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However, the mechanism by which \u03b1Syn aggregates in the brain remains unclear. Biochemical studies have demonstrated that \u03b1Syn interacts with lipids, and these interactions affect the aggregation process of \u03b1Syn. Furthermore, genetic studies have identified mutations in lipid metabolism-associated genes such as glucocerebrosidase 1 (GBA1) and synaptojanin 1 (SYNJ1) in sporadic and familial forms of PD, respectively. In this review, we focus on the role of lipids in triggering \u03b1Syn aggregation in the pathogenesis of PD and propose the possibility of modulating the interaction of lipids with \u03b1Syn as a potential therapy for PD.<\/jats:p>","DOI":"10.3390\/ijms25168935","type":"journal-article","created":{"date-parts":[[2024,8,16]],"date-time":"2024-08-16T09:15:41Z","timestamp":1723799741000},"page":"8935","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Role of Lipids in the Pathogenesis of Parkinson\u2019s Disease"],"prefix":"10.3390","volume":"25","author":[{"given":"Shumpei","family":"Kamano","sequence":"first","affiliation":[{"name":"Department of Neurology, Kindai University Faculty of Medicine, Osaka-Sayama 589-8511, Osaka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daisaku","family":"Ozawa","sequence":"additional","affiliation":[{"name":"Department of Neurology, Kindai University Faculty of Medicine, Osaka-Sayama 589-8511, Osaka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kensuke","family":"Ikenaka","sequence":"additional","affiliation":[{"name":"Department of Neurology, Osaka University Graduate School of Medicine, Suita 565-0871, Osaka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1037-3129","authenticated-orcid":false,"given":"Yoshitaka","family":"Nagai","sequence":"additional","affiliation":[{"name":"Department of Neurology, Kindai University Faculty of Medicine, Osaka-Sayama 589-8511, Osaka, Japan"},{"name":"Life Science Research Institute, Kindai University, Osaka-Sayama 589-8511, Osaka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,8,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1016\/S0140-6736(21)00218-X","article-title":"Parkinson\u2019s disease","volume":"397","author":"Bloem","year":"2021","journal-title":"Lancet"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"\u03b1-Synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0304-3940(98)00504-7","article-title":"Filamentous \u03b1-synuclein inclusions link multiple system atrophy with Parkinson\u2019s disease and dementia with Lewy bodies","volume":"251","author":"Spillantini","year":"1998","journal-title":"Neurosci. Lett."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"\u03b1-Synuclein in filamentous inclusions of Lewy bodies from Parkinson\u2019s disease and dementia with Lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding \u03b1-synuclein in Parkinson\u2019s disease","volume":"18","author":"Kuhn","year":"1998","journal-title":"Nat. Genet."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of \u03b1-synuclein causes Parkinson and Lewy body dementia","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann. Neurol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1002\/mds.25421","article-title":"Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson\u2019s disease","volume":"28","author":"Encarnacion","year":"2013","journal-title":"Mov. Disord."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1212\/WNL.0b013e31828727ba","article-title":"A novel \u03b1-synuclein missense mutation in Parkinson disease","volume":"80","author":"Proukakis","year":"2013","journal-title":"Neurology"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/ana.23894","article-title":"G51D \u03b1-synuclein mutation causes a novel parkinsonian-pyramidal syndrome","volume":"73","author":"Lesage","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the \u03b1-synuclein gene identified in families with Parkinson\u2019s disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2180.e1","DOI":"10.1016\/j.neurobiolaging.2014.03.024","article-title":"Novel \u03b1-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson\u2019s disease-type pathology","volume":"35","author":"Pasanen","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"\u03b1-Synuclein locus triplication causes Parkinson\u2019s disease","volume":"302","author":"Singleton","year":"2003","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/S0140-6736(04)17103-1","article-title":"\u03b1-Synuclein locus duplication as a cause of familial Parkinson\u2019s disease","volume":"364","author":"Kachergus","year":"2004","journal-title":"Lancet"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/ana.20438","article-title":"Multiple regions of \u03b1-synuclein are associated with Parkinson\u2019s disease","volume":"57","author":"Mueller","year":"2005","journal-title":"Ann. Neurol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1038\/ng.485","article-title":"Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson\u2019s disease","volume":"41","author":"Satake","year":"2009","journal-title":"Nat. Genet."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1038\/ng.487","article-title":"Genome-wide association study reveals genetic risk underlying Parkinson\u2019s disease","volume":"41","author":"Schulte","year":"2009","journal-title":"Nat. Genet."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1038\/35006074","article-title":"A Drosophila model of Parkinson\u2019s disease","volume":"404","author":"Feany","year":"2000","journal-title":"Nature"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"8968","DOI":"10.1073\/pnas.132197599","article-title":"Human \u03b1-synuclein-harboring familial Parkinson\u2019s disease-linked Ala-53 \u2192 Thr mutation causes neurodegenerative disease with \u03b1-synuclein aggregation in transgenic mice","volume":"99","author":"Lee","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1265","DOI":"10.1126\/science.287.5456.1265","article-title":"Dopaminergic loss and inclusion body formation in \u03b1-synuclein mice: Implications for neurodegenerative disorders","volume":"287","author":"Masliah","year":"2000","journal-title":"Science"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1038\/3311","article-title":"Accelerated in vitro fibril formation by a mutant \u03b1-synuclein linked to early-onset Parkinson disease","volume":"4","author":"Conway","year":"1998","journal-title":"Nat. Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1471-4159.2007.04764.x","article-title":"Neuropathology, biochemistry, and biophysics of \u03b1-synuclein aggregation","volume":"103","author":"Uversky","year":"2007","journal-title":"J. Neurochem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/0163-7827(85)90011-6","article-title":"Lipids of nervous tissue: Composition and metabolism","volume":"24","author":"Sastry","year":"1985","journal-title":"Prog. Lipid Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0009-3084(00)00128-6","article-title":"Glycerophospholipids in brain: Their metabolism, incorporation into membranes, functions, and involvement in neurological disorders","volume":"106","author":"Farooqui","year":"2000","journal-title":"Chem. Phys. Lipids"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00401-019-01977-2","article-title":"\u03b1-Synuclein and astrocytes: Tracing the pathways from homeostasis to neurodegeneration in Lewy body disease","volume":"138","author":"Sorrentino","year":"2019","journal-title":"Acta Neuropathol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1111\/j.1471-4159.2005.03247.x","article-title":"Fatty acid incorporation is decreased in astrocytes cultured from alpha-synuclein gene-ablated mice","volume":"94","author":"Castagnet","year":"2005","journal-title":"J Neurochem."},{"key":"ref_26","first-page":"433","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. Park. Dis."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/S1474-4422(12)70190-4","article-title":"The link between the GBA gene and parkinsonism","volume":"11","author":"Sidransky","year":"2012","journal-title":"Lancet Neurol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"6675","DOI":"10.1093\/hmg\/ddv372","article-title":"Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant \u03b1-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson\u2019s disease","volume":"24","author":"Suzuki","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1007\/s00401-023-02555-3","article-title":"Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson\u2019s disease-related fibril polymorphism","volume":"145","author":"Choong","year":"2023","journal-title":"Acta Neuropathol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1038\/ng1826","article-title":"PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron","volume":"38","author":"Morgan","year":"2006","journal-title":"Nat. Genet."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1002\/mds.27516","article-title":"Identification of a large homozygous VPS13C deletion in a patient with early-onset Parkinsonism","volume":"33","author":"Darvish","year":"2018","journal-title":"Mov. Disord."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Ill\u00e9s, A., Csab\u00e1n, D., Grosz, Z., Balicza, P., G\u00e9zsi, A., Moln\u00e1r, V., Bencsik, R., G\u00e1l, A., Kliv\u00e9nyi, P., and Molnar, M.J. (2019). The Role of Genetic Testing in the Clinical Practice and Research of Early-Onset Parkinsonian Disorders in a Hungarian Cohort: Increasing Challenge in Genetic Counselling, Improving Chances in Stratification for Clinical Trials. Front. Genet., 10.","DOI":"10.3389\/fgene.2019.01061"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1002\/jnr.23751","article-title":"Beyond Krabbe\u2019s disease: The potential contribution of galactosylceramidase deficiency to neuronal vulnerability in late-onset synucleinopathies","volume":"94","author":"Marshall","year":"2016","journal-title":"J. Neurosci. Res."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Araki, K., Yagi, N., Ikemoto, Y., Yagi, H., Choong, C.J., Hayakawa, H., Beck, G., Sumi, H., Fujimura, H., and Moriwaki, T. (2015). Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson\u2019s disease patients. Sci. Rep., 5.","DOI":"10.1038\/srep17625"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1093\/dnares\/5.6.401","article-title":"Absence of mutation in the beta- and gamma-synuclein genes in familial autosomal dominant Parkinson\u2019s disease","volume":"5","author":"Lavedan","year":"1998","journal-title":"DNA Res."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/0896-6273(95)90040-3","article-title":"Characterization of a novel protein regulated during the critical period for song learning in the zebra finch","volume":"15","author":"George","year":"1995","journal-title":"Neuron"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/0896-6273(95)90302-X","article-title":"The precursor protein of non-A beta component of Alzheimer\u2019s disease amyloid is a presynaptic protein of the central nervous system","volume":"14","author":"Iwai","year":"1995","journal-title":"Neuron"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2804","DOI":"10.1523\/JNEUROSCI.08-08-02804.1988","article-title":"Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal","volume":"8","author":"Maroteaux","year":"1988","journal-title":"J. Neurosci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S0165-3806(96)00210-6","article-title":"Delayed localization of synelfin (synuclein, NACP) to presynaptic terminals in cultured rat hippocampal neurons","volume":"99","author":"Withers","year":"1997","journal-title":"Brain Res. Dev. Brain Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"26292","DOI":"10.1074\/jbc.273.41.26292","article-title":"Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson\u2019s disease mutation","volume":"273","author":"Jensen","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"6715","DOI":"10.1523\/JNEUROSCI.1594-04.2004","article-title":"Lipid rafts mediate the synaptic localization of alpha-synuclein","volume":"24","author":"Fortin","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"6365","DOI":"10.1523\/JNEUROSCI.20-17-06365.2000","article-title":"Subcellular localization of wild-type and Parkinson\u2019s disease-associated mutant alpha -synuclein in human and transgenic mouse brain","volume":"20","author":"Kahle","year":"2000","journal-title":"J. Neurosci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1074\/jbc.M107045200","article-title":"Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form","volume":"277","author":"Lee","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0014-5793(94)00395-5","article-title":"Identification of two distinct synucleins from human brain","volume":"345","author":"Jakes","year":"1994","journal-title":"FEBS Lett."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"13709","DOI":"10.1021\/bi961799n","article-title":"NACP, a protein implicated in Alzheimer\u2019s disease and learning, is natively unfolded","volume":"35","author":"Weinreb","year":"1996","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"40186","DOI":"10.1074\/jbc.M305326200","article-title":"The association of \u03b1-synuclein with membranes affects bilayer structure, stability, and fibril formation","volume":"278","author":"Zhu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1038\/nsmb.3433","article-title":"Asparagine endopeptidase cleaves \u03b1-synuclein and mediates pathologic activities in Parkinson\u2019s disease","volume":"24","author":"Zhang","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/exnr.2000.7527","article-title":"In situ and in vitro study of colocalization and segregation of \u03b1-synuclein, ubiquitin, and lipids in Lewy bodies","volume":"166","author":"Gai","year":"2000","journal-title":"Exp. Neurol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2654","DOI":"10.1093\/brain\/awh584","article-title":"\u03b1-synuclein redistributes to neuromelanin lipid in the substantia nigra early in Parkinson\u2019s disease","volume":"128","author":"Halliday","year":"2005","journal-title":"Brain"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1074\/jbc.M008919200","article-title":"A hydrophobic stretch of 12 amino acid residues in the middle of \u03b1-synuclein is essential for filament assembly","volume":"276","author":"Giasson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1523\/JNEUROSCI.0285-07.2007","article-title":"Aggregated \u03b1-synuclein mediates dopaminergic neurotoxicity in vivo","volume":"27","author":"Periquet","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/nature15368","article-title":"Structure of the toxic core of \u03b1-synuclein from invisible crystals","volume":"525","author":"Rodriguez","year":"2015","journal-title":"Nature"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1046\/j.1471-4159.2001.00408.x","article-title":"Identification of the region of non-A\u03b2 component (NAC) of Alzheimer\u2019s disease amyloid responsible for its aggregation and toxicity","volume":"78","author":"Bodles","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.febslet.2011.01.009","article-title":"The role of the C-terminus of human \u03b1-synuclein: Intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers","volume":"585","author":"Hong","year":"2011","journal-title":"FEBS Lett."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1073\/pnas.0407146102","article-title":"Release of long-range tertiary interactions potentiates aggregation of natively unstructured \u03b1-synuclein","volume":"102","author":"Bertoncini","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/mds.26479","article-title":"Synaptic failure and alpha-synuclein","volume":"31","author":"Calo","year":"2016","journal-title":"Mov. Disord."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"11915","DOI":"10.1523\/JNEUROSCI.3821-06.2006","article-title":"Alpha-synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis","volume":"26","author":"Larsen","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neuron.2009.12.023","article-title":"Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis","volume":"65","author":"Nemani","year":"2010","journal-title":"Neuron"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3213","DOI":"10.1073\/pnas.1200575109","article-title":"Impaired neurotransmission caused by overexpression of alpha-synuclein in nigral dopamine neurons","volume":"109","author":"Lundblad","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Phan, J.A., Stokholm, K., Zareba-Paslawska, J., Jakobsen, S., Vang, K., Gjedde, A., Landau, A.M., and Romero-Ramos, M. (2017). Early synaptic dysfunction induced by alpha-synuclein in a rat model of Parkinson\u2019s disease. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-06724-9"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"4810","DOI":"10.1021\/bi036135+","article-title":"Effects of Parkinson\u2019s disease-linked mutations on the structure of lipid-associated alpha-synuclein","volume":"43","author":"Bussell","year":"2004","journal-title":"Biochemistry"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"7107","DOI":"10.1021\/bi7000246","article-title":"The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states","volume":"46","author":"Fredenburg","year":"2007","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1126\/science.1195227","article-title":"Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro","volume":"329","author":"Burre","year":"2010","journal-title":"Science"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e00592","DOI":"10.7554\/eLife.00592","article-title":"Native alpha-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2\/VAMP2","volume":"2","author":"Diao","year":"2013","journal-title":"Elife"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1038\/nn.4529","article-title":"alpha-Synuclein promotes dilation of the exocytotic fusion pore","volume":"20","author":"Logan","year":"2017","journal-title":"Nat. Neurosci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41556-024-01456-1","article-title":"VAMP2 chaperones \u03b1-synuclein in synaptic vesicle co-condensates","volume":"26","author":"Wang","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"ref_67","doi-asserted-by":"crossref","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":"ref_68","doi-asserted-by":"crossref","first-page":"20689","DOI":"10.1073\/pnas.1902958116","article-title":"Parkinson\u2019s disease-associated iPLA2-VIA\/PLA2G6 regulates neuronal functions and alpha-synuclein stability through membrane remodeling","volume":"116","author":"Mori","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"34393","DOI":"10.1074\/jbc.M004851200","article-title":"Interaction of human alpha-Synuclein and Parkinson\u2019s disease variants with phospholipids. Structural analysis using site-directed mutagenesis","volume":"275","author":"Perrin","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"4692","DOI":"10.1529\/biophysj.105.079251","article-title":"Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy","volume":"90","author":"Rhoades","year":"2006","journal-title":"Biophys. J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"7065","DOI":"10.1073\/pnas.1601899113","article-title":"Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of alpha-synuclein","volume":"113","author":"Galvagnion","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"31664","DOI":"10.1074\/jbc.M504894200","article-title":"A combinatorial code for the interaction of alpha-synuclein with membranes","volume":"280","author":"Kubo","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_73","first-page":"148","article-title":"Effects of oxidative stress inducers, neurotoxins, and ganglioside GM1 on Na+, K+-ATPase in PC12 and brain synaptosomes","volume":"43","author":"Zakharova","year":"2007","journal-title":"Zhurnal Evoliutsionnoi Biokhimii Fiziol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2279","DOI":"10.1016\/j.bpj.2010.07.056","article-title":"Effects of curvature and composition on alpha-synuclein binding to lipid vesicles","volume":"99","author":"Middleton","year":"2010","journal-title":"Biophys. J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/nrm2330","article-title":"Membrane lipids: Where they are and how they behave","volume":"9","author":"Voelker","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"32157","DOI":"10.1074\/jbc.M202838200","article-title":"Separation and characterization of late endosomal membrane domains","volume":"277","author":"Kobayashi","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"11195","DOI":"10.1074\/jbc.RA118.002780","article-title":"Effects of phosphatidylcholine membrane fluidity on theconformation and aggregation of N-terminally acetylated alpha-synuclein","volume":"293","author":"Jiang","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"15313","DOI":"10.1074\/jbc.M213128200","article-title":"A broken alpha -helix in folded alpha -Synuclein","volume":"278","author":"Chandra","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"7796","DOI":"10.1021\/ja801594s","article-title":"Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein","volume":"130","author":"Drescher","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.jmb.2009.05.066","article-title":"Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy","volume":"390","author":"Bodner","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/nrn3549","article-title":"Parkinson\u2019s disease dementia: Convergence of alpha-synuclein, tau and amyloid-beta pathologies","volume":"14","author":"Irwin","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nm1747","article-title":"Lewybody-likepathologyinlong-term embryonic nigral transplants in Parkinson\u2019s disease","volume":"14","author":"Kordower","year":"2008","journal-title":"Nat. Med."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2303","DOI":"10.1002\/mds.22369","article-title":"Transplanteddopaminergicneurons develop PD pathologic changes: A second case report","volume":"23","author":"Kordower","year":"2008","journal-title":"Mov. Disord."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/nm1746","article-title":"Lewy bodies in grafted neurons in subjects with Parkinson\u2019s disease suggest host-to-graft disease propagation","volume":"14","author":"Li","year":"2008","journal-title":"Nat. Med."},{"key":"ref_85","doi-asserted-by":"crossref","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. USA"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1172\/JCI43366","article-title":"alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells","volume":"121","author":"Hansen","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.nbd.2011.05.001","article-title":"Transfer of host-derived alpha synuclein to grafted dopaminergic neurons in rat","volume":"43","author":"Kordower","year":"2011","journal-title":"Neurobiol. Dis."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1126\/science.1227157","article-title":"Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice","volume":"338","author":"Luk","year":"2012","journal-title":"Science"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/s40478-017-0413-0","article-title":"Propagation of pathological alpha-synuclein in marmoset brain","volume":"5","author":"Shimozawa","year":"2017","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1186\/s40478-018-0587-0","article-title":"Rapid dissemination of alpha-synuclein seeds through neural circuits in an in-vivo prion-like seeding experiment","volume":"6","author":"Okuzumi","year":"2018","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"34328","DOI":"10.1074\/jbc.M004345200","article-title":"alpha-Synuclein membrane interactions and lipid specificity","volume":"275","author":"Jo","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4491","DOI":"10.1093\/hmg\/ddu165","article-title":"The novel Parkinson\u2019s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells","volume":"23","author":"Fares","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1021\/bi901723p","article-title":"Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson\u2019s disease revealed by solution NMR spectroscopy","volume":"49","author":"Bodner","year":"2010","journal-title":"Biochemistry"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"21856","DOI":"10.1074\/jbc.M114.553297","article-title":"The H50Q mutation enhances alpha-synuclein aggregation, secretion, and toxicity","volume":"289","author":"Khalaf","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","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":"ref_96","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1073\/pnas.97.2.571","article-title":"Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson\u2019s disease: Implications for pathogenesis and therapy","volume":"97","author":"Conway","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"6925","DOI":"10.1021\/bi400999d","article-title":"The Parkinson\u2019s disease-associated H50Q mutation accelerates \u03b1-Synuclein aggregation in vitro","volume":"52","author":"Ghosh","year":"2013","journal-title":"Biochemistry"},{"key":"ref_98","doi-asserted-by":"crossref","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":"ref_99","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1007\/s12035-012-8331-4","article-title":"\u03b1-Synuclein oligomers: An amyloid pore? Insights into mechanisms of \u03b1-synuclein oligomer-lipid interactions","volume":"47","author":"Zijlstra","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"7812","DOI":"10.1021\/bi0102398","article-title":"Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson\u2019s disease","volume":"40","author":"Volles","year":"2001","journal-title":"Biochemistry"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"4595","DOI":"10.1021\/bi0121353","article-title":"Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson\u2019s disease-linked mutations and occurs by a pore-like mechanism","volume":"41","author":"Volles","year":"2002","journal-title":"Biochemistry"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1021\/bi501369k","article-title":"Oligomers of Parkinson\u2019s Disease-Related \u03b1-Synuclein Mutants Have Similar Structures but Distinctive Membrane Permeabilization Properties","volume":"54","author":"Stefanovic","year":"2015","journal-title":"Biochemistry"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"44284","DOI":"10.1074\/jbc.M105343200","article-title":"Metal-triggered structural transformations, aggregation, and fibrillation of human \u03b1-synuclein. A possible molecular NK between Parkinson\u2019s disease and heavy metal exposure","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1111\/j.1749-6632.2000.tb06902.x","article-title":"Physiology and pathophysiology of alpha-synuclein. Cell culture and transgenic animal models based on a Parkinson\u2019s disease-associated protein","volume":"920","author":"Kahle","year":"2000","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.arr.2017.06.002","article-title":"Evolution of human apolipoprotein E (APOE) isoforms: Gene structure, protein function and interaction with dietary factors","volume":"37","author":"Huebbe","year":"2017","journal-title":"Ageing Res. Rev."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"32486","DOI":"10.1074\/jbc.M110.139576","article-title":"Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins","volume":"285","author":"Varkey","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"555","DOI":"10.2217\/clp.10.37","article-title":"Apolipoproteins in the brain: Implications for neurological and psychiatric disorders","volume":"51","author":"Elliott","year":"2010","journal-title":"Clin. Lipidol."},{"key":"ref_108","first-page":"1122","article-title":"Association of apolipoprotein E genotypes with prognosis in multiple sclerosis","volume":"15","author":"Tamam","year":"2011","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1089\/neu.2010.1623","article-title":"The association between apolipoprotein E and traumatic brain injury severity and functional outcome in a rehabilitation sample","volume":"28","author":"Ponsford","year":"2011","journal-title":"J. Neurotrauma"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/S0140-6736(94)90691-2","article-title":"The apolipoprotein E alleles as major susceptibility factors for Creutzfeldt-Jakob disease. The French Research Group on Epidemiology of Human Spongiform Encephalopathies","volume":"344","author":"Amouyel","year":"1994","journal-title":"Lancet"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.1016\/j.ajpath.2011.07.021","article-title":"Apolipoprotein E and LRP1 increase early in Parkinson\u2019s disease pathogenesis","volume":"179","author":"Wilhelmus","year":"2011","journal-title":"Am. J. Pathol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.neulet.2016.02.042","article-title":"Effects of different isoforms of apoE on aggregation of the \u03b1-synuclein protein implicated in Parkinson\u2019s disease","volume":"618","author":"Emamzadeh","year":"2016","journal-title":"Neurosci. Lett."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"15226","DOI":"10.1073\/pnas.1821409116","article-title":"\u03b1-synuclein-lipoprotein interactions and elevated ApoE level in cerebrospinal fluid from Parkinson\u2019s disease patients","volume":"116","author":"Paslawski","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1126\/science.1172046","article-title":"Germline P granules are liquid droplets that localize by controlled dissolution\/condensation","volume":"324","author":"Brangwynne","year":"2009","journal-title":"Science"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","article-title":"Liquid-liquid phase separation in biology","volume":"30","author":"Hyman","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.cell.2016.06.010","article-title":"Compositional control of phase-separated cellular bodies","volume":"166","author":"Banani","year":"2016","journal-title":"Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"R1097","DOI":"10.1016\/j.cub.2017.08.069","article-title":"Phase separation in biology","volume":"27","author":"Alberti","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tcb.2018.02.004","article-title":"Protein phase separation: A new phase in cell biology","volume":"28","author":"Boeynaems","year":"2018","journal-title":"Trends Cell Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"2415","DOI":"10.1021\/acs.biochem.7b01136","article-title":"Functional Implications of Intracellular Phase Transitions","volume":"57","author":"Holehouse","year":"2018","journal-title":"Biochemistry"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.str.2016.07.007","article-title":"ALS mutations disrupt phase separation mediated by \u03b1-helical structure in the TDP-43 low-complexity C-terminal domain","volume":"24","author":"Conicella","year":"2016","journal-title":"Structure"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"e98049","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"EMBO J."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/s41467-017-00480-0","article-title":"Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau","volume":"8","author":"Ambadipudi","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1038\/s41557-020-0465-9","article-title":"\u03b1-Synuclein aggregation nucleates through liquid-liquid phase separation","volume":"12","author":"Ray","year":"2020","journal-title":"Nat. Chem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.bbrc.2022.02.097","article-title":"Calcium promotes \u03b1-synuclein liquid-liquid phase separation to accelerate amyloid aggregation","volume":"603","author":"Huang","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3643","DOI":"10.1021\/bm500937p","article-title":"Protein\/lipid coaggregates are formed during \u03b1-synuclein-induced disruption of lipid bilayers","volume":"15","author":"Vetri","year":"2014","journal-title":"Biomacromolecules"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1002\/path.1710990106","article-title":"Ultrastructural observations in Parkinsonism","volume":"99","author":"Roy","year":"1969","journal-title":"J. Pathol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/BF00685366","article-title":"Presenile dementia with Alzheimer-, Pick- and Lewy-body changes","volume":"36","author":"Kosaka","year":"1976","journal-title":"Acta Neuropathol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1001\/archneur.55.2.151","article-title":"Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia","volume":"55","author":"Trojanowski","year":"1998","journal-title":"Arch. Neurol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"21500","DOI":"10.1074\/jbc.M000099200","article-title":"Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments","volume":"275","author":"Jensen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1007\/s00401-017-1722-x","article-title":"Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins","volume":"134","author":"Flavin","year":"2017","journal-title":"Acta Neuropathol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1001\/archneur.1969.00480180071006","article-title":"Sphingomyelin in Lewy inclusion bodies in Parkinson\u2019s disease","volume":"21","year":"1969","journal-title":"Arch. Neurol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/BF02251136","article-title":"Lewy bodies in parkinsonism share components with intraneuronal protein bodies of normal brains","volume":"3","author":"Issidorides","year":"1991","journal-title":"J. Neural. Transm. Park. Dis. Dement. Sect."},{"key":"ref_136","doi-asserted-by":"crossref","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":"ref_137","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1111\/jnc.13385","article-title":"The relationship between glucocerebrosidase mutations and Parkinson disease","volume":"139","author":"Schapira","year":"2016","journal-title":"J. Neurochem."},{"key":"ref_138","first-page":"212706","article-title":"\u03b1-Synuclein transgenic Drosophila as a model of Parkinson\u2019s disease and related synucleinopathies","volume":"2011","author":"Mizuno","year":"2010","journal-title":"Park. Dis."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.neuron.2017.12.012","article-title":"Reversible conformational conversion of \u03b1-synuclein into toxic assemblies by glucosylceramide","volume":"97","author":"Zunke","year":"2018","journal-title":"Neuron"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1002\/mds.23774","article-title":"Lysosomal storage disorders and Parkinson\u2019s disease: Gaucher disease and beyond","volume":"26","author":"Shachar","year":"2011","journal-title":"Mov. Disord."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.semcdb.2004.03.002","article-title":"Secondary accumulation of gangliosides in lysosomal storage disorders","volume":"15","author":"Walkley","year":"2004","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_142","doi-asserted-by":"crossref","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":"ref_143","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1007\/s12035-018-1090-0","article-title":"Characterization of brain lysosomal activities in GBA-related and sporadic Parkinson\u2019s disease and dementia with Lewy bodies","volume":"56","author":"Moors","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1093\/brain\/awt367","article-title":"Reduced glucocerebrosidase is associated with increased alpha- synuclein in sporadic Parkinson\u2019s disease","volume":"137","author":"Murphy","year":"2014","journal-title":"Brain"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1186\/s13024-015-0010-2","article-title":"Selective loss of glucocerebrosidase activity in sporadic Parkinson\u2019s disease and dementia with Lewy bodies","volume":"10","author":"Chiasserini","year":"2015","journal-title":"Mol. Neurodegener."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1002\/humu.22373","article-title":"Mutation in the SYNJ1 gene associated with autosomal recessive, early-onset Parkinsonism","volume":"34","author":"Quadri","year":"2013","journal-title":"Hum. Mutat."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/s40478-016-0298-3","article-title":"High expression of \u03b1-synuclein in damaged mitochondria with PLA2G6 dysfunction","volume":"4","author":"Beck","year":"2016","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.cmet.2018.05.019","article-title":"Phospholipase PLA2G6, a Parkinsonism-Associated Gene, Affects Vps26 and Vps35, Retromer Function, and Ceramide Levels, Similar to \u03b1-Synuclein Gain","volume":"28","author":"Lin","year":"2018","journal-title":"Cell Metab."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Olsen, A.L., and Feany, M.B. (2021). Parkinson\u2019s disease risk genes act in glia to control neuronal \u03b1-synuclein toxicity. Neurobiol. Dis., 159.","DOI":"10.1016\/j.nbd.2021.105482"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1093\/brain\/awac002","article-title":"Prion-like \u03b1-synuclein pathology in the brain of infants with Krabbe disease","volume":"145","author":"Hatton","year":"2022","journal-title":"Brain"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1007\/s00401-007-0264-z","article-title":"Neuronal and glial accumulation of a- and b-synucleins in human lipidoses","volume":"114","author":"Suzuki","year":"2007","journal-title":"Acta Neuropathol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1007\/s00401-007-0325-3","article-title":"Mechanisms of neurodegeneration in mucopolysaccharidoses II and IIIB: Analysis of human brain tissue","volume":"115","author":"Hamano","year":"2008","journal-title":"Acta Neuropathol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1021\/bi061749a","article-title":"GM1 specifically interacts with alpha-synuclein and inhibits fibrillation","volume":"46","author":"Martinez","year":"2007","journal-title":"Biochemistry"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.jmb.2011.03.009","article-title":"Molecular basis for the glycosphingolipid-binding specificity of a-synuclein: Key role of tyrosine 39 in membrane insertion","volume":"408","author":"Fantini","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.1074\/jbc.M114.585703","article-title":"Acceleration of a-synuclein aggregation by exosomes","volume":"290","author":"Grey","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.jmb.2009.09.008","article-title":"Molecular insights into the interaction between \u03b1-synuclein and docosahexaenoic acid","volume":"394","author":"Frare","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"9110","DOI":"10.1073\/pnas.171300598","article-title":"\u03b1-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins","volume":"98","author":"Sharon","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1194\/jlr.M600003-JLR200","article-title":"Interactions between fatty acids and \u03b1-synuclein","volume":"47","author":"Gantz","year":"2006","journal-title":"J. Lipid Res."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"15610","DOI":"10.1021\/bi061743l","article-title":"\u03b1-Synuclein adopts an \u03b1-helical conformation in the presence of polyunsaturated fatty acids to hinder micelle formation","volume":"45","author":"Broersen","year":"2006","journal-title":"Biochemistry"},{"key":"ref_160","first-page":"219","article-title":"Role of different regions of \u03b1-synuclein in the interaction with the brain fatty acid DHA","volume":"5","year":"2014","journal-title":"J. Chromatogr. Sep. Tech."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/S0896-6273(03)00024-2","article-title":"The formation of highly soluble oligomers of \u03b1-synuclein is regulated by fatty acids and enhanced in Parkinson\u2019s disease","volume":"37","author":"Sharon","year":"2003","journal-title":"Neuron"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"22262","DOI":"10.1074\/jbc.M110.202937","article-title":"Structural and morphological characterization of aggregated species of \u03b1-synuclein induced by docosahexaenoic acid","volume":"286","author":"Frare","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"46674","DOI":"10.1074\/jbc.M308231200","article-title":"Rapid anionic micelle-mediated \u03b1-synuclein fibrillization in vitro","volume":"278","author":"Necula","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Iljina, M., Tosatto, L., Choi, M.L., Sang, J.C., Ye, Y., Hughes, C.D., Bryant, C.E., Gandhi, S., and Klenerman, D. (2016). Arachidonic acid mediates the formation of abundant \u03b1-helical multimers of \u03b1-synuclein. Sci. Rep., 6.","DOI":"10.1038\/srep33928"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"41958","DOI":"10.1074\/jbc.M105022200","article-title":"Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins","volume":"276","author":"Perrin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1007\/s12031-010-9439-5","article-title":"Membrane lipid modification by docosahexaenoic acid (DHA) promotes the formation of \u03b1-synuclein inclusion bodies immunopositive for SUMO-1 in oligodendroglial cells after oxidative stress","volume":"43","author":"Riedel","year":"2011","journal-title":"J. Mol. Neurosci."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.freeradbiomed.2017.07.004","article-title":"Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways","volume":"110","author":"Welander","year":"2017","journal-title":"Free Radic. Biol. Med."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/16\/8935\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:37:46Z","timestamp":1760110666000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/16\/8935"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,8,16]]},"references-count":167,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2024,8]]}},"alternative-id":["ijms25168935"],"URL":"https:\/\/doi.org\/10.3390\/ijms25168935","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,8,16]]}}}