{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T23:24:07Z","timestamp":1793316247704,"version":"4.5.0"},"reference-count":340,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T00:00:00Z","timestamp":1785110400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Neurosci."],"abstract":"<jats:p>Parkinson\u2019s disease (PD) is the second most prevalent neurodegenerative disorder worldwide, characterized pathologically by the loss of dopaminergic neurons in the substantia nigra and the formation of Lewy bodies, which predominantly consist of misfolded \u03b1-synuclein (\u03b1-Syn) aggregates. Recent advances have highlighted the critical role of the interplay between \u03b1-Syn and lysosomal function, termed the \u03b1-Syn-lysosome axis, as a central mechanism underlying PD pathogenesis. This review systematically summarizes the molecular mechanisms driving \u03b1-Syn aggregation and the lysosomal dysfunction contributing to impaired autophagy-lysosome pathway (ALP) activity. We further discuss emerging therapeutic strategies targeting this axis to restore lysosomal function and mitigate \u03b1-Syn toxicity. By integrating the latest findings from molecular biology, cell biology, and preclinical studies, this article aims to elucidate the complex regulatory network of the \u03b1-Syn-lysosome axis and provide a theoretical foundation for the development of novel therapeutic interventions for PD.<\/jats:p>","DOI":"10.3389\/fnins.2026.1885103","type":"journal-article","created":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T05:39:37Z","timestamp":1785130777000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":1,"title":["Research progress on the \u03b1-synuclein-lysosome axis in Parkinson\u2019s disease: molecular mechanisms of protein aggregation, autophagy dysfunction, and therapeutic targeting"],"prefix":"10.3389","volume":"20","author":[{"given":"Jiaojiao","family":"Fu","sequence":"first","affiliation":[{"name":"Department of Rehabilitation Medicine, The 960th Hospital of the PLA Joint Logistics Support Force","place":["Jinan, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chuanxi","family":"Zhu","sequence":"additional","affiliation":[{"name":"Department of Rehabilitation Medicine, The 960th Hospital of the PLA Joint Logistics Support Force","place":["Jinan, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhenzhen","family":"Fan","sequence":"additional","affiliation":[{"name":"Department of Rehabilitation Medicine, The 960th Hospital of the PLA Joint Logistics Support Force","place":["Jinan, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,7,27]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"2120","DOI":"10.15252\/embj.201593411","article-title":"Tunneling nanotubes spread fibrillar \u03b1-synuclein by intercellular trafficking of lysosomes.","volume":"35","author":"Abounit","year":"2016","journal-title":"EMBO J."},{"key":"B2","doi-asserted-by":"publisher","first-page":"7441","DOI":"10.1523\/JNEUROSCI.0636-16.2016","article-title":"A new glucocerebrosidase chaperone reduces \u03b1-synuclein and glycolipid levels in iPSC-derived dopaminergic neurons from patients with gaucher disease and parkinsonism.","volume":"36","author":"Aflaki","year":"2016","journal-title":"J. Neurosci."},{"key":"B3","doi-asserted-by":"publisher","DOI":"10.3390\/ijms23010398","article-title":"Metformin repurposing for Parkinson disease therapy: Opportunities and challenges.","volume":"23","author":"Agostini","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"B4","doi-asserted-by":"publisher","first-page":"522","DOI":"10.1111\/jnc.14808","article-title":"\u03b1-synuclein oligomers and fibrils: A spectrum of species, a spectrum of toxicities.","volume":"150","author":"Alam","year":"2019","journal-title":"J. Neurochem."},{"key":"B5","doi-asserted-by":"publisher","first-page":"102944","DOI":"10.1016\/j.ebiom.2020.102944","article-title":"Anti-\u03b1-synuclein ASO delivered to monoamine neurons prevents \u03b1-synuclein accumulation in a Parkinson\u2019s disease-like mouse model and in monkeys.","volume":"59","author":"Alarc\u00f3n-Ar\u00eds","year":"2020","journal-title":"EBioMedicine"},{"key":"B6","doi-asserted-by":"publisher","first-page":"2648","DOI":"10.1093\/brain\/awv179","article-title":"Glucocerebrosidase activity in Parkinson\u2019s disease with and without GBA mutations.","volume":"138","author":"Alcalay","year":"2015","journal-title":"Brain"},{"key":"B7","doi-asserted-by":"publisher","first-page":"328","DOI":"10.3389\/fnins.2019.00328","article-title":"Dysregulated lipid metabolism and its role in \u03b1-synucleinopathy in Parkinson\u2019s disease.","volume":"13","author":"Alecu","year":"2019","journal-title":"Front. Neurosci."},{"key":"B8","doi-asserted-by":"publisher","first-page":"2478","DOI":"10.1111\/febs.70363","article-title":"Familial mutations modulate \u03b1-Synuclein interactions with key neuronal membrane lipids.","volume":"293","author":"Ali","year":"2026","journal-title":"FEBS J"},{"key":"B9","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1186\/s13024-022-00544-w","article-title":"The role of NURR1 in metabolic abnormalities of Parkinson\u2019s disease.","volume":"17","author":"Al-Nusaif","year":"2022","journal-title":"Mol. Neurodegener."},{"key":"B10","doi-asserted-by":"publisher","first-page":"1464","DOI":"10.1001\/archneurol.2010.198","article-title":"Chaperone-mediated autophagy markers in Parkinson disease brains.","volume":"67","author":"Alvarez-Erviti","year":"2010","journal-title":"Arch. Neurol."},{"key":"B11","doi-asserted-by":"publisher","first-page":"e39465","DOI":"10.1371\/journal.pone.0039465","article-title":"Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo.","volume":"7","author":"Angot","year":"2012","journal-title":"PLoS One"},{"key":"B12","doi-asserted-by":"publisher","first-page":"5405","DOI":"10.3390\/ijms26115405","article-title":"\u03b1-Synuclein pathology in synucleinopathies: mechanisms, biomarkers, and therapeutic challenges.","volume":"26","author":"Arias-Carri\u00f3n","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"B13","doi-asserted-by":"publisher","first-page":"e13584","DOI":"10.1111\/acel.13584","article-title":"Acidic nanoparticles protect against \u03b1-Synuclein-induced neurodegeneration through the restoration of lysosomal function.","volume":"21","author":"Arotcarena","year":"2022","journal-title":"Aging Cell"},{"key":"B14","doi-asserted-by":"publisher","first-page":"565","DOI":"10.3390\/cells8060565","article-title":"Autophagy in synucleinopathy: the overwhelmed and defective machinery.","volume":"8","author":"Arotcarena","year":"2019","journal-title":"Cells"},{"key":"B15","doi-asserted-by":"publisher","first-page":"e153","DOI":"10.1038\/emm.2014.128","article-title":"Loss of glucocerebrosidase 1 activity causes lysosomal dysfunction and \u03b1-synuclein aggregation.","volume":"47","author":"Bae","year":"2015","journal-title":"Exp. Mol. Med."},{"key":"B16","doi-asserted-by":"publisher","first-page":"4755","DOI":"10.1038\/ncomms5755","article-title":"Glucocerebrosidase depletion enhances cell-to-cell transmission of \u03b1-synuclein.","volume":"5","author":"Bae","year":"2014","journal-title":"Nat. Commun."},{"key":"B17","doi-asserted-by":"publisher","first-page":"13270","DOI":"10.3390\/ijms241713270","article-title":"The bidirectional interplay of \u03b1-synuclein with lipids in the central nervous system and its implications for the pathogenesis of Parkinson\u2019s disease.","volume":"24","author":"Battis","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"B18","doi-asserted-by":"publisher","first-page":"107742","DOI":"10.1016\/j.jbc.2024.107742","article-title":"Alpha-synuclein, autophagy-lysosomal pathway, and Lewy bodies: Mutations, propagation, aggregation, and the formation of inclusions.","volume":"300","author":"Bayati","year":"2024","journal-title":"J. Biol. Chem."},{"key":"B19","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1002\/mds.27895","article-title":"The vicious cycle between \u03b1-synuclein aggregation and autophagic-lysosomal dysfunction.","volume":"35","author":"Bellomo","year":"2020","journal-title":"Mov. Disord."},{"key":"B20","doi-asserted-by":"publisher","first-page":"2332","DOI":"10.4103\/1673-5374.371345","article-title":"\u03b1-Synuclein oligomers and fibrils: Partners in crime in synucleinopathies.","volume":"18","author":"Bigi","year":"2023","journal-title":"Neural Regen. Res."},{"key":"B21","doi-asserted-by":"publisher","first-page":"2577406","DOI":"10.1080\/27694127.2025.2577406","article-title":"The role of autophagy in synucleinopathy: Clearance versus spread of \u03b1-synuclein.","volume":"4","author":"Birnbaum","year":"2025","journal-title":"Autophagy Rep."},{"key":"B22","doi-asserted-by":"publisher","first-page":"666585","DOI":"10.3389\/fchem.2021.666585","article-title":"\u03b1-Synuclein: An all-inclusive trip around its structure, influencing factors and applied techniques.","volume":"9","author":"Bisi","year":"2021","journal-title":"Front. Chem."},{"key":"B23","doi-asserted-by":"publisher","first-page":"1645","DOI":"10.1093\/hmg\/ddz004","article-title":"LRRK2 impairs PINK1\/Parkin-dependent mitophagy via its kinase activity: Pathologic insights into Parkinson\u2019s disease.","volume":"28","author":"Bonello","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"B24","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1080\/15548627.2015.1136769","article-title":"Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases.","volume":"12","author":"Bourdenx","year":"2016","journal-title":"Autophagy"},{"key":"B25","doi-asserted-by":"publisher","first-page":"6434","DOI":"10.1038\/onc.2008.310","article-title":"Lysosomal membrane permeabilization in cell death.","volume":"27","author":"Boya","year":"2008","journal-title":"Oncogene"},{"key":"B26","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1016\/s0197-4580(02)00065-9","article-title":"Staging of brain pathology related to sporadic Parkinson\u2019s disease.","volume":"24","author":"Braak","year":"2003","journal-title":"Neurobiol. Aging"},{"key":"B27","doi-asserted-by":"publisher","first-page":"396","DOI":"10.1016\/j.cmet.2022.02.001","article-title":"The NADPARK study: A randomized phase I trial of nicotinamide riboside supplementation in Parkinson\u2019s disease.","volume":"34","author":"Brakedal","year":"2022","journal-title":"Cell Metab."},{"key":"B28","doi-asserted-by":"publisher","first-page":"71","DOI":"10.3390\/neurosci5010005","article-title":"The role of astrocytes and alpha-synuclein in Parkinson\u2019s disease: A review.","volume":"5","author":"Brash-Arias","year":"2024","journal-title":"NeuroSci"},{"key":"B29","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1002\/ana.21541","article-title":"A critical evaluation of the Braak staging scheme for Parkinson\u2019s disease.","volume":"64","author":"Burke","year":"2008","journal-title":"Ann. Neurol."},{"key":"B30","doi-asserted-by":"publisher","first-page":"699","DOI":"10.3233\/JPD-150642","article-title":"The synaptic function of \u03b1-Synuclein.","volume":"5","author":"Burr\u00e9","year":"2015","journal-title":"J. Parkinsons Dis"},{"key":"B31","doi-asserted-by":"publisher","first-page":"E4274","DOI":"10.1073\/pnas.1416598111","article-title":"\u03b1-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation.","volume":"111","author":"Burr\u00e9","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B32","doi-asserted-by":"publisher","first-page":"862","DOI":"10.1110\/ps.041255905","article-title":"Helix periodicity, topology, and dynamics of membrane-associated alpha-synuclein.","volume":"14","author":"Bussell","year":"2005","journal-title":"Protein Sci."},{"key":"B33","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1038\/s41419-023-05835-8","article-title":"Tunnelling nanotubes between neuronal and microglial cells allow bi-directional transfer of \u03b1-Synuclein and mitochondria.","volume":"14","author":"Chakraborty","year":"2023","journal-title":"Cell. Death Dis."},{"key":"B34","doi-asserted-by":"publisher","first-page":"168023","DOI":"10.1016\/j.jmb.2023.168023","article-title":"Mechanisms of glucocerebrosidase dysfunction in Parkinson\u2019s disease.","volume":"435","author":"Chatterjee","year":"2023","journal-title":"J. Mol. Biol."},{"key":"B35","doi-asserted-by":"publisher","first-page":"1031","DOI":"10.1080\/14728222.2022.2166828","article-title":"Targeting protein clearance pathways in GBA1-associated Parkinson disease.","volume":"26","author":"Chen","year":"2022","journal-title":"Expert Opin. Ther. Targets"},{"key":"B36","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1186\/s13024-022-00560-w","article-title":"LRP1 is a neuronal receptor for \u03b1-synuclein uptake and spread.","volume":"17","author":"Chen","year":"2022","journal-title":"Mol. Neurodegener."},{"key":"B37","doi-asserted-by":"publisher","first-page":"7205","DOI":"10.3390\/ijms24087205","article-title":"Gut-to-brain \u03b1-synuclein transmission in parkinson\u2019s disease: evidence for prion-like mechanisms.","volume":"24","author":"Chen","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"B38","doi-asserted-by":"publisher","first-page":"E1994","DOI":"10.1073\/pnas.1421204112","article-title":"Structural characterization of toxic oligomers that are kinetically trapped during \u03b1-synuclein fibril formation.","volume":"112","author":"Chen","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B39","doi-asserted-by":"publisher","first-page":"1612389","DOI":"10.3389\/fnagi.2025.1612389","article-title":"Nurr1 deficiency impairs autophagy-lysosomal function through GBA-dependent transcriptional regulation in Parkinson\u2019s disease pathogenesis.","volume":"17","author":"Cheng","year":"2025","journal-title":"Front. Aging Neurosci."},{"key":"B40","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1126\/science.2799391","article-title":"A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins.","volume":"246","author":"Chiang","year":"1989","journal-title":"Science"},{"key":"B41","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1016\/j.febslet.2004.09.038","article-title":"Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein.","volume":"576","author":"Choi","year":"2004","journal-title":"FEBS Lett."},{"key":"B42","doi-asserted-by":"publisher","first-page":"e55375","DOI":"10.1371\/journal.pone.0055375","article-title":"Triggering of inflammasome by aggregated \u03b1-synuclein, an inflammatory response in synucleinopathies.","volume":"8","author":"Codolo","year":"2013","journal-title":"PLoS One"},{"key":"B43","doi-asserted-by":"publisher","first-page":"21","DOI":"10.5802\/crbiol.174","article-title":"Parkinson\u2019s disease: From genetics to targeted therapies.","volume":"348","author":"Cogan","year":"2025","journal-title":"Comptes Rendus Biol."},{"key":"B44","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.arr.2016.05.004","article-title":"Disorders of lysosomal acidification-The emerging role of v-ATPase in aging and neurodegenerative disease.","volume":"32","author":"Colacurcio","year":"2016","journal-title":"Ageing Res. Rev."},{"key":"B45","doi-asserted-by":"publisher","first-page":"e135633","DOI":"10.1172\/jci.insight.135633","article-title":"\u03b1-Synuclein antisense oligonucleotides as a disease-modifying therapy for Parkinson\u2019s disease.","volume":"6","author":"Cole","year":"2021","journal-title":"JCI Insight"},{"key":"B46","doi-asserted-by":"publisher","first-page":"e000535","DOI":"10.1136\/bmjno-2023-000535","article-title":"Ambroxol as a disease-modifying treatment to reduce the risk of cognitive impairment in GBA-associated Parkinson\u2019s disease: a multicentre, randomised, double-blind, placebo-controlled, phase II trial. The AMBITIOUS study protocol.","volume":"5","author":"Colucci","year":"2023","journal-title":"BMJ Neurol. Open"},{"key":"B47","doi-asserted-by":"publisher","first-page":"1048","DOI":"10.1016\/j.cell.2012.03.037","article-title":"Direct observation of the interconversion of normal and toxic forms of \u03b1-synuclein.","volume":"149","author":"Cremades","year":"2012","journal-title":"Cell"},{"key":"B48","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1038\/nrd.2016.220","article-title":"Lysosomal storage diseases: HSP70 reverses lysosomal pathology.","volume":"15","author":"Crunkhorn","year":"2016","journal-title":"Nat. Rev. Drug Discov."},{"key":"B49","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1016\/j.neuron.2019.09.001","article-title":"Stress-induced cellular clearance is mediated by the SNARE protein ykt6 and disrupted by \u03b1-synuclein.","volume":"104","author":"Cuddy","year":"2019","journal-title":"Neuron"},{"key":"B50","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1126\/science.273.5274.501","article-title":"A receptor for the selective uptake and degradation of proteins by lysosomes.","volume":"273","author":"Cuervo","year":"1996","journal-title":"Science"},{"key":"B51","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1038\/cr.2013.153","article-title":"Chaperone-mediated autophagy: Roles in disease and aging.","volume":"24","author":"Cuervo","year":"2014","journal-title":"Cell Res"},{"key":"B52","doi-asserted-by":"publisher","first-page":"1292","DOI":"10.1126\/science.1101738","article-title":"Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy.","volume":"305","author":"Cuervo","year":"2004","journal-title":"Science"},{"key":"B53","doi-asserted-by":"publisher","first-page":"3919","DOI":"10.1074\/jbc.M116.759373","article-title":"Dissecting the molecular pathway involved in PLK2 kinase-mediated \u03b1-synuclein-selective autophagic degradation.","volume":"292","author":"Dahmene","year":"2017","journal-title":"J. Biol. Chem."},{"key":"B54","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1007\/s00018-024-05419-5","article-title":"Lysosomal dysfunction in \u03b1-synuclein pathology: molecular mechanisms and therapeutic strategies.","volume":"81","author":"Dai","year":"2024","journal-title":"Cell Mol. Life Sci."},{"key":"B55","doi-asserted-by":"publisher","first-page":"2075","DOI":"10.1002\/mds.29162","article-title":"\u03b1-Synuclein V15A variant in familial Parkinson\u2019s disease exhibits a weaker lipid-binding property.","volume":"37","author":"Daida","year":"2022","journal-title":"Mov. Disord."},{"key":"B56","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1186\/1750-1326-7-42","article-title":"Exosomal cell-to-cell transmission of alpha synuclein oligomers.","volume":"7","author":"Danzer","year":"2012","journal-title":"Mol. Neurodegener."},{"key":"B57","doi-asserted-by":"publisher","first-page":"e98649","DOI":"10.7554\/eLife.98649","article-title":"Novel autophagy inducers by accelerating lysosomal clustering against Parkinson\u2019s disease.","volume":"13","author":"Date","year":"2024","journal-title":"Elife"},{"key":"B58","doi-asserted-by":"publisher","first-page":"9443","DOI":"10.1074\/jbc.273.16.9443","article-title":"Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes.","volume":"273","author":"Davidson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"B59","doi-asserted-by":"publisher","first-page":"a041644","DOI":"10.1101\/cshperspect.a041644","article-title":"Animal models of Parkinson\u2019s disease.","volume":"15","author":"Dawson","year":"2025","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"B60","doi-asserted-by":"publisher","first-page":"1006","DOI":"10.3390\/genes12071006","article-title":"The genetics of Parkinson\u2019s disease and implications for clinical practice.","volume":"12","author":"Day","year":"2021","journal-title":"Genes"},{"key":"B61","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1016\/S1474-4422(15)00006-X","article-title":"Targeting \u03b1-synuclein for treatment of Parkinson\u2019s disease: Mechanistic and therapeutic considerations.","volume":"14","author":"Dehay","year":"2015","journal-title":"Lancet Neurol."},{"key":"B62","doi-asserted-by":"publisher","first-page":"12535","DOI":"10.1523\/JNEUROSCI.1920-10.2010","article-title":"Pathogenic lysosomal depletion in Parkinson\u2019s disease.","volume":"30","author":"Dehay","year":"2010","journal-title":"J. Neurosci."},{"key":"B63","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1002\/mds.25462","article-title":"Lysosomal impairment in Parkinson\u2019s disease.","volume":"28","author":"Dehay","year":"2013","journal-title":"Mov. Disord."},{"key":"B64","doi-asserted-by":"publisher","first-page":"13010","DOI":"10.1073\/pnas.0903691106","article-title":"Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein.","volume":"106","author":"Desplats","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B65","doi-asserted-by":"publisher","first-page":"e3001287","DOI":"10.1371\/journal.pbio.3001287","article-title":"\u03b1-Synuclein fibrils subvert lysosome structure and function for the propagation of protein misfolding between cells through tunneling nanotubes.","volume":"19","author":"Dilsizoglu Senol","year":"2021","journal-title":"PLoS Biol."},{"key":"B66","doi-asserted-by":"publisher","first-page":"758","DOI":"10.1111\/jnc.13712","article-title":"Rab7 induces clearance of \u03b1-synuclein aggregates.","volume":"138","author":"Dinter","year":"2016","journal-title":"J. Neurochem."},{"key":"B67","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1186\/s40035-023-00368-8","article-title":"Animal models of Parkinson\u2019s disease: Bridging the gap between disease hallmarks and research questions.","volume":"12","author":"Dovonou","year":"2023","journal-title":"Transl. Neurodegener."},{"key":"B68","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1186\/s40035-023-00363-z","article-title":"Reciprocal effects of alpha-synuclein aggregation and lysosomal homeostasis in synucleinopathy models.","volume":"12","author":"Drobny","year":"2023","journal-title":"Transl. Neurodegener."},{"key":"B69","doi-asserted-by":"publisher","first-page":"14508","DOI":"10.1523\/JNEUROSCI.1560-11.2011","article-title":"Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of \u03b1-synuclein.","volume":"31","author":"Ebrahimi-Fakhari","year":"2011","journal-title":"J. Neurosci."},{"key":"B70","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1007\/s00401-012-1004-6","article-title":"Protein degradation pathways in Parkinson\u2019s disease: Curse or blessing.","volume":"124","author":"Ebrahimi-Fakhari","year":"2012","journal-title":"Acta Neuropathol."},{"key":"B71","doi-asserted-by":"publisher","first-page":"1721","DOI":"10.1152\/physrev.00041.2021","article-title":"Mitochondrial quality control in health and in Parkinson\u2019s disease.","volume":"102","author":"Eldeeb","year":"2022","journal-title":"Physiol. Rev."},{"key":"B72","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1007\/s00702-020-02167-1","article-title":"Parkinson\u2019s disease treatment: Past, present, and future.","volume":"127","author":"Elsworth","year":"2020","journal-title":"J. Neural Transm."},{"key":"B73","doi-asserted-by":"publisher","first-page":"865","DOI":"10.3390\/biom5020865","article-title":"Mechanisms of alpha-synuclein action on neurotransmission: Cell-autonomous and non-cell autonomous role.","volume":"5","author":"Emanuele","year":"2015","journal-title":"Biomolecules"},{"key":"B74","doi-asserted-by":"publisher","first-page":"5512","DOI":"10.1038\/s41467-022-33252-6","article-title":"Small soluble \u03b1-synuclein aggregates are the toxic species in Parkinson\u2019s disease.","volume":"13","author":"Emin","year":"2022","journal-title":"Nat. Commun."},{"key":"B75","doi-asserted-by":"publisher","first-page":"e938519","DOI":"10.12659\/MSM.938519","article-title":"Autophagy and its association with genetic mutations in Parkinson disease.","volume":"28","author":"Erekat","year":"2022","journal-title":"Med. Sci. Monit."},{"key":"B76","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.ejcb.2017.01.002","article-title":"Impact of high cholesterol in a Parkinson\u2019s disease model: Prevention of lysosomal leakage versus stimulation of \u03b1-synuclein aggregation.","volume":"96","author":"Eriksson","year":"2017","journal-title":"Eur. J. Cell. Biol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"105966","DOI":"10.1016\/j.nbd.2022.105966","article-title":"Monitoring \u03b1-synuclein aggregation.","volume":"176","author":"Estaun-Panzano","year":"2023","journal-title":"Neurobiol. Dis."},{"key":"B78","doi-asserted-by":"publisher","first-page":"1441","DOI":"10.3390\/cells13171441","article-title":"ATPase dysfunction in the brain: Genetic insights and therapeutic opportunities.","volume":"13","author":"Falace","year":"2024","journal-title":"Cells"},{"key":"B79","doi-asserted-by":"publisher","first-page":"342","DOI":"10.1016\/j.stemcr.2016.01.013","article-title":"ER stress and autophagic perturbations lead to elevated extracellular \u03b1-Synuclein in GBA-N370S Parkinson\u2019s iPSC-derived dopamine neurons.","volume":"6","author":"Fernandes","year":"2016","journal-title":"Stem. Cell. Rep"},{"key":"B80","doi-asserted-by":"publisher","first-page":"299","DOI":"10.3389\/fnmol.2019.00299","article-title":"Targeting alpha-synuclein as a therapy for Parkinson\u2019s disease.","volume":"12","author":"Fields","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"B81","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1016\/j.neuron.2022.01.017","article-title":"The different autophagy degradation pathways and neurodegeneration.","volume":"110","author":"Fleming","year":"2022","journal-title":"Neuron"},{"key":"B82","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1007\/s00401-023-02601-0","article-title":"More than meets the eye in Parkinson\u2019s disease and other synucleinopathies: From proteinopathy to lipidopathy.","volume":"146","author":"Flores-Leon","year":"2023","journal-title":"Acta Neuropathol."},{"key":"B83","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1111\/tra.12136","article-title":"The Vps35 D620N mutation linked to Parkinson\u2019s disease disrupts the cargo sorting function of retromer.","volume":"15","author":"Follett","year":"2014","journal-title":"Traffic"},{"key":"B84","doi-asserted-by":"publisher","first-page":"e62143","DOI":"10.1371\/journal.pone.0062143","article-title":"Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis.","volume":"8","author":"Freeman","year":"2013","journal-title":"PLoS One"},{"key":"B85","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/ncb748","article-title":"alpha-Synuclein is phosphorylated in synucleinopathy lesions.","volume":"4","author":"Fujiwara","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"B86","doi-asserted-by":"publisher","first-page":"433","DOI":"10.3233\/JPD-171103","article-title":"The role of lipids interacting with \u03b1-Synuclein in the pathogenesis of Parkinson\u2019s disease.","volume":"7","author":"Galvagnion","year":"2017","journal-title":"J. Parkinsons Dis."},{"key":"B87","doi-asserted-by":"publisher","first-page":"1038","DOI":"10.1093\/brain\/awab371","article-title":"Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote \u03b1-synuclein aggregation.","volume":"145","author":"Galvagnion","year":"2022","journal-title":"Brain"},{"key":"B88","doi-asserted-by":"publisher","first-page":"527","DOI":"10.3389\/fneur.2017.00527","article-title":"Mitophagy in Parkinson\u2019s disease: Pathogenic and therapeutic implications.","volume":"8","author":"Gao","year":"2017","journal-title":"Front. Neurol."},{"key":"B89","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1002\/ana.23614","article-title":"Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains.","volume":"72","author":"Gegg","year":"2012","journal-title":"Ann. Neurol."},{"key":"B90","doi-asserted-by":"publisher","first-page":"28261","DOI":"10.1074\/jbc.M110.157214","article-title":"The lipid-binding domain of wild type and mutant alpha-Synuclein: compactness and interconversion between the broken and extended helix forms.","volume":"285","author":"Georgieva","year":"2010","journal-title":"J. Biol. Chem."},{"key":"B91","doi-asserted-by":"publisher","first-page":"985","DOI":"10.1126\/science.290.5493.985","article-title":"Oxidative damage linked to neurodegeneration by selective alpha-Synuclein nitration in synucleinopathy lesions.","volume":"290","author":"Giasson","year":"2000","journal-title":"Science"},{"key":"B92","doi-asserted-by":"publisher","first-page":"e1529","DOI":"10.1212\/WNL.0000000000206772","article-title":"Cutaneous \u03b1-Synuclein signatures in patients with multiple system atrophy and Parkinson disease.","volume":"100","author":"Gibbons","year":"2023","journal-title":"Neurology"},{"key":"B93","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1093\/brain\/aww230","article-title":"Like prions: the propagation of aggregated tau and \u03b1-synuclein in neurodegeneration.","volume":"140","author":"Goedert","year":"2017","journal-title":"Brain"},{"key":"B94","doi-asserted-by":"publisher","first-page":"e2409040","DOI":"10.1002\/advs.202409040","article-title":"\u03b1-Synuclein pathology spreads in a midbrain-hindbrain assembloid model.","volume":"12","author":"Gomez-Giro","year":"2025","journal-title":"Adv. Sci."},{"key":"B95","doi-asserted-by":"publisher","first-page":"6779","DOI":"10.1093\/hmg\/ddu395","article-title":"LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity.","volume":"23","author":"G\u00f3mez-Suaga","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"B96","doi-asserted-by":"publisher","first-page":"7253","DOI":"10.1007\/s12035-023-03530-5","article-title":"Metformin and trehalose-modulated autophagy exerts a neurotherapeutic effect on Parkinson\u2019s disease.","volume":"60","author":"Gopar-Cuevas","year":"2023","journal-title":"Mol. Neurobiol."},{"key":"B97","doi-asserted-by":"publisher","first-page":"7800","DOI":"10.1074\/jbc.M411638200","article-title":"The E46K mutation in alpha-synuclein increases amyloid fibril formation.","volume":"280","author":"Greenbaum","year":"2005","journal-title":"J. Biol. Chem."},{"key":"B98","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1124\/pharmrev.120.000133","article-title":"Therapeutics in the pipeline targeting \u03b1-synuclein for Parkinson\u2019s disease.","volume":"74","author":"Grosso Jasutkar","year":"2022","journal-title":"Pharmacol. Rev."},{"key":"B99","doi-asserted-by":"publisher","first-page":"452","DOI":"10.3390\/cells8050452","article-title":"Synergistic effect of mitochondrial and lysosomal dysfunction in Parkinson\u2019s disease.","volume":"8","author":"Guerra","year":"2019","journal-title":"Cells"},{"key":"B100","doi-asserted-by":"publisher","first-page":"e48907","DOI":"10.7554\/eLife.48907","article-title":"Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.","volume":"8","author":"Guerrero-Ferreira","year":"2019","journal-title":"Elife"},{"key":"B101","doi-asserted-by":"publisher","first-page":"45","DOI":"10.3389\/fncel.2020.00045","article-title":"Proteostasis of \u03b1-synuclein and its role in the pathogenesis of Parkinson\u2019s disease.","volume":"14","author":"Han","year":"2020","journal-title":"Front. Cell. Neurosci."},{"key":"B102","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/s0092-8674(02)00833-4","article-title":"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action.","volume":"110","author":"Hara","year":"2002","journal-title":"Cell"},{"key":"B103","doi-asserted-by":"publisher","first-page":"802","DOI":"10.1016\/j.amjmed.2019.03.001","article-title":"Parkinson\u2019s disease and parkinsonism.","volume":"132","author":"Hayes","year":"2019","journal-title":"Am. J. Med."},{"key":"B104","doi-asserted-by":"publisher","first-page":"2258","DOI":"10.1007\/s12035-015-9173-7","article-title":"Treatment with trehalose prevents behavioral and neurochemical deficits produced in an AAV \u03b1-synuclein rat model of Parkinson\u2019s disease.","volume":"53","author":"He","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"B105","doi-asserted-by":"publisher","first-page":"1248","DOI":"10.1038\/s41593-019-0457-5","article-title":"Spread of \u03b1-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis.","volume":"22","author":"Henderson","year":"","journal-title":"Nat. Neurosci."},{"key":"B106","doi-asserted-by":"publisher","first-page":"134316","DOI":"10.1016\/j.neulet.2019.134316","article-title":"\u03b1-Synuclein pathology in Parkinson\u2019s disease and related \u03b1-synucleinopathies.","volume":"709","author":"Henderson","year":"","journal-title":"Neurosci. Lett."},{"key":"B107","doi-asserted-by":"publisher","first-page":"1574755","DOI":"10.3389\/fimmu.2025.1574755","article-title":"Engineered sequestrins inhibit aggregation of pathogenic alpha-synuclein mutants.","volume":"16","author":"Hjelm","year":"2025","journal-title":"Front. Immunol."},{"key":"B108","doi-asserted-by":"publisher","first-page":"544","DOI":"10.1038\/s41598-018-35811-8","article-title":"Extracellular aggregated alpha synuclein primarily triggers lysosomal dysfunction in neural cells prevented by trehalose.","volume":"9","author":"Hoffmann","year":"2019","journal-title":"Sci. Rep."},{"key":"B109","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/j.neulet.2004.05.100","article-title":"Alpha-synuclein missense and multiplication mutations in autosomal dominant Parkinson\u2019s disease.","volume":"367","author":"Hope","year":"2004","journal-title":"Neurosci. Lett."},{"key":"B110","doi-asserted-by":"publisher","first-page":"e13175","DOI":"10.1111\/bpa.13175","article-title":"Alpha-synuclein-associated changes in PINK1-PRKN-mediated mitophagy are disease context dependent.","volume":"33","author":"Hou","year":"2023","journal-title":"Brain Pathol."},{"key":"B111","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1016\/s0002-9440(10)64553-1","article-title":"alpha-synuclein promotes mitochondrial deficit and oxidative stress.","volume":"157","author":"Hsu","year":"2000","journal-title":"Am. J. Pathol."},{"key":"B112","doi-asserted-by":"publisher","first-page":"13","DOI":"10.3892\/mmr.2024.13378","article-title":"Selective protein degradation through chaperone-mediated autophagy: Implications for cellular homeostasis and disease (Review).","volume":"31","author":"Huang","year":"2025","journal-title":"Mol. Med. Rep."},{"key":"B113","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1186\/2047-9158-1-2","article-title":"Macroautophagy in sporadic and the genetic form of Parkinson\u2019s disease with the A53T \u03b1-synuclein mutation.","volume":"1","author":"Huang","year":"2012","journal-title":"Transl. Neurodegener."},{"key":"B114","doi-asserted-by":"publisher","first-page":"156652","DOI":"10.1016\/j.phymed.2025.156652","article-title":"Apigenin enhances Nrf2-induced chaperone-mediated autophagy and mitigates \u03b1-synuclein pathology: Implications for Parkinson\u2019s disease therapy.","volume":"141","author":"Huang","year":"2025","journal-title":"Phytomedicine"},{"key":"B115","doi-asserted-by":"publisher","first-page":"1898","DOI":"10.1080\/15548627.2018.1491489","article-title":"The lysosomal membrane protein LAMP2A promotes autophagic flux and prevents SNCA-induced Parkinson disease-like symptoms in the Drosophila brain.","volume":"14","author":"Issa","year":"2018","journal-title":"Autophagy"},{"key":"B116","doi-asserted-by":"publisher","first-page":"8338","DOI":"10.3390\/ijms22158338","article-title":"The prion-like spreading of alpha-synuclein in Parkinson\u2019s disease: update on models and hypotheses.","volume":"22","author":"Jan","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"B117","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1002\/mds.28810","article-title":"Parkinson\u2019s disease phenotypes in patient neuronal cultures and brain organoids improved by 2-hydroxypropyl-\u03b2-cyclodextrin treatment.","volume":"37","author":"Jarazo","year":"2022","journal-title":"Mov. Disord."},{"key":"B118","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1186\/s12964-025-02310-z","article-title":"Lysosomal targeting of liposomes with acidic pH and Cathepsin B induces protein aggregate clearance.","volume":"23","author":"Jeon","year":"2025","journal-title":"Cell. Commun. Signal."},{"key":"B119","doi-asserted-by":"publisher","first-page":"471","DOI":"10.3390\/genes13030471","article-title":"Monogenic Parkinson\u2019s disease: Genotype, phenotype, pathophysiology, and genetic testing.","volume":"13","author":"Jia","year":"2022","journal-title":"Genes"},{"key":"B120","doi-asserted-by":"publisher","first-page":"139","DOI":"10.4103\/NRR.NRR-D-23-01195","article-title":"The autophagy-lysosome pathway: A potential target in the chemical and gene therapeutic strategies for Parkinson\u2019s disease.","volume":"20","author":"Jiao","year":"2025","journal-title":"Neural. Regen. Res."},{"key":"B121","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1006\/jmbi.2001.5269","article-title":"Defective membrane interactions of familial Parkinson\u2019s disease mutant A30P alpha-synuclein.","volume":"315","author":"Jo","year":"2002","journal-title":"J. Mol. Biol."},{"key":"B122","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1007\/s10495-009-0452-5","article-title":"Regulation of apoptosis-associated lysosomal membrane permeabilization.","volume":"15","author":"Johansson","year":"2010","journal-title":"Apoptosis"},{"key":"B123","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1186\/s13024-024-00779-9","article-title":"The Parkinson\u2019s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons.","volume":"19","author":"Jones-Tabah","year":"2024","journal-title":"Mol. Neurodegener."},{"key":"B124","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1083\/jcb.201402104","article-title":"PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.","volume":"205","author":"Kane","year":"2014","journal-title":"J. Cell. Biol."},{"key":"B125","doi-asserted-by":"publisher","first-page":"eadd0499","DOI":"10.1126\/scitranslmed.add0499","article-title":"Enhanced mTORC1 signaling and protein synthesis in pathologic \u03b1-synuclein cellular and animal models of Parkinson\u2019s disease.","volume":"15","author":"Khan","year":"2023","journal-title":"Sci. Transl. Med."},{"key":"B126","doi-asserted-by":"publisher","first-page":"1618","DOI":"10.1111\/j.1742-4658.2010.07588.x","article-title":"The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase.","volume":"277","author":"Khanna","year":"2010","journal-title":"FEBS J."},{"key":"B127","doi-asserted-by":"publisher","first-page":"e1011920","DOI":"10.1371\/journal.ppat.1011920","article-title":"The role of \u03b1-synuclein prion strains in Parkinson\u2019s disease and multiple system atrophy.","volume":"20","author":"Khedmatgozar","year":"2024","journal-title":"PLoS Pathog."},{"key":"B128","doi-asserted-by":"publisher","first-page":"17482","DOI":"10.1021\/ja9077599","article-title":"Structural properties of pore-forming oligomers of alpha-synuclein.","volume":"131","author":"Kim","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"B129","doi-asserted-by":"publisher","first-page":"2418","DOI":"10.1038\/s12276-025-01579-x","article-title":"Failure of lysosomal acidification and endomembrane network in neurodegeneration.","volume":"57","author":"Kim","year":"2025","journal-title":"Exp. Mol. Med."},{"key":"B130","doi-asserted-by":"publisher","first-page":"621","DOI":"10.3390\/cells12040621","article-title":"Pathogenic aspects and therapeutic avenues of autophagy in Parkinson\u2019s disease.","volume":"12","author":"Kinet","year":"2023","journal-title":"Cells"},{"key":"B131","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1038\/nature08710","article-title":"Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology.","volume":"463","author":"Kirkegaard","year":"2010","journal-title":"Nature"},{"key":"B132","doi-asserted-by":"publisher","first-page":"909273","DOI":"10.3389\/fnagi.2022.909273","article-title":"Impact of aging on animal models of Parkinson\u2019s disease.","volume":"14","author":"Kl\u00e6strup","year":"2022","journal-title":"Front. Aging Neurosci."},{"key":"B133","doi-asserted-by":"publisher","first-page":"25497","DOI":"10.1074\/jbc.M400255200","article-title":"Hsp70 reduces alpha-Synuclein aggregation and toxicity.","volume":"279","author":"Klucken","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B134","doi-asserted-by":"publisher","first-page":"S1","DOI":"10.1016\/j.parkreldis.2015.09.007","article-title":"Autosomal dominant Parkinson\u2019s disease caused by SNCA duplications.","volume":"22","author":"Konno","year":"2016","journal-title":"Parkinsonism. Relat. Disord."},{"key":"B135","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.parkreldis.2021.02.003","article-title":"Ambroxol increases glucocerebrosidase (GCase) activity and restores GCase translocation in primary patient-derived macrophages in Gaucher disease and Parkinsonism.","volume":"84","author":"Kopytova","year":"2021","journal-title":"Parkinsonism. Relat. Disord."},{"key":"B136","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson\u2019s disease.","volume":"18","author":"Kr\u00fcger","year":"1998","journal-title":"Nat. Genet."},{"key":"B137","doi-asserted-by":"publisher","first-page":"1888","DOI":"10.1093\/hmg\/ddad025","article-title":"Acid ceramidase involved in pathogenic cascade leading to accumulation of \u03b1-synuclein in iPSC model of GBA1-associated Parkinson\u2019s disease.","volume":"32","author":"Kumar","year":"2023","journal-title":"Hum. Mol. Genet."},{"key":"B138","doi-asserted-by":"publisher","first-page":"1919","DOI":"10.1021\/acschemneuro.1c00001","article-title":"Ellagic acid inhibits \u03b1-synuclein aggregation at multiple stages and reduces its cytotoxicity.","volume":"12","author":"Kumar","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"B139","doi-asserted-by":"publisher","first-page":"eabm6393","DOI":"10.1126\/sciadv.abm6393","article-title":"Mutant glucocerebrosidase impairs \u03b1-synuclein degradation by blockade of chaperone-mediated autophagy.","volume":"8","author":"Kuo","year":"2022","journal-title":"Sci. Adv."},{"key":"B140","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1038\/s41531-024-00842-8","article-title":"Mitochondrial oxidant stress promotes \u03b1-synuclein aggregation and spreading in mice with mutated glucocerebrosidase.","volume":"10","author":"La Vitola","year":"2024","journal-title":"NPJ Parkinsons Dis"},{"key":"B141","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1002\/mds.27360","article-title":"Disease modification in Parkinson\u2019s disease: current approaches, challenges, and future considerations.","volume":"33","author":"Lang","year":"2018","journal-title":"Mov. Disord."},{"key":"B142","doi-asserted-by":"publisher","first-page":"408","DOI":"10.1056\/NEJMoa2203395","article-title":"Trial of cinpanemab in early Parkinson\u2019s disease.","volume":"387","author":"Lang","year":"2022","journal-title":"N. Engl. J. Med."},{"key":"B143","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of \u03b1-synuclein: From structure and toxicity to therapeutic target.","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"B144","doi-asserted-by":"publisher","first-page":"e22","DOI":"10.1038\/emm.2013.45","article-title":"Autophagic failure promotes the exocytosis and intercellular transfer of \u03b1-synuclein.","volume":"45","author":"Lee","year":"2013","journal-title":"Exp. Mol. Med."},{"key":"B145","doi-asserted-by":"publisher","first-page":"e70363","DOI":"10.1111\/jnc.70363","article-title":"Zinc-mediated lysosomal destabilization links mitochondrial damage to neuronal death in a cellular MPP+ Model of Parkinson\u2019s disease.","volume":"170","author":"Lee","year":"2026","journal-title":"J. Neurochem."},{"key":"B146","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1080\/15548627.2023.2274711","article-title":"Targeted degradation of SNCA\/\u03b1-synuclein aggregates in neurodegeneration using the AUTOTAC chemical platform.","volume":"20","author":"Lee","year":"2024","journal-title":"Autophagy"},{"key":"B147","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1038\/s41419-019-1364-0","article-title":"A30P mutant \u03b1-synuclein impairs autophagic flux by inactivating JNK signaling to enhance ZKSCAN3 activity in midbrain dopaminergic neurons.","volume":"10","author":"Lei","year":"2019","journal-title":"Cell Death Dis"},{"key":"B148","doi-asserted-by":"publisher","first-page":"e49750","DOI":"10.1371\/journal.pone.0049750","article-title":"Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson\u2019s disease associated mutations A53T and E46K.","volume":"8","author":"Lemkau","year":"2013","journal-title":"PLoS One"},{"key":"B149","doi-asserted-by":"publisher","first-page":"104021","DOI":"10.1016\/j.ebiom.2022.104021","article-title":"Safety, tolerability and pharmacokinetics of the oligomer modulator anle138b with exposure levels sufficient for therapeutic efficacy in a murine Parkinson model: A randomised, double-blind, placebo-controlled phase 1a trial.","volume":"80","author":"Levin","year":"2022","journal-title":"EBioMedicine"},{"key":"B150","doi-asserted-by":"publisher","first-page":"3609","DOI":"10.1038\/s41467-018-05971-2","article-title":"Cryo-EM of full-length \u03b1-synuclein reveals fibril polymorphs with a common structural kernel.","volume":"9","author":"Li","year":"2018","journal-title":"Nat. Commun."},{"key":"B151","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.parkreldis.2010.12.008","article-title":"A new perspective in Parkinson\u2019s disease, chaperone-mediated autophagy.","volume":"17","author":"Li","year":"2011","journal-title":"Parkinsonism Relat. Disord."},{"key":"B152","doi-asserted-by":"publisher","first-page":"562","DOI":"10.1016\/j.ijbiomac.2020.06.274","article-title":"Copper and iron ions accelerate the prion-like propagation of \u03b1-Synuclein: A vicious cycle in Parkinson\u2019s disease.","volume":"163","author":"Li","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"B153","doi-asserted-by":"publisher","first-page":"233","DOI":"10.4103\/NRR.NRR-D-24-00764","article-title":"Targeting the glymphatic system to promote \u03b1-synuclein clearance: A novel therapeutic strategy for Parkinson\u2019s disease.","volume":"21","author":"Lian","year":"2026","journal-title":"Neural Regen. Res."},{"key":"B154","doi-asserted-by":"publisher","first-page":"5312","DOI":"10.3390\/ijms20215312","article-title":"The overcrowded crossroads: mitochondria, alpha-synuclein, and the endo-lysosomal system interaction in Parkinson\u2019s disease.","volume":"20","author":"Lin","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"B155","doi-asserted-by":"publisher","first-page":"3196","DOI":"10.1080\/15548627.2020.1850008","article-title":"Aberrant mitochondrial morphology and function associated with impaired mitophagy and DNM1L-MAPK\/ERK signaling are found in aged mutant Parkinsonian LRRK2R1441G mice.","volume":"17","author":"Liu","year":"2021","journal-title":"Autophagy"},{"key":"B156","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1039\/d1fo02534a","article-title":"Urolithin A protects dopaminergic neurons in experimental models of Parkinson\u2019s disease by promoting mitochondrial biogenesis through the SIRT1\/PGC-1\u03b1 signaling pathway.","volume":"13","author":"Liu","year":"2022","journal-title":"Food Funct"},{"key":"B157","doi-asserted-by":"publisher","first-page":"712","DOI":"10.3390\/cells8070712","article-title":"Mitophagy in Parkinson\u2019s disease: From pathogenesis to treatment.","volume":"8","author":"Liu","year":"2019","journal-title":"Cells"},{"key":"B158","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1007\/s11064-012-0909-8","article-title":"Therapeutic effects of rapamycin on MPTP-induced Parkinsonism in mice.","volume":"38","author":"Liu","year":"2013","journal-title":"Neurochem. Res."},{"key":"B159","doi-asserted-by":"publisher","first-page":"100972","DOI":"10.1016\/j.mam.2021.100972","article-title":"Neuronal autophagy and mitophagy in Parkinson\u2019s disease.","volume":"82","author":"Lizama","year":"2021","journal-title":"Mol. Aspects Med."},{"key":"B160","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1186\/s40035-023-00362-0","article-title":"Defective lysosomal acidification: A new prognostic marker and therapeutic target for neurodegenerative diseases.","volume":"12","author":"Lo","year":"2023","journal-title":"Transl. Neurodegener."},{"key":"B161","doi-asserted-by":"publisher","first-page":"e02906","DOI":"10.1002\/adhm.202502906","article-title":"Lysosome-acidifying nanoparticles rescue A30P \u03b1-synuclein induced neuronal death in cellular and drosophila models of Parkinson\u2019s disease.","volume":"15","author":"Lo","year":"2026","journal-title":"Adv. Healthc. Mater."},{"key":"B162","doi-asserted-by":"publisher","first-page":"435","DOI":"10.3390\/biom5020435","article-title":"The Interplay between alpha-synuclein clearance and spreading.","volume":"5","author":"Lopes da Fonseca","year":"2015","journal-title":"Biomolecules"},{"key":"B163","doi-asserted-by":"publisher","first-page":"949","DOI":"10.1126\/science.1227157","article-title":"Pathological \u03b1-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice.","volume":"338","author":"Luk","year":"2012","journal-title":"Science"},{"key":"B164","doi-asserted-by":"publisher","first-page":"20051","DOI":"10.1073\/pnas.0908005106","article-title":"Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells.","volume":"106","author":"Luk","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B165","doi-asserted-by":"publisher","first-page":"1030390","DOI":"10.3389\/fcell.2022.1030390","article-title":"Mitochondrial dysfunction of induced pluripotent stem cells-based neurodegenerative disease modeling and therapeutic strategy.","volume":"10","author":"Luo","year":"2022","journal-title":"Front. Cell. Dev. Biol."},{"key":"B166","doi-asserted-by":"publisher","first-page":"729","DOI":"10.1038\/s41419-023-06251-8","article-title":"Aggregation of alpha-synuclein disrupts mitochondrial metabolism and induce mitophagy via cardiolipin externalization.","volume":"14","author":"Lurette","year":"2023","journal-title":"Cell Death Dis."},{"key":"B167","doi-asserted-by":"publisher","first-page":"2107","DOI":"10.1038\/cdd.2015.79","article-title":"Fibril growth and seeding capacity play key roles in \u03b1-synuclein-mediated apoptotic cell death.","volume":"22","author":"Mahul-Mellier","year":"2015","journal-title":"Cell. Death Differ."},{"key":"B168","doi-asserted-by":"publisher","first-page":"13621","DOI":"10.1074\/jbc.M109.074617","article-title":"Lysosomal degradation of alpha-synuclein in vivo.","volume":"285","author":"Mak","year":"2010","journal-title":"J. Biol. Chem."},{"key":"B169","doi-asserted-by":"publisher","first-page":"1610","DOI":"10.1016\/j.bpj.2024.05.002","article-title":"Parkinson\u2019s disease-associated mutations in \u03b1-synuclein alters its lipid-bound state.","volume":"123","author":"Maltseva","year":"2024","journal-title":"Biophys. J."},{"key":"B170","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.brainres.2018.07.023","article-title":"Analysis of macroautophagy related proteins in G2019S LRRK2 Parkinson\u2019s disease brains with Lewy body pathology.","volume":"1701","author":"Mamais","year":"2018","journal-title":"Brain Res"},{"key":"B171","doi-asserted-by":"publisher","first-page":"4663","DOI":"10.1038\/s41467-024-49016-3","article-title":"Aplp1 interacts with Lag3 to facilitate transmission of pathologic \u03b1-synuclein.","volume":"15","author":"Mao","year":"2024","journal-title":"Nat. Commun."},{"key":"B172","doi-asserted-by":"publisher","first-page":"777","DOI":"10.1172\/JCI32806","article-title":"Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy.","volume":"118","author":"Martinez-Vicente","year":"2008","journal-title":"J. Clin. Invest."},{"key":"B173","doi-asserted-by":"publisher","first-page":"5805","DOI":"10.1073\/pnas.0507436103","article-title":"Consequences of the selective blockage of chaperone-mediated autophagy.","volume":"103","author":"Massey","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B174","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1083\/jcb.200910140","article-title":"PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy.","volume":"189","author":"Matsuda","year":"2010","journal-title":"J. Cell. Biol."},{"key":"B175","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1111\/gtc.13099","article-title":"Cathepsin L prevents the accumulation of alpha-synuclein fibrils in the cell.","volume":"29","author":"Matsuki","year":"2024","journal-title":"Genes Cells"},{"key":"B176","doi-asserted-by":"publisher","first-page":"2104","DOI":"10.1080\/15548627.2021.2016256","article-title":"Autophagy mediates the clearance of oligodendroglial SNCA\/alpha-synuclein and TPPP\/p25A in multiple system atrophy models.","volume":"18","author":"Mavroeidi","year":"2022","journal-title":"Autophagy"},{"key":"B177","doi-asserted-by":"publisher","first-page":"920","DOI":"10.1093\/brain\/awaa008","article-title":"\u03b1-Synuclein oligomers in skin biopsy of idiopathic and monozygotic twin patients with Parkinson\u2019s disease.","volume":"143","author":"Mazzetti","year":"2020","journal-title":"Brain"},{"key":"B178","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.cell.2011.06.001","article-title":"Gaucher disease glucocerebrosidase and \u03b1-synuclein form a bidirectional pathogenic loop in synucleinopathies.","volume":"146","author":"Mazzulli","year":"2011","journal-title":"Cell"},{"key":"B179","doi-asserted-by":"publisher","first-page":"1931","DOI":"10.1073\/pnas.1520335113","article-title":"\u03b1-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models.","volume":"113","author":"Mazzulli","year":"","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B180","doi-asserted-by":"publisher","first-page":"7693","DOI":"10.1523\/JNEUROSCI.0628-16.2016","article-title":"Activation of \u03b2-glucocerebrosidase reduces pathological \u03b1-synuclein and restores lysosomal function in Parkinson\u2019s patient midbrain neurons.","volume":"36","author":"Mazzulli","year":"","journal-title":"J. Neurosci."},{"key":"B181","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1002\/mds.26421","article-title":"Neuropathology of \u03b1-synuclein propagation and braak hypothesis.","volume":"31","author":"McCann","year":"2016","journal-title":"Mov. Disord."},{"key":"B182","doi-asserted-by":"publisher","first-page":"9322","DOI":"10.1073\/pnas.1500937112","article-title":"Cysteine cathepsins are essential in lysosomal degradation of \u03b1-synuclein.","volume":"112","author":"McGlinchey","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B183","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1186\/s13024-019-0329-1","article-title":"Alpha-synuclein structure and Parkinson\u2019s disease - lessons and emerging principles.","volume":"14","author":"Meade","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"B184","doi-asserted-by":"publisher","first-page":"1419","DOI":"10.3390\/biom11101419","article-title":"Structural and functional insights into \u03b1-Synuclein fibril polymorphism.","volume":"11","author":"Mehra","year":"2021","journal-title":"Biomolecules"},{"key":"B185","doi-asserted-by":"publisher","first-page":"852003","DOI":"10.3389\/fneur.2022.852003","article-title":"Alpha-synuclein targeting therapeutics for Parkinson\u2019s disease and related synucleinopathies.","volume":"13","author":"Menon","year":"2022","journal-title":"Front. Neurol."},{"key":"B186","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1007\/s40263-020-00746-0","article-title":"Enhancing the activity of glucocerebrosidase as a treatment for Parkinson disease.","volume":"34","author":"Menozzi","year":"2020","journal-title":"CNS Drugs"},{"key":"B187","doi-asserted-by":"publisher","first-page":"766","DOI":"10.1002\/ana.24790","article-title":"Ambroxol effects in glucocerebrosidase and \u03b1-synuclein transgenic mice.","volume":"80","author":"Migdalska-Richards","year":"2016","journal-title":"Ann. Neurol."},{"key":"B188","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1111\/bpa.12297","article-title":"Alteration of upstream autophagy-related proteins (ULK1, ULK2, Beclin1, VPS34 and AMBRA1) in lewy body disease.","volume":"26","author":"Miki","year":"2016","journal-title":"Brain Pathol"},{"key":"B189","doi-asserted-by":"publisher","first-page":"580634","DOI":"10.3389\/fcell.2020.580634","article-title":"The convergence of alpha-synuclein, mitochondrial, and lysosomal pathways in vulnerability of midbrain dopaminergic neurons in Parkinson\u2019s disease.","volume":"8","author":"Minakaki","year":"2020","journal-title":"Front. Cell. Dev. Biol."},{"key":"B190","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1080\/15548627.2017.1395992","article-title":"Autophagy inhibition promotes SNCA\/alpha-synuclein release and transfer via extracellular vesicles with a hybrid autophagosome-exosome-like phenotype.","volume":"14","author":"Minakaki","year":"2018","journal-title":"Autophagy"},{"key":"B191","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1126\/science.adq6650","article-title":"Commander complex regulates lysosomal function and is implicated in Parkinson\u2019s disease risk.","volume":"388","author":"Minakaki","year":"2025","journal-title":"Science"},{"key":"B192","doi-asserted-by":"publisher","first-page":"1117","DOI":"10.1002\/mds.27090","article-title":"A user\u2019s guide for \u03b1-synuclein biomarker studies in biological fluids: Perianalytical considerations.","volume":"32","author":"Mollenhauer","year":"2017","journal-title":"Mov. Disord."},{"key":"B193","doi-asserted-by":"publisher","first-page":"17","DOI":"10.3233\/JPD-230183","article-title":"Defining a lewy body: Running up the hill of shifting definitions and evolving concepts.","volume":"14","author":"Moors","year":"2024","journal-title":"J. Parkinsons Dis."},{"key":"B194","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1186\/s13024-017-0154-3","article-title":"Therapeutic potential of autophagy-enhancing agents in Parkinson\u2019s disease.","volume":"12","author":"Moors","year":"2017","journal-title":"Mol. Neurodegener."},{"key":"B195","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1038\/s41531-025-00902-7","article-title":"Lysophosphatidylcholine promoting \u03b1-Synuclein aggregation in Parkinson\u2019s disease: disrupting GCase glycosylation and lysosomal \u03b1-Synuclein degradation.","volume":"11","author":"Mu","year":"2025","journal-title":"NPJ Parkinsons Dis."},{"key":"B196","doi-asserted-by":"publisher","first-page":"1152503","DOI":"10.3389\/fnins.2023.1152503","article-title":"Deregulation of mTORC1-TFEB axis in human iPSC model of GBA1-associated Parkinson\u2019s disease.","volume":"17","author":"Mubariz","year":"2023","journal-title":"Front. Neurosci."},{"key":"B197","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1001\/jamaneurol.2019.4611","article-title":"Ambroxol for the treatment of patients with Parkinson disease with and without glucocerebrosidase gene mutations: A nonrandomized.","volume":"77","author":"Mullin","year":"2020","journal-title":"Noncontrolled Trial. JAMA Neurol."},{"key":"B198","doi-asserted-by":"publisher","first-page":"33","DOI":"10.2169\/internalmedicine.8940-21","article-title":"Recent advances in drug therapy for Parkinson\u2019s disease.","volume":"62","author":"Murakami","year":"2023","journal-title":"Intern. Med."},{"key":"B199","doi-asserted-by":"publisher","first-page":"1639","DOI":"10.1002\/mds.26141","article-title":"Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson\u2019s disease.","volume":"30","author":"Murphy","year":"2015","journal-title":"Mov. Disord."},{"key":"B200","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1093\/brain\/awt367","article-title":"Reduced glucocerebrosidase is associated with increased \u03b1-synuclein in sporadic Parkinson\u2019s disease.","volume":"137","author":"Murphy","year":"2014","journal-title":"Brain"},{"key":"B201","doi-asserted-by":"publisher","first-page":"e1000298","DOI":"10.1371\/journal.pbio.1000298","article-title":"PINK1 is selectively stabilized on impaired mitochondria to activate Parkin.","volume":"8","author":"Narendra","year":"2010","journal-title":"PLoS Biol"},{"key":"B202","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1083\/jcb.200809125","article-title":"Parkin is recruited selectively to impaired mitochondria and promotes their autophagy.","volume":"183","author":"Narendra","year":"2008","journal-title":"J. Cell. Biol."},{"key":"B203","doi-asserted-by":"publisher","first-page":"2399","DOI":"10.3390\/cells9112399","article-title":"The emerging role of the lysosome in Parkinson\u2019s disease.","volume":"9","author":"Navarro-Romero","year":"2020","journal-title":"Cells"},{"key":"B204","doi-asserted-by":"publisher","first-page":"1435","DOI":"10.3390\/biom13101435","article-title":"Autophagy in Parkinson\u2019s disease.","volume":"13","author":"Nechushtai","year":"2023","journal-title":"Biomolecules"},{"key":"B205","doi-asserted-by":"publisher","first-page":"136491","DOI":"10.1016\/j.neulet.2022.136491","article-title":"Lysophosphatidylcholine acyltransferase 1 promotes pathology and toxicity in two distinct cell-based alpha-synuclein models.","volume":"772","author":"Nicholatos","year":"2022","journal-title":"Neurosci. Lett."},{"key":"B206","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1021\/bi0485528","article-title":"Ubiquitination of alpha-synuclein.","volume":"44","author":"Nonaka","year":"2005","journal-title":"Biochemistry"},{"key":"B207","doi-asserted-by":"publisher","first-page":"986","DOI":"10.3390\/ijms25020986","article-title":"From synaptic physiology to synaptic pathology: the enigma of \u03b1-Synuclein.","volume":"25","author":"Nordengen","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"B208","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1084\/jem.20040531","article-title":"Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization.","volume":"200","author":"Nylandsted","year":"2004","journal-title":"J. Exp. Med."},{"key":"B209","doi-asserted-by":"publisher","first-page":"3011","DOI":"10.1523\/JNEUROSCI.1508-21.2022","article-title":"S-Nitrosylation of p62 inhibits autophagic flux to promote \u03b1-synuclein secretion and spread in Parkinson\u2019s disease and lewy body dementia.","volume":"42","author":"Oh","year":"2022","journal-title":"J. Neurosci."},{"key":"B210","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1038\/s41531-025-01080-2","article-title":"Impact of \u03b1-synuclein fibril structure on seeding activity in experimental models of Parkinson\u2019s disease.","volume":"11","author":"Ohira","year":"2025","journal-title":"NPJ Parkinsons Dis."},{"key":"B211","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1002\/mds.28792","article-title":"Glucocerebrosidase activity is not associated with Parkinson\u2019s disease risk or severity.","volume":"37","author":"Omer","year":"2022","journal-title":"Mov. Disord."},{"key":"B212","doi-asserted-by":"publisher","first-page":"2543","DOI":"10.1111\/jnc.16114","article-title":"Variant-specific effects of GBA1 mutations on dopaminergic neuron proteostasis.","volume":"168","author":"Onal","year":"2024","journal-title":"J. Neurochem."},{"key":"B213","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1111\/j.1471-4159.2006.03707.x","article-title":"Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro.","volume":"97","author":"Ono","year":"2006","journal-title":"J. Neurochem"},{"key":"B214","doi-asserted-by":"publisher","first-page":"39","DOI":"10.3233\/JPD-160779","article-title":"Implication of Alpha-Synuclein phosphorylation at S129 in synucleinopathies: what have we learned in the last decade?","volume":"6","author":"Oueslati","year":"2016","journal-title":"J. Parkinsons Dis."},{"key":"B215","doi-asserted-by":"publisher","first-page":"E3945","DOI":"10.1073\/pnas.1309991110","article-title":"Polo-like kinase 2 regulates selective autophagic \u03b1-synuclein clearance and suppresses its toxicity in vivo.","volume":"110","author":"Oueslati","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B216","doi-asserted-by":"publisher","first-page":"2349","DOI":"10.1016\/j.cub.2015.07.050","article-title":"Elevated mitochondrial bioenergetics and axonal arborization size are key contributors to the vulnerability of dopamine neurons.","volume":"25","author":"Pacelli","year":"2015","journal-title":"Curr. Biol."},{"key":"B217","doi-asserted-by":"publisher","first-page":"705407","DOI":"10.3389\/fneur.2021.705407","article-title":"A phase II study to evaluate the safety and efficacy of prasinezumab in early Parkinson\u2019s disease (PASADENA): rationale, design, and baseline data.","volume":"12","author":"Pagano","year":"2021","journal-title":"Front. Neurol."},{"key":"B218","doi-asserted-by":"publisher","first-page":"1096","DOI":"10.1038\/s41591-024-02886-y","article-title":"Prasinezumab slows motor progression in rapidly progressing early-stage Parkinson\u2019s disease.","volume":"30","author":"Pagano","year":"2024","journal-title":"Nat. Med."},{"key":"B219","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1056\/NEJMoa2202867","article-title":"Trial of prasinezumab in early-stage Parkinson\u2019s disease.","volume":"387","author":"Pagano","year":"2022","journal-title":"N. Engl. J. Med."},{"key":"B220","doi-asserted-by":"publisher","first-page":"1310","DOI":"10.1080\/15548627.2018.1474992","article-title":"Transcription factor NFE2L2\/NRF2 modulates chaperone-mediated autophagy through the regulation of LAMP2A.","volume":"14","author":"Pajares","year":"2018","journal-title":"Autophagy"},{"key":"B221","doi-asserted-by":"publisher","first-page":"1992","DOI":"10.1016\/j.bbadis.2018.11.017","article-title":"The role of posttranslational modifications of \u03b1-Synuclein and LRRK2 in Parkinson\u2019s disease: Potential contributions of environmental factors.","volume":"1865","author":"Pajarillo","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"B222","doi-asserted-by":"publisher","first-page":"1969","DOI":"10.1093\/brain\/awm318","article-title":"The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson\u2019s disease.","volume":"131","author":"Pan","year":"2008","journal-title":"Brain"},{"key":"B223","doi-asserted-by":"publisher","first-page":"2015","DOI":"10.1016\/j.biocel.2009.05.008","article-title":"Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells.","volume":"41","author":"Parihar","year":"2009","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"B224","doi-asserted-by":"publisher","first-page":"1423","DOI":"10.1002\/mds.27136","article-title":"Cerebrospinal fluid \u03b2-glucocerebrosidase activity is reduced in parkinson\u2019s disease patients.","volume":"32","author":"Parnetti","year":"2017","journal-title":"Mov. Disord."},{"key":"B225","doi-asserted-by":"publisher","first-page":"8053","DOI":"10.1523\/JNEUROSCI.21-20-08053.2001","article-title":"Induction of alpha-synuclein aggregation by intracellular nitrative insult.","volume":"21","author":"Paxinou","year":"2001","journal-title":"J. Neurosci."},{"key":"B226","doi-asserted-by":"publisher","first-page":"839","DOI":"10.3390\/pharmaceutics15030839","article-title":"Development of small molecules targeting \u03b1-synuclein aggregation: a promising strategy to treat parkinson\u2019s disease.","volume":"15","author":"Pe\u00f1a-D\u00edaz","year":"2023","journal-title":"Pharmaceutics"},{"key":"B227","doi-asserted-by":"publisher","first-page":"1508","DOI":"10.3390\/biom11101508","article-title":"Mitochondrial dysfunction, protein misfolding and neuroinflammation in Parkinson\u2019s disease: roads to biomarker discovery.","volume":"11","author":"Picca","year":"2021","journal-title":"Biomolecules"},{"key":"B228","doi-asserted-by":"publisher","first-page":"13","DOI":"10.3389\/fncom.2013.00013","article-title":"The energy cost of action potential propagation in dopamine neurons: Clues to susceptibility in Parkinson\u2019s disease.","volume":"7","author":"Pissadaki","year":"2013","journal-title":"Front. Comput. Neurosci."},{"key":"B229","doi-asserted-by":"publisher","first-page":"2615","DOI":"10.1523\/JNEUROSCI.0610-22.2023","article-title":"Impaired autophagic-lysosomal fusion in Parkinson\u2019s patient midbrain neurons occurs through loss of ykt6 and is rescued by farnesyltransferase inhibition.","volume":"43","author":"Pitcairn","year":"2023","journal-title":"J. Neurosci"},{"key":"B230","doi-asserted-by":"publisher","first-page":"1260","DOI":"10.3390\/brainsci15121260","article-title":"Alpha-synuclein neurobiology in Parkinson\u2019s disease: a comprehensive review of its role, mechanisms, and therapeutic perspectives.","volume":"15","author":"Pitton Rissardo","year":"2025","journal-title":"Brain Sci."},{"key":"B231","doi-asserted-by":"publisher","first-page":"303","DOI":"10.3233\/JPD-171248","article-title":"Best practices for generating and using alpha-Synuclein pre-formed fibrils to model parkinson\u2019s disease in rodents.","volume":"8","author":"Polinski","year":"2018","journal-title":"J. Parkinsons Dis."},{"key":"B232","doi-asserted-by":"publisher","first-page":"912","DOI":"10.3390\/biom10060912","article-title":"The future of targeted gene-based treatment strategies and biomarkers in Parkinson\u2019s disease.","volume":"10","author":"Polissidis","year":"2020","journal-title":"Biomolecules"},{"key":"B233","doi-asserted-by":"publisher","first-page":"861202","DOI":"10.3389\/fncel.2022.861202","article-title":"Activated endolysosomal cation channel TRPML1 facilitates maturation of \u03b1-synuclein-containing autophagosomes.","volume":"16","author":"Pollmanns","year":"2022","journal-title":"Front. Cell. Neurosci."},{"key":"B234","doi-asserted-by":"publisher","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":"B235","doi-asserted-by":"publisher","first-page":"16165","DOI":"10.1038\/s41598-018-34490-9","article-title":"The small molecule alpha-synuclein misfolding inhibitor, NPT200-11, produces multiple benefits in an animal model of Parkinson\u2019s disease.","volume":"8","author":"Price","year":"2018","journal-title":"Sci. Rep."},{"key":"B236","doi-asserted-by":"publisher","first-page":"1127","DOI":"10.1080\/15548627.2022.2045534","article-title":"Recombinant pro-CTSD (cathepsin D) enhances SNCA\/\u03b1-Synuclein degradation in \u03b1-Synucleinopathy models.","volume":"18","author":"Prieto Huarcaya","year":"2022","journal-title":"Autophagy"},{"key":"B237","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1111\/cns.12514","article-title":"Atp13a2 deficiency aggravates astrocyte-mediated neuroinflammation via nlrp3 inflammasome activation.","volume":"22","author":"Qiao","year":"2016","journal-title":"CNS Neurosci. Ther."},{"key":"B238","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1186\/1756-6606-1-17","article-title":"Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity.","volume":"1","author":"Qiao","year":"2008","journal-title":"Mol. Brain"},{"key":"B239","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1186\/s12974-023-02866-y","article-title":"Lysosomal acidification dysfunction in microglia: an emerging pathogenic mechanism of neuroinflammation and neurodegeneration.","volume":"20","author":"Quick","year":"2023","journal-title":"J. Neuroinflammation"},{"key":"B240","doi-asserted-by":"publisher","first-page":"85","DOI":"10.3390\/nu16010085","article-title":"Ellagic acid prevents \u03b1-synuclein spread and mitigates toxicity by enhancing autophagic flux in an animal model of Parkinson\u2019s disease.","volume":"16","author":"Radwan","year":"2023","journal-title":"Nutrients"},{"key":"B241","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1038\/s41531-023-00578-x","article-title":"Alpha synuclein modulates mitochondrial Ca2+ uptake from ER during cell stimulation and under stress conditions.","volume":"9","author":"Ramezani","year":"2023","journal-title":"NPJ Parkinsons Dis."},{"key":"B242","doi-asserted-by":"publisher","first-page":"212.e5","DOI":"10.1016\/j.neurobiolaging.2016.04.022","article-title":"Strong association between glucocerebrosidase mutations and Parkinson\u2019s disease in Sweden.","volume":"45","author":"Ran","year":"2016","journal-title":"Neurobiol. Aging"},{"key":"B243","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1016\/S0002-9440(10)64160-0","article-title":"Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts.","volume":"161","author":"Roberg","year":"2002","journal-title":"Am. J. Pathol."},{"key":"B244","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1016\/j.nbd.2015.09.009","article-title":"Glucocerebrosidase gene therapy prevents \u03b1-synucleinopathy of midbrain dopamine neurons.","volume":"82","author":"Rocha","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"B245","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1097\/WCO.0000000000000715","article-title":"GBA1-associated parkinsonism: New insights and therapeutic opportunities.","volume":"32","author":"Ryan","year":"2019","journal-title":"Curr. Opin. Neurol."},{"key":"B246","doi-asserted-by":"publisher","first-page":"157","DOI":"10.3389\/fnmol.2016.00157","article-title":"Role of chaperone-mediated autophagy dysfunctions in the pathogenesis of Parkinson\u2019s disease.","volume":"9","author":"Sala","year":"2016","journal-title":"Front. Mol. Neurosci."},{"key":"B247","doi-asserted-by":"publisher","first-page":"921314","DOI":"10.3389\/fcell.2022.921314","article-title":"Targeting macroautophagy as a therapeutic opportunity to treat Parkinson\u2019s disease.","volume":"10","author":"Sanchez-Mirasierra","year":"2022","journal-title":"Front. Cell. Dev. Biol."},{"key":"B248","doi-asserted-by":"publisher","first-page":"5641","DOI":"10.1074\/jbc.M609532200","article-title":"Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein.","volume":"282","author":"Sarkar","year":"2007","journal-title":"J. Biol. Chem."},{"key":"B249","doi-asserted-by":"publisher","first-page":"1101","DOI":"10.1083\/jcb.200504035","article-title":"Lithium induces autophagy by inhibiting inositol monophosphatase.","volume":"170","author":"Sarkar","year":"2005","journal-title":"J. Cell. Biol."},{"key":"B250","doi-asserted-by":"publisher","first-page":"e1009359","DOI":"10.1371\/journal.pgen.1009359","article-title":"\u03b1-synuclein impairs autophagosome maturation through abnormal actin stabilization.","volume":"17","author":"Sarkar","year":"2021","journal-title":"PLoS Genet"},{"key":"B251","doi-asserted-by":"publisher","first-page":"2839","DOI":"10.1080\/15548627.2024.2413295","article-title":"Clustering lysosomes around the MTOC: A promising strategy for SNCA\/alpha-synuclein breakdown leading to parkinson disease treatment.","volume":"20","author":"Sasazawa","year":"2024","journal-title":"Autophagy"},{"key":"B252","doi-asserted-by":"publisher","first-page":"e42545","DOI":"10.1371\/journal.pone.0042545","article-title":"Single-channel electrophysiology reveals a distinct and uniform pore complex formed by \u03b1-synuclein oligomers in lipid membranes.","volume":"7","author":"Schmidt","year":"2012","journal-title":"PLoS One"},{"key":"B253","doi-asserted-by":"publisher","first-page":"2976","DOI":"10.1016\/j.celrep.2018.05.009","article-title":"The NAD+ precursor nicotinamide riboside rescues mitochondrial defects and neuronal loss in iPSC and fly models of parkinson\u2019s disease.","volume":"23","author":"Sch\u00f6ndorf","year":"2018","journal-title":"Cell Rep."},{"key":"B254","doi-asserted-by":"publisher","first-page":"9678","DOI":"10.1021\/bi800699v","article-title":"Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species.","volume":"47","author":"Sevlever","year":"2008","journal-title":"Biochemistry"},{"key":"B255","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1038\/s41593-019-0423-2","article-title":"Lewy pathology in Parkinson\u2019s disease consists of crowded organelles and lipid membranes.","volume":"22","author":"Shahmoradian","year":"2019","journal-title":"Nat. Neurosci."},{"key":"B256","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1007\/s00401-018-1873-4","article-title":"Alpha-synuclein delays mitophagy and targeting Miro rescues neuron loss in Parkinson\u2019s models.","volume":"136","author":"Shaltouki","year":"2018","journal-title":"Acta Neuropathol"},{"key":"B257","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.tins.2022.11.007","article-title":"\u03b1-Synuclein in synaptic function and dysfunction.","volume":"46","author":"Sharma","year":"2023","journal-title":"Trends Neurosci."},{"key":"B258","doi-asserted-by":"publisher","first-page":"1649","DOI":"10.3390\/biom14121649","article-title":"Alpha-synuclein effects on mitochondrial quality control in Parkinson\u2019s disease.","volume":"14","author":"Shen","year":"2024","journal-title":"Biomolecules"},{"key":"B259","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1056\/NEJMoa0901281","article-title":"Multicenter analysis of glucocerebrosidase mutations in Parkinson\u2019s disease.","volume":"361","author":"Sidransky","year":"2009","journal-title":"N. Engl. J. Med."},{"key":"B260","doi-asserted-by":"publisher","first-page":"797","DOI":"10.1001\/jamaneurol.2025.1687","article-title":"Ambroxol as a treatment for parkinson disease dementia: A randomized clinical trial.","volume":"82","author":"Silveira","year":"2025","journal-title":"JAMA Neurol."},{"key":"B261","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1042\/BST20190236","article-title":"Parkinson\u2019s disease and mitophagy: An emerging role for LRRK2.","volume":"49","author":"Singh","year":"2021","journal-title":"Biochem. Soc. Trans."},{"key":"B262","doi-asserted-by":"publisher","first-page":"7102","DOI":"10.3390\/ijms25137102","article-title":"GBA1-associated Parkinson\u2019s disease is a distinct entity.","volume":"25","author":"Skrahin","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"B263","doi-asserted-by":"publisher","first-page":"1261","DOI":"10.3390\/cells11081261","article-title":"GBA variants and Parkinson disease: Mechanisms and treatments.","volume":"11","author":"Smith","year":"2022","journal-title":"Cells"},{"key":"B264","doi-asserted-by":"publisher","first-page":"971252","DOI":"10.3389\/fneur.2022.971252","article-title":"Genetic variations in GBA1 and LRRK2 genes: Biochemical and clinical consequences in Parkinson disease.","volume":"13","author":"Smith","year":"2022","journal-title":"Front. Neurol."},{"key":"B265","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1186\/s40478-020-00935-4","article-title":"Genetic perspective on the synergistic connection between vesicular transport, lysosomal and mitochondrial pathways associated with Parkinson\u2019s disease pathogenesis.","volume":"8","author":"Smolders","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"B266","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1186\/s40035-020-00196-0","article-title":"The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases.","volume":"9","author":"Song","year":"2020","journal-title":"Transl. Neurodegener."},{"key":"B267","doi-asserted-by":"publisher","first-page":"13578","DOI":"10.1523\/JNEUROSCI.4390-09.2009","article-title":"Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson\u2019s and Lewy body diseases.","volume":"29","author":"Spencer","year":"2009","journal-title":"J. Neurosci."},{"key":"B268","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1007\/s00441-017-2704-y","article-title":"Molecular mechanisms of \u03b1-synuclein and GBA1 in Parkinson\u2019s disease.","volume":"373","author":"Stojkovska","year":"2018","journal-title":"Cell. Tissue Res."},{"key":"B269","doi-asserted-by":"publisher","first-page":"109099","DOI":"10.1016\/j.celrep.2021.109099","article-title":"\u03b1-Synuclein mutation impairs processing of endomembrane compartments and promotes exocytosis and seeding of \u03b1-synuclein pathology.","volume":"35","author":"Stykel","year":"2021","journal-title":"Cell. Rep."},{"key":"B270","doi-asserted-by":"publisher","first-page":"4275","DOI":"10.1074\/jbc.M111.280016","article-title":"Ex vivo and in vivo effects of isofagomine on acid \u03b2-glucosidase variants and substrate levels in Gaucher disease.","volume":"287","author":"Sun","year":"2012","journal-title":"J. Biol. Chem."},{"key":"B271","doi-asserted-by":"publisher","first-page":"3657","DOI":"10.1111\/febs.14607","article-title":"Determinants of dopaminergic neuron loss in Parkinson\u2019s disease.","volume":"285","author":"Surmeier","year":"2018","journal-title":"FEBS J."},{"key":"B272","doi-asserted-by":"publisher","first-page":"9617","DOI":"10.1523\/JNEUROSCI.1525-17.2017","article-title":"Glucosylsphingosine promotes \u03b1-synuclein pathology in mutant GBA-associated Parkinson\u2019s disease.","volume":"37","author":"Taguchi","year":"2017","journal-title":"J. Neurosci."},{"key":"B273","doi-asserted-by":"publisher","DOI":"10.1101\/2025.01.09.632210","article-title":"Glucocerebrosidase deficiency dysregulates human astrocyte lipid metabolism.","author":"Tahanis","year":"2025","journal-title":"bioRxiv [Preprint]"},{"key":"B274","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/s0006-8993(02)02498-8","article-title":"Tyrosine 125 of alpha-Synuclein plays a critical role for dimerization following nitrative stress.","volume":"938","author":"Takahashi","year":"2002","journal-title":"Brain Res."},{"key":"B275","doi-asserted-by":"publisher","first-page":"854","DOI":"10.1038\/s41419-021-04138-0","article-title":"Alpha-Synuclein defects autophagy by impairing SNAP29-mediated autophagosome-lysosome fusion.","volume":"12","author":"Tang","year":"2021","journal-title":"Cell. Death Dis."},{"key":"B276","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1016\/bs.pmbts.2019.07.005","article-title":"Prion-like propagation of \u03b1-synuclein in neurodegenerative diseases.","volume":"168","author":"Tarutani","year":"2019","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"B277","doi-asserted-by":"publisher","first-page":"1333","DOI":"10.3390\/biom11091333","article-title":"Alpha-Synuclein and the endolysosomal system in Parkinson\u2019s disease: Guilty by association.","volume":"11","author":"Teixeira","year":"2021","journal-title":"Biomolecules"},{"key":"B278","doi-asserted-by":"publisher","first-page":"947191","DOI":"10.3389\/fnmol.2022.947191","article-title":"The relationship of alpha-synuclein to mitochondrial dynamics and quality control.","volume":"15","author":"Thorne","year":"2022","journal-title":"Front. Mol. Neurosci."},{"key":"B279","doi-asserted-by":"publisher","first-page":"110470","DOI":"10.1016\/j.abb.2025.110470","article-title":"Mechanism of flavonoid myricetin modulated aggregation in \u03b1-Synuclein and its familial mutants E46K and A30P.","volume":"770","author":"Tinku","year":"2025","journal-title":"Arch. Biochem. Biophys."},{"key":"B280","doi-asserted-by":"publisher","first-page":"44405","DOI":"10.1074\/jbc.M308041200","article-title":"Ubiquitination of alpha-Synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function.","volume":"278","author":"Tofaris","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B281","doi-asserted-by":"publisher","first-page":"2876","DOI":"10.1016\/j.bbamem.2012.07.007","article-title":"Alpha-synuclein pore forming activity upon membrane association.","volume":"1818","author":"Tosatto","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"B282","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1093\/brain\/awaf326","article-title":"A human striatal-midbrain assembloid model of alpha-synuclein propagation.","volume":"149","author":"Tran","year":"2026","journal-title":"Brain"},{"key":"B283","doi-asserted-by":"publisher","first-page":"7567","DOI":"10.1038\/s41598-019-43772-9","article-title":"Amido-bridged nucleic acid (AmNA)-modified antisense oligonucleotides targeting \u03b1-synuclein as a novel therapy for Parkinson\u2019s disease.","volume":"9","author":"Uehara","year":"2019","journal-title":"Sci. Rep."},{"key":"B284","doi-asserted-by":"publisher","first-page":"9152","DOI":"10.3390\/ijms26189152","article-title":"p.N370S GBA1 mutation influences the morphology and lipid composition of extracellular vesicles in blood plasma from patients with Parkinson\u2019s disease.","volume":"26","author":"Usenko","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"B285","doi-asserted-by":"publisher","first-page":"292","DOI":"10.1016\/j.jinorgbio.2016.04.012","article-title":"Coordination and redox properties of copper interaction with \u03b1-synuclein.","volume":"163","author":"Valensin","year":"2016","journal-title":"J. Inorg. Biochem."},{"key":"B286","doi-asserted-by":"publisher","first-page":"1732","DOI":"10.3390\/cells11111732","article-title":"Alpha-Synuclein aggregation pathway in Parkinson\u2019s disease: Current status and novel therapeutic approaches.","volume":"11","author":"Vidovi\u0107","year":"2022","journal-title":"Cells"},{"key":"B287","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1007\/s00702-022-02531-3","article-title":"Glucocerebrosidase mutations and Parkinson disease.","volume":"129","author":"Vieira","year":"2022","journal-title":"J. Neural Transm."},{"key":"B288","doi-asserted-by":"publisher","first-page":"23542","DOI":"10.1074\/jbc.M801992200","article-title":"Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells.","volume":"283","author":"Vogiatzi","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B289","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1016\/S1474-4422(20)30136-8","article-title":"Safety and immunogenicity of the \u03b1-synuclein active immunotherapeutic PD01A in patients with Parkinson\u2019s disease: A randomised, single-blinded, phase 1 trial.","volume":"19","author":"Volc","year":"2020","journal-title":"Lancet Neurol"},{"key":"B290","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/B978-0-444-63945-5.00017-9","article-title":"Prion-like propagation of pathology in Parkinson disease.","volume":"153","author":"Volpicelli-Daley","year":"2018","journal-title":"Handb. Clin. Neurol."},{"key":"B291","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1007\/s00401-013-1114-9","article-title":"Anle138b: A novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson\u2019s disease.","volume":"125","author":"Wagner","year":"2013","journal-title":"Acta Neuropathol"},{"key":"B292","doi-asserted-by":"publisher","first-page":"35","DOI":"10.3233\/JPD-230154","article-title":"Prevalence of concomitant pathologies in parkinson\u2019s Disease: Implications for prognosis, diagnosis, and insights into common pathogenic mechanisms.","volume":"14","author":"Walker","year":"2024","journal-title":"J. Parkinsons Dis."},{"key":"B293","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1186\/s40035-016-0065-1","article-title":"Dysregulation of autophagy and mitochondrial function in Parkinson\u2019s disease.","volume":"5","author":"Wang","year":"2016","journal-title":"Transl. Neurodegener."},{"key":"B294","doi-asserted-by":"publisher","first-page":"918","DOI":"10.1111\/tra.12613","article-title":"Lysosomal membrane permeabilization and cell death.","volume":"19","author":"Wang","year":"2018","journal-title":"Traffic"},{"key":"B295","doi-asserted-by":"publisher","first-page":"eabq1141","DOI":"10.1126\/sciadv.abq1141","article-title":"The link between neuroinflammation and the neurovascular unit in synucleinopathies.","volume":"9","author":"Wang","year":"2023","journal-title":"Sci. Adv."},{"key":"B296","doi-asserted-by":"publisher","first-page":"1931","DOI":"10.1093\/hmg\/dds003","article-title":"LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1.","volume":"21","author":"Wang","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"B297","doi-asserted-by":"publisher","first-page":"1723","DOI":"10.4103\/1673-5374.363831","article-title":"Targeting chaperone-mediated autophagy for Parkinson\u2019s disease therapy.","volume":"18","author":"Wang","year":"2023","journal-title":"Neural. Regen. Res."},{"key":"B298","doi-asserted-by":"publisher","first-page":"e52868","DOI":"10.1371\/journal.pone.0052868","article-title":"p62\/SQSTM1-dependent autophagy of Lewy body-like \u03b1-synuclein inclusions.","volume":"7","author":"Watanabe","year":"2012","journal-title":"PLoS One"},{"key":"B299","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1080\/15548627.2019.1603548","article-title":"LRRK2 mutations impair depolarization-induced mitophagy through inhibition of mitochondrial accumulation of RAB10.","volume":"16","author":"Wauters","year":"2020","journal-title":"Autophagy"},{"key":"B300","doi-asserted-by":"publisher","first-page":"25009","DOI":"10.1074\/jbc.M300227200","article-title":"Alpha-Synuclein is degraded by both autophagy and the proteasome.","volume":"278","author":"Webb","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B301","doi-asserted-by":"publisher","first-page":"598446","DOI":"10.3389\/fcell.2020.598446","article-title":"Current evidence for a bidirectional loop between the lysosome and alpha-synuclein proteoforms.","volume":"8","author":"Wildburger","year":"2020","journal-title":"Front. Cell. Dev. Biol."},{"key":"B302","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1038\/nchembio.79","article-title":"Novel targets for Huntington\u2019s disease in an mTOR-independent autophagy pathway.","volume":"4","author":"Williams","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"B303","doi-asserted-by":"publisher","first-page":"2808","DOI":"10.1093\/hmg\/ddad102","article-title":"Mitochondrial dysfunction and mitophagy defects in LRRK2-R1441C Parkinson\u2019s disease models.","volume":"32","author":"Williamson","year":"2023","journal-title":"Hum. Mol. Genet."},{"key":"B304","doi-asserted-by":"publisher","first-page":"4194","DOI":"10.1073\/pnas.1100976108","article-title":"In vivo demonstration that alpha-synuclein oligomers are toxic.","volume":"108","author":"Winner","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B305","doi-asserted-by":"publisher","first-page":"429","DOI":"10.4161\/auto.7.4.14393","article-title":"The Parkinson disease protein \u03b1-synuclein inhibits autophagy.","volume":"7","author":"Winslow","year":"2011","journal-title":"Autophagy"},{"key":"B306","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1083\/jcb.201003122","article-title":"\u03b1-Synuclein impairs macroautophagy: Implications for Parkinson\u2019s disease.","volume":"190","author":"Winslow","year":"2010","journal-title":"J. Cell. Biol."},{"key":"B307","doi-asserted-by":"publisher","first-page":"2466","DOI":"10.3390\/antiox11122466","article-title":"Neuronal oxidative stress promotes \u03b1-synuclein aggregation in vivo.","volume":"11","author":"Won","year":"2022","journal-title":"Antioxidants"},{"key":"B308","doi-asserted-by":"publisher","first-page":"1284","DOI":"10.1007\/s12035-014-8933-0","article-title":"Crosstalk between macroautophagy and chaperone-mediated autophagy: implications for the treatment of neurological diseases.","volume":"52","author":"Wu","year":"2015","journal-title":"Mol. Neurobiol."},{"key":"B309","doi-asserted-by":"publisher","first-page":"892","DOI":"10.1126\/science.adp3645","article-title":"Neuronal FAM171A2 mediates \u03b1-synuclein fibril uptake and drives Parkinson\u2019s disease.","volume":"387","author":"Wu","year":"2025","journal-title":"Science"},{"key":"B310","doi-asserted-by":"publisher","first-page":"1470171","DOI":"10.3389\/fnmol.2024.1470171","article-title":"Intercellular transmission of alpha-synuclein.","volume":"17","author":"Wu","year":"2024","journal-title":"Front. Mol. Neurosci."},{"key":"B311","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1038\/s41419-019-1404-9","article-title":"Microglia as modulators of exosomal alpha-synuclein transmission.","volume":"10","author":"Xia","year":"2019","journal-title":"Cell. Death Dis."},{"key":"B312","doi-asserted-by":"publisher","first-page":"104922","DOI":"10.1016\/j.antiviral.2020.104922","article-title":"ML-SA1, a selective TRPML agonist, inhibits DENV2 and ZIKV by promoting lysosomal acidification and protease activity.","volume":"182","author":"Xia","year":"2020","journal-title":"Antiviral Res."},{"key":"B313","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.ncl.2024.12.003","article-title":"Pathogenesis of Parkinson\u2019s disease.","volume":"43","author":"Xiao","year":"2025","journal-title":"Neurol. Clin."},{"key":"B314","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1002\/mds.26477","article-title":"Autophagy and alpha-synuclein: relevance to Parkinson\u2019s disease and related synucleopathies.","volume":"31","author":"Xilouri","year":"2016","journal-title":"Mov. Disord."},{"key":"B315","doi-asserted-by":"publisher","first-page":"2166","DOI":"10.4161\/auto.26451","article-title":"LAMP2A as a therapeutic target in Parkinson disease.","volume":"9","author":"Xilouri","year":"","journal-title":"Autophagy"},{"key":"B316","doi-asserted-by":"publisher","first-page":"2130","DOI":"10.1093\/brain\/awt131","article-title":"Boosting chaperone-mediated autophagy in vivo mitigates \u03b1-synuclein-induced neurodegeneration.","volume":"136","author":"Xilouri","year":"","journal-title":"Brain"},{"key":"B317","doi-asserted-by":"publisher","first-page":"e5515","DOI":"10.1371\/journal.pone.0005515","article-title":"Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy.","volume":"4","author":"Xilouri","year":"2009","journal-title":"PLoS One"},{"key":"B318","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/s41422-024-01022-2","article-title":"\u03b1-Synuclein amyloid fibril directly binds to LC3B and suppresses SQSTM1\/p62-mediated selective autophagy.","volume":"35","author":"Xu","year":"2025","journal-title":"Cell Res."},{"key":"B319","doi-asserted-by":"publisher","first-page":"2370","DOI":"10.4103\/1673-5374.371346","article-title":"Enhancement of lysosome biogenesis as a potential therapeutic approach for neurodegenerative diseases.","volume":"18","author":"Xue","year":"2023","journal-title":"Neural. Regen. Res."},{"key":"B320","doi-asserted-by":"publisher","first-page":"S369","DOI":"10.3233\/JPD-230393","article-title":"Experimental animal models of prodromal Parkinson\u2019s disease.","volume":"14","author":"Yamakado","year":"2024","journal-title":"J. Parkinsons Dis."},{"key":"B321","doi-asserted-by":"publisher","first-page":"2613401","DOI":"10.1155\/2016\/2613401","article-title":"Chaperone-mediated autophagy and mitochondrial homeostasis in Parkinson\u2019s disease.","volume":"2016","author":"Yang","year":"2016","journal-title":"Parkinsons Dis."},{"key":"B322","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1016\/j.ymgme.2012.11.010","article-title":"Membrane-bound \u03b1-synuclein interacts with glucocerebrosidase and inhibits enzyme activity.","volume":"108","author":"Yap","year":"2013","journal-title":"Mol. Genet. Metab."},{"key":"B323","doi-asserted-by":"publisher","first-page":"744","DOI":"10.3390\/biomedicines12040744","article-title":"Detection of ER stress in iPSC-derived neurons carrying the p.N370S mutation in the GBA1 gene.","volume":"12","author":"Yarkova","year":"2024","journal-title":"Biomedicines"},{"key":"B324","doi-asserted-by":"publisher","first-page":"806","DOI":"10.14348\/molcells.2022.0102","article-title":"\u03b1-synuclein disrupts vesicle fusion by two mutant-specific mechanisms.","volume":"45","author":"Yoo","year":"2022","journal-title":"Mol. Cells"},{"key":"B325","doi-asserted-by":"publisher","first-page":"e3091","DOI":"10.1038\/cddis.2017.501","article-title":"Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation.","volume":"8","author":"Yoon","year":"2017","journal-title":"Cell. Death Dis."},{"key":"B326","doi-asserted-by":"publisher","first-page":"1416","DOI":"10.1002\/mds.29016","article-title":"A randomized first-in-human study with UB-312, a UBITh\u00a7\u03b1-synuclein peptide vaccine.","volume":"37","author":"Yu","year":"2022","journal-title":"Mov. Disord."},{"key":"B327","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia.","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann. Neurol."},{"key":"B328","doi-asserted-by":"publisher","first-page":"1623","DOI":"10.1080\/15548627.2024.2448914","article-title":"PLK2 disrupts autophagic flux to promote SNCA\/\u03b1-synuclein pathology.","volume":"21","author":"Zhang","year":"2025","journal-title":"Autophagy"},{"key":"B329","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1111\/jnc.14308","article-title":"Mitochondrial function and autophagy: Integrating proteotoxic, redox, and metabolic stress in Parkinson\u2019s disease.","volume":"144","author":"Zhang","year":"2018","journal-title":"J. Neurochem."},{"key":"B330","doi-asserted-by":"publisher","first-page":"3015","DOI":"10.1016\/j.apsb.2021.02.016","article-title":"Targeting autophagy using small-molecule compounds to improve potential therapy of Parkinson\u2019s disease.","volume":"11","author":"Zhang","year":"2021","journal-title":"Acta Pharm. Sin. B."},{"key":"B331","doi-asserted-by":"publisher","first-page":"2581","DOI":"10.4103\/NRR.NRR-D-23-01900","article-title":"Strain-dependent alpha-synuclein spreading in Parkinson\u2019s disease and multiple system atrophy.","volume":"19","author":"Zhang","year":"2024","journal-title":"Neural. Regen. Res."},{"key":"B332","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1080\/15548627.2024.2442858","article-title":"Drosophila aux orchestrates the phosphorylation-dependent assembly of the lysosomal V-ATPase in glia and contributes to SNCA\/\u03b1-synuclein degradation.","volume":"21","author":"Zhang","year":"2025","journal-title":"Autophagy"},{"key":"B333","doi-asserted-by":"publisher","first-page":"e2301002120","DOI":"10.1073\/pnas.2301002120","article-title":"Cyclin-G-associated kinase GAK\/dAux regulates autophagy initiation via ULK1\/Atg1 in glia.","volume":"120","author":"Zhang","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B334","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1186\/s40035-024-00437-6","article-title":"Clinical, mechanistic, biomarker, and therapeutic advances in GBA1-associated Parkinson\u2019s disease.","volume":"13","author":"Zhang","year":"","journal-title":"Transl. Neurodegener."},{"key":"B335","doi-asserted-by":"publisher","first-page":"1411104","DOI":"10.3389\/fnagi.2024.1411104","article-title":"Emerging role of microglia in inter-cellular transmission of \u03b1-synuclein in Parkinson\u2019s disease.","volume":"16","author":"Zhang","year":"","journal-title":"Front. Aging Neurosci."},{"key":"B336","doi-asserted-by":"publisher","first-page":"2643","DOI":"10.1038\/s41467-020-16386-3","article-title":"Parkinson\u2019s disease associated mutation E46K of \u03b1-synuclein triggers the formation of a distinct fibril structure.","volume":"11","author":"Zhao","year":"2020","journal-title":"Nat. Commun."},{"key":"B337","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1007\/s12035-021-02599-0","article-title":"SNARE proteins mediate \u03b1-Synuclein secretion via multiple vesicular pathways.","volume":"59","author":"Zhao","year":"2021","journal-title":"Mol. Neurobiol."},{"key":"B338","doi-asserted-by":"publisher","first-page":"851135","DOI":"10.3389\/fnagi.2022.851135","article-title":"Glucocerebrosidase mutations cause mitochondrial and lysosomal dysfunction in Parkinson\u2019s disease: Pathogenesis and therapeutic implications.","volume":"14","author":"Zheng","year":"2022","journal-title":"Front. Aging Neurosci."},{"key":"B339","doi-asserted-by":"publisher","first-page":"26846","DOI":"10.1074\/jbc.M403129200","article-title":"The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils.","volume":"279","author":"Zhu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B340","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/j.abb.2016.09.007","article-title":"RKIP suppresses the proliferation and metastasis of breast cancer cell lines through up-regulation of miR-185 targeting HMGA2.","volume":"610","author":"Zou","year":"2016","journal-title":"Arch. Biochem. Biophys."}],"container-title":["Frontiers in Neuroscience"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fnins.2026.1885103\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T05:39:41Z","timestamp":1785130781000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fnins.2026.1885103\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,27]]},"references-count":340,"alternative-id":["10.3389\/fnins.2026.1885103"],"URL":"https:\/\/doi.org\/10.3389\/fnins.2026.1885103","relation":{},"ISSN":["1662-453X"],"issn-type":[{"value":"1662-453X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,27]]},"article-number":"1885103"}}