Weickert, C., and Pantelis, C. (2019). Elevated ubiquitinated proteins in brain and blood of individuals with schizophrenia. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-38490-1"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1038\/npp.2013.84","article-title":"Dysfunction of the ubiquitin proteasome and ubiquitin-like systems in schizophrenia","volume":"38","author":"Rubio","year":"2013","journal-title":"Neuropsychopharmacology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1038\/s41380-019-0359-7","article-title":"Intracellular compartment-specific proteasome dysfunction in postmortem cortex in schizophrenia subjects","volume":"25","author":"Scott","year":"2020","journal-title":"Mol. Psychiatry"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1002\/ajmg.b.30759","article-title":"FBXL21 association with schizophrenia in Irish family and case-control samples","volume":"147","author":"Chen","year":"2008","journal-title":"Am. J. Med. Genet. B Neuropsychiatr. Genet."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"5600","DOI":"10.1073\/pnas.0501769102","article-title":"Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination","volume":"102","author":"Kato","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Han, C., Cui, K., Bi, X., Wang, L., Sun, M., Yang, L., and Liu, L. (2019). Association between polymorphism of the NEDD4 gene and cognitive dysfunction of schizophrenia patients in Chinese Han population. BMC Psychiatry, 19.","DOI":"10.1186\/s12888-019-2386-y"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1111\/j.1471-4159.2011.07221.x","article-title":"Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking","volume":"119","author":"Lin","year":"2011","journal-title":"J. Neurochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"e32743","DOI":"10.1016\/j.heliyon.2024.e32743","article-title":"Interaction between RNF4 and SART3 is associated with the risk of schizophrenia","volume":"10","author":"Cheng","year":"2024","journal-title":"Heliyon"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","article-title":"TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"351","author":"Arai","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1126\/science.1166066","article-title":"Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis","volume":"323","author":"Kwiatkowski","year":"2009","journal-title":"Science"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"Vance","year":"2009","journal-title":"Science"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/0022-510X(96)00031-7","article-title":"Proteasome inhibition enhances the stability of mouse Cu\/Zn superoxide dismutase with mutations linked to familial amyotrophic lateral sclerosis","volume":"139","author":"Hoffman","year":"1996","journal-title":"J. Neurol. Sci."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"12571","DOI":"10.1073\/pnas.220417997","article-title":"Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis","volume":"97","author":"Johnston","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"36793","DOI":"10.1074\/jbc.M206559200","article-title":"Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity","volume":"277","author":"Niwa","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"11327","DOI":"10.1074\/jbc.M312389200","article-title":"NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1","volume":"279","author":"Miyazaki","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"39907","DOI":"10.1074\/jbc.M506247200","article-title":"Proteasomal degradation of mutant superoxide dismutases linked to amyotrophic lateral sclerosis","volume":"280","author":"Whitson","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"30524","DOI":"10.1074\/jbc.M603337200","article-title":"Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome","volume":"281","author":"Kabuta","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/S0014-5793(02)03546-9","article-title":"Differentially expressed genes in sporadic amyotrophic lateral sclerosis spinal cords-screening by molecular indexing and subsequent cDNA microarray analysis","volume":"531","author":"Ishigaki","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1046\/j.1471-4159.2002.01211.x","article-title":"Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis","volume":"83","author":"Urushitani","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1046\/j.1471-4159.2002.01056.x","article-title":"No correlation between aggregates of Cu\/Zn superoxide dismutase and cell death in familial amyotrophic lateral sclerosis","volume":"82","author":"Lee","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1080\/14660820310016804","article-title":"Long term proteasome inhibition does not preferentially afflict motor neurons in organotypical spinal cord cultures","volume":"5","author":"Vlug","year":"2004","journal-title":"Amyotroph. Lateral Scler. Other Mot. Neuron Disord."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1046\/j.1471-4159.2003.01783.x","article-title":"Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu,Zn superoxide dismutase mutant involved in familial ALS","volume":"85","author":"Aquilano","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1046\/j.1471-4159.2003.01841.x","article-title":"Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins","volume":"86","author":"Hyun","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1093\/hmg\/ddn319","article-title":"Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis","volume":"18","author":"Cheroni","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"4268","DOI":"10.1093\/hmg\/ddp380","article-title":"Gp78, an ER associated E3, promotes SOD1 and ataxin-3 degradation","volume":"18","author":"Ying","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1093\/hmg\/ddac008","article-title":"E3 ligase Smurf1 protects against misfolded SOD1 in neuronal cells by promoting its K63 ubiquitylation and aggresome formation","volume":"31","author":"Dong","year":"2022","journal-title":"Hum. Mol. Genet."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"4524","DOI":"10.1091\/mbc.e09-02-0112","article-title":"Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation","volume":"20","author":"Yonashiro","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1074\/jbc.M112.419945","article-title":"Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6)","volume":"288","author":"Hebron","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1093\/brain\/awad046","article-title":"RNA polymerase II-associated proteins reveal pathways affected in VCP-related amyotrophic lateral sclerosis","volume":"146","author":"Rafiee","year":"2023","journal-title":"Brain"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Lee, Y.C., Huang, W.C., Lin, J.H., Kao, T.J., Lin, H.C., Lee, K.H., Lin, H.C., Shen, C.J., Chang, W.C., and Huang, C.C. (2018). Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology. J. Biomed. Sci., 25.","DOI":"10.1186\/s12929-018-0479-4"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1111\/neup.12694","article-title":"Praja1 RING-finger E3 ubiquitin ligase suppresses neuronal cytoplasmic TDP-43 aggregate formation","volume":"40","author":"Watabe","year":"2020","journal-title":"Neuropathology"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"19164","DOI":"10.1074\/jbc.M114.561704","article-title":"UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination","volume":"289","author":"Hans","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1093\/jmcb\/mjaa072","article-title":"Haploinsufficiency of the TDP43 ubiquitin E3 ligase RNF220 leads to ALS-like motor neuron defects in the mouse","volume":"13","author":"Ma","year":"2021","journal-title":"J. Mol. Cell Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/j.molmed.2008.09.001","article-title":"TDP-43: An emerging new player in neurodegenerative diseases","volume":"14","author":"Wang","year":"2008","journal-title":"Trends Mol. Med."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-2660(09)66001-6","article-title":"The molecular links between TDP-43 dysfunction and neurodegeneration","volume":"66","author":"Buratti","year":"2009","journal-title":"Adv. Genet."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"101700","DOI":"10.1016\/j.isci.2020.101700","article-title":"Ubiquitin Homeostasis Is Disrupted in TDP-43 and FUS Cell Models of ALS","volume":"23","author":"Farrawell","year":"2020","journal-title":"iScience"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"The Huntington\u2019s Disease Collaborative Research Group (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington\u2019s disease chromosomes. Cell, 72, 971\u2013983.","DOI":"10.1016\/0092-8674(93)90585-E"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the ubiquitin-proteasome system by protein aggregation","volume":"292","author":"Bence","year":"2001","journal-title":"Science"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1038\/nature06022","article-title":"Global changes to the ubiquitin system in Huntington\u2019s disease","volume":"448","author":"Bennett","year":"2007","journal-title":"Nature"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"5706","DOI":"10.1073\/pnas.1402215111","article-title":"Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A","volume":"111","author":"Bhat","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"6235","DOI":"10.1093\/hmg\/ddu343","article-title":"Deficiency of Ube3a in Huntington\u2019s disease mice brain increases aggregate load and accelerates disease pathology","volume":"23","author":"Maheshwari","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"7648","DOI":"10.1074\/jbc.M706620200","article-title":"E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity","volume":"283","author":"Mishra","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.cell.2015.07.003","article-title":"Identification of Genetic Factors that Modify Clinical Onset of Huntington\u2019s Disease","volume":"162","author":"Lee","year":"2015","journal-title":"Cell"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1038\/s41467-018-05320-3","article-title":"The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington\u2019s disease patients","volume":"9","author":"Koyuncu","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.yexcr.2006.10.031","article-title":"Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin","volume":"313","author":"Yang","year":"2007","journal-title":"Exp. Cell. Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the alpha-synuclein gene identified in families with Parkinson\u2019s disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/33416","article-title":"Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism","volume":"392","author":"Kitada","year":"1998","journal-title":"Nature"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1126\/science.1077209","article-title":"Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism","volume":"299","author":"Bonifati","year":"2003","journal-title":"Science"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.neuron.2004.10.023","article-title":"Cloning of the gene containing mutations that cause PARK8-linked Parkinson\u2019s disease","volume":"44","author":"Jain","year":"2004","journal-title":"Neuron"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1126\/science.1096284","article-title":"Hereditary early-onset Parkinson\u2019s disease caused by mutations in PINK1","volume":"304","author":"Valente","year":"2004","journal-title":"Science"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1038\/ng1884","article-title":"Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase","volume":"38","author":"Ramirez","year":"2006","journal-title":"Nat. Genet."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"49071","DOI":"10.1074\/jbc.M208046200","article-title":"Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions","volume":"277","author":"Hasegawa","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/S0968-0004(03)00092-6","article-title":"A potential proteasome-interacting motif within the ubiquitin-like domain of parkin and other proteins","volume":"28","author":"Upadhya","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/sj.cdd.4401704","article-title":"Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities","volume":"13","author":"Shinbo","year":"2006","journal-title":"Cell Death Differ."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Ding, X., and Goldberg, M.S. (2009). Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0005949"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1042\/BCJ20160909","article-title":"The G2385R risk factor for Parkinson\u2019s disease enhances CHIP-dependent intracellular degradation of LRRK2","volume":"474","author":"Rudenko","year":"2017","journal-title":"Biochem. J."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1016\/j.celrep.2016.12.090","article-title":"PINK1 Primes Parkin-Mediated Ubiquitination of PARIS in Dopaminergic Neuronal Survival","volume":"18","author":"Lee","year":"2017","journal-title":"Cell Rep."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Si, J., Van den Haute, C., Lobbestael, E., Martin, S., van Veen, S., Vangheluwe, P., and Baekelandt, V. (2021). ATP13A2 Regulates Cellular \u03b1-Synuclein Multimerization, Membrane Association, and Externalization. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22052689"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/26652","article-title":"The ubiquitin pathway in Parkinson\u2019s disease","volume":"395","author":"Leroy","year":"1998","journal-title":"Nature"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Kumar, R., Jangir, D.K., Verma, G., Shekhar, S., Hanpude, P., Kumar, S., Kumari, R., Singh, N., Sarovar Bhavesh, N., and Ranjan Jana, N. (2017). S-nitrosylation of UCHL1 induces its structural instability and promotes \u03b1-synuclein aggregation. Sci. Rep., 7.","DOI":"10.1038\/srep44558"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.jmb.2010.12.029","article-title":"The effect of Parkinson\u2019s-disease-associated mutations on the deubiquitinating enzyme UCH-L1","volume":"407","author":"Andersson","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.neurobiolaging.2005.07.023","article-title":"Parkin-mediated lysine 63-linked polyubiquitination: A link to protein inclusions formation in Parkinson\u2019s and other conformational diseases?","volume":"27","author":"Lim","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"85","DOI":"10.4161\/auto.5172","article-title":"Parkin-mediated K63-linked polyubiquitination: A signal for targeting misfolded proteins to the aggresome-autophagy pathway","volume":"4","author":"Olzmann","year":"2008","journal-title":"Autophagy"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1042\/BST0380144","article-title":"Parkin-mediated ubiquitin signalling in aggresome formation and autophagy","volume":"38","author":"Chin","year":"2010","journal-title":"Biochem. Soc. Trans."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.molcel.2014.09.007","article-title":"Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis","volume":"56","author":"Ordureau","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"6637","DOI":"10.1073\/pnas.1506593112","article-title":"Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy","volume":"112","author":"Ordureau","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"22044","DOI":"10.1074\/jbc.M212235200","article-title":"Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function","volume":"278","author":"Tsai","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"3942","DOI":"10.1093\/hmg\/ddn296","article-title":"CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins","volume":"17","author":"Morishima","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"26436","DOI":"10.1074\/jbc.M803692200","article-title":"The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains","volume":"283","author":"Winborn","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/emboj.2008.289","article-title":"Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3","volume":"28","author":"Todi","year":"2009","journal-title":"EMBO J."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"47","DOI":"10.2174\/092986708783330692","article-title":"Aggresome formation and neurodegenerative diseases: Therapeutic implications","volume":"15","author":"Olzmann","year":"2008","journal-title":"Curr. Med. Chem."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1002\/mds.10322","article-title":"Dopaminergic response in Parkinsonian phenotype of Machado-Joseph disease","volume":"18","author":"Buhmann","year":"2003","journal-title":"Mov. Disord."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"8189","DOI":"10.1523\/JNEUROSCI.2218-08.2008","article-title":"Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies","volume":"28","author":"Bedford","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1007\/s00702-008-0054-3","article-title":"A comprehensive genetic study of the proteasomal subunit S6 ATPase in German Parkinson\u2019s disease patients","volume":"115","author":"Wahl","year":"2008","journal-title":"J. Neural. Transm."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.ibror.2020.07.001","article-title":"Rpt2 proteasome subunit reduction causes Parkinson\u2019s disease like symptoms in Drosophila","volume":"9","author":"Reynaud","year":"2020","journal-title":"IBRO Rep."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1007\/s100380170060","article-title":"The genomic structure and expression of MJD, the Machado-Joseph disease gene","volume":"46","author":"Ichikawa","year":"2001","journal-title":"J. Hum. Genet."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1016\/j.bbrc.2007.08.062","article-title":"Inactivation of the mouse Atxn3 (ataxin-3) gene increases protein ubiquitination","volume":"362","author":"Schmitt","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1093\/hmg\/ddl164","article-title":"Ataxin-3 binds VCP\/p97 and regulates retrotranslocation of ERAD substrates","volume":"15","author":"Zhong","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.nbd.2018.04.013","article-title":"Toxicity and aggregation of the polyglutamine disease protein, ataxin-3 is regulated by its binding to VCP\/p97 in Drosophila melanogaster","volume":"116","author":"Ristic","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/ng1006","article-title":"Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease","volume":"32","author":"Wilson","year":"2002","journal-title":"Nat. Genet."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1111\/j.1471-4159.2005.03409.x","article-title":"Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice","volume":"95","author":"Anderson","year":"2005","journal-title":"J. Neurochem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"11423","DOI":"10.1523\/JNEUROSCI.3600-06.2006","article-title":"Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14","volume":"26","author":"Crimmins","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"10909","DOI":"10.1523\/JNEUROSCI.2635-09.2009","article-title":"The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions","volume":"29","author":"Chen","year":"2009","journal-title":"J. Neurosci."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/3\/966\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T10:35:02Z","timestamp":1759919702000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/3\/966"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,24]]},"references-count":147,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,2]]}},"alternative-id":["ijms26030966"],"URL":"https:\/\/doi.org\/10.3390\/ijms26030966","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,24]]}}}