{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T02:18:43Z","timestamp":1787451523152,"version":"build-2736575974"},"reference-count":61,"publisher":"Oxford University Press (OUP)","issue":"23","license":[{"start":{"date-parts":[[2021,7,13]],"date-time":"2021-07-13T00:00:00Z","timestamp":1626134400000},"content-version":"vor","delay-in-days":1,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS099328"],"award-info":[{"award-number":["NS099328"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS121826"],"award-info":[{"award-number":["NS121826"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS083845"],"award-info":[{"award-number":["NS083845"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Michael J Fox Foundation"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,11,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>\u03b1-Synuclein (\u03b1S) has been well-documented to play a role in human synucleinopathies such as Parkinson\u2019s disease (PD) and dementia with Lewy bodies (DLB). First, the lesions found in PD\/DLB brains\u2014Lewy bodies and Lewy neurites\u2014are rich in aggregated \u03b1S. Second, genetic evidence links missense mutations and increased \u03b1S expression to familial forms of PD\/DLB. Third, toxicity and cellular stress can be caused by \u03b1S under certain experimental conditions. In contrast, the homologs \u03b2-synuclein (\u03b2S) and \u03b3-synuclein (\u03b3S) are not typically found in Lewy bodies\/neurites, have not been clearly linked to brain diseases and have been largely non-toxic in experimental settings. In \u03b1S, the so-called non-amyloid-\u03b2 component of plaques (NAC) domain, constituting amino acids 61\u201395, has been identified to be critical for aggregation in vitro. This domain is partially absent in \u03b2S and only incompletely conserved in \u03b3S, which could explain why both homologs do not cause disease. However, \u03b1S in vitro aggregation and cellular toxicity have not been firmly linked experimentally, and it has been proposed that excess \u03b1S membrane binding is sufficient to induce neurotoxicity. Indeed, recent characterizations of Lewy bodies have highlighted the accumulation of lipids and membranous organelles, raising the possibility that \u03b2S and \u03b3S could also become neurotoxic if they were more prone to membrane\/lipid binding. Here, we increased \u03b2S and \u03b3S membrane affinity by strategic point mutations and demonstrate that these proteins behave like membrane-associated monomers, are cytotoxic and form round cytoplasmic inclusions that can be prevented by inhibiting stearoyl-CoA desaturase.<\/jats:p>","DOI":"10.1093\/hmg\/ddab188","type":"journal-article","created":{"date-parts":[[2021,7,9]],"date-time":"2021-07-09T11:13:24Z","timestamp":1625829204000},"page":"2332-2346","source":"Crossref","is-referenced-by-count":17,"title":["Excess membrane binding of monomeric alpha-, beta- and gamma-synuclein is invariably associated with inclusion formation and toxicity"],"prefix":"10.1093","volume":"30","author":[{"given":"Tae-Eun","family":"Kim","sequence":"first","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew J","family":"Newman","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thibaut","family":"Imberdis","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lisa","family":"Brontesi","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arati","family":"Tripathi","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nagendran","family":"Ramalingam","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saranna","family":"Fanning","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dennis","family":"Selkoe","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulf","family":"Dettmer","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,7,12]]},"reference":[{"key":"2021111806111839700_ref1","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"2021111806111839700_ref2","first-page":"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. Int. J. Rapid Publ. Rep. Genes Genomes"},{"key":"2021111806111839700_ref3","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0304-3940(99)00420-6","article-title":"No pathogenic mutations in the beta-synuclein gene in Parkinson\u2019s disease","volume":"269","author":"Lincoln","year":"1999","journal-title":"Neurosci. Lett."},{"key":"2021111806111839700_ref4","first-page":"879","article-title":"Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson\u2019s disease and dementia with Lewy bodies","volume":"152","author":"Baba","year":"1998","journal-title":"Am. J. Pathol."},{"key":"2021111806111839700_ref5","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S0002-9440(10)64548-8","article-title":"Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology","volume":"157","author":"Galvin","year":"2000","journal-title":"Am. J. Pathol."},{"key":"2021111806111839700_ref6","doi-asserted-by":"crossref","first-page":"13450","DOI":"10.1073\/pnas.96.23.13450","article-title":"Axon pathology in Parkinson\u2019s disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein","volume":"96","author":"Galvin","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111806111839700_ref7","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1001\/archneurol.2010.177","article-title":"Association of alpha-, beta-, and gamma-synuclein with diffuse lewy body disease","volume":"67","author":"Nishioka","year":"2010","journal-title":"Arch. Neurol."},{"key":"2021111806111839700_ref8","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1212\/01.WNL.0000139870.14385.3C","article-title":"Beta-synuclein gene alterations in dementia with Lewy bodies","volume":"63","author":"Ohtake","year":"2004","journal-title":"Neurology"},{"key":"2021111806111839700_ref9","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":"2021111806111839700_ref10","doi-asserted-by":"crossref","first-page":"9335","DOI":"10.1523\/JNEUROSCI.18-22-09335.1998","article-title":"Persyn, a member of the synuclein family, has a distinct pattern of expression in the developing nervous system","volume":"18","author":"Buchman","year":"1998","journal-title":"J. Neurosci."},{"key":"2021111806111839700_ref11","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1007\/s004390050792","article-title":"Identification, localization and characterization of the human gamma-synuclein gene","volume":"103","author":"Lavedan","year":"1998","journal-title":"Hum. Genet."},{"key":"2021111806111839700_ref12","first-page":"759","article-title":"Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing","volume":"57","author":"Ji","year":"1997","journal-title":"Cancer Res."},{"key":"2021111806111839700_ref13","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":"2021111806111839700_ref14","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":"2021111806111839700_ref15","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":"2021111806111839700_ref16","doi-asserted-by":"crossref","first-page":"19666","DOI":"10.1073\/pnas.0807826105","article-title":"Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement","volume":"105","author":"Jao","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111806111839700_ref17","doi-asserted-by":"crossref","first-page":"12856","DOI":"10.1021\/ja804517m","article-title":"Membrane-bound alpha-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles","volume":"130","author":"Georgieva","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"2021111806111839700_ref18","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/1074-5521(95)90071-3","article-title":"The core Alzheimer\u2019s peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease?","volume":"2","author":"Han","year":"1995","journal-title":"Chem. Biol."},{"key":"2021111806111839700_ref19","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1097\/00005072-199608000-00004","article-title":"Characterization of the precursor protein of the non-A beta component of senile plaques (NACP) in the human central nervous system","volume":"55","author":"Irizarry","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"2021111806111839700_ref20","doi-asserted-by":"crossref","first-page":"9427","DOI":"10.1021\/bi900539p","article-title":"Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization","volume":"48","author":"Waxman","year":"2009","journal-title":"Biochemistry"},{"key":"2021111806111839700_ref21","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 alpha-synuclein is essential for filament assembly","volume":"276","author":"Giasson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref22","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1110\/ps.073181508","article-title":"Molecular determinants of the aggregation behavior of alpha- and beta-synuclein","volume":"17","author":"Rivers","year":"2008","journal-title":"Protein Sci."},{"key":"2021111806111839700_ref23","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1016\/j.bbrc.2008.02.127","article-title":"Characterization of fibrillation process of alpha-synuclein at the initial stage","volume":"369","author":"Tashiro","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021111806111839700_ref24","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1016\/j.bbadis.2009.06.010","article-title":"The effect of amino acid substitution in the imperfect repeat sequences of alpha-synuclein on fibrillation","volume":"1792","author":"Harada","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111806111839700_ref25","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.nbd.2014.05.031","article-title":"Lysine residues at the first and second KTKEGV repeats mediate \u03b1-synuclein binding to membrane phospholipids","volume":"70","author":"Zarbiv","year":"2014","journal-title":"Neurobiol. Dis."},{"key":"2021111806111839700_ref26","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/j.ejmech.2016.01.044","article-title":"Coupling of the non-amyloid-component (NAC) domain and the KTK(E\/Q)GV repeats stabilize the \u03b1-synuclein fibrils","volume":"121","author":"Xu","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"2021111806111839700_ref27","doi-asserted-by":"publisher","first-page":"104543","DOI":"10.1016\/j.nbd.2019.104543","article-title":"Dynamic behaviors of \u03b1-synuclein and tau in the cellular context: new mechanistic insights and therapeutic opportunities in neurodegeneration","volume":"132","author":"Yeboah","year":"2019","journal-title":"Neurobiol. Dis."},{"key":"2021111806111839700_ref28","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"\u03b1-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"Bartels","year":"2011","journal-title":"Nature"},{"key":"2021111806111839700_ref29","doi-asserted-by":"crossref","first-page":"6371","DOI":"10.1074\/jbc.M112.403311","article-title":"In vivo cross-linking reveals principally oligomeric forms of \u03b1-synuclein and \u03b2-synuclein in neurons and non-neural cells","volume":"288","author":"Dettmer","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref30","doi-asserted-by":"crossref","first-page":"9596","DOI":"10.1073\/pnas.1505953112","article-title":"KTKEGV repeat motifs are key mediators of normal \u03b1-synuclein tetramerization: their mutation causes excess monomers and neurotoxicity","volume":"112","author":"Dettmer","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111806111839700_ref31","doi-asserted-by":"crossref","first-page":"7314","DOI":"10.1038\/ncomms8314","article-title":"Parkinson-causing \u03b1-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation","volume":"6","author":"Dettmer","year":"2015","journal-title":"Nat. Commun."},{"key":"2021111806111839700_ref32","doi-asserted-by":"crossref","first-page":"147349","DOI":"10.1016\/j.brainres.2021.147349","article-title":"Crowded organelles, lipid accumulation, and abnormal membrane tubulation in cellular models of enhanced \u03b1-synuclein membrane interaction","volume":"1758","author":"Ericsson","year":"2021","journal-title":"Brain Res."},{"key":"2021111806111839700_ref33","doi-asserted-by":"crossref","first-page":"7177","DOI":"10.1074\/jbc.M808895200","article-title":"Curvature dynamics of alpha-synuclein familial Parkinson disease mutants: molecular simulations of the micelle- and bilayer-bound forms","volume":"284","author":"Perlmutter","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref34","doi-asserted-by":"crossref","first-page":"9799","DOI":"10.1074\/jbc.RA118.006551","article-title":"E46K-like \u03b1-synuclein mutants increase lipid interactions and disrupt membrane selectivity","volume":"294","author":"Rovere","year":"2019","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref35","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1016\/j.cub.2014.08.027","article-title":"\u03b1-Synuclein multimers cluster synaptic vesicles and attenuate recycling","volume":"24","author":"Wang","year":"2014","journal-title":"Curr. Biol. CB"},{"key":"2021111806111839700_ref36","doi-asserted-by":"crossref","first-page":"5221","DOI":"10.1523\/JNEUROSCI.4650-14.2015","article-title":"Definition of a molecular pathway mediating \u03b1-synuclein neurotoxicity","volume":"35","author":"Burr\u00e9","year":"2015","journal-title":"J. Neurosci."},{"key":"2021111806111839700_ref37","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1002\/1873-3468.13047","article-title":"Refolding of helical soluble \u03b1-synuclein through transient interaction with lipid interfaces","volume":"592","author":"Rovere","year":"2018","journal-title":"FEBS Lett."},{"key":"2021111806111839700_ref38","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2021.100271","article-title":"Temperature is a key determinant of alpha- and beta-synuclein membrane interactions in neurons","volume":"296","author":"Ramalingam","year":"2021","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref39","doi-asserted-by":"crossref","first-page":"3466","DOI":"10.1093\/hmg\/ddx227","article-title":"Loss of native \u03b1-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells","volume":"26","author":"Dettmer","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"2021111806111839700_ref40","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21155193","article-title":"Rapid alpha-synuclein toxicity in a neural cell model and its rescue by a stearoyl-CoA desaturase inhibitor","volume":"21","author":"Terry-Kantor","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"2021111806111839700_ref41","article-title":"Lipidomic analysis of \u03b1-synuclein neurotoxicity identifies stearoyl CoA desaturase as a target for Parkinson treatment","volume":"73","author":"Fanning","year":"2018","journal-title":"Mol. Cell."},{"key":"2021111806111839700_ref42","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1903216116","article-title":"Cell models of lipid-rich \u03b1-synuclein aggregation validate known modifiers of \u03b1-synuclein biology and identify stearoyl-CoA desaturase","volume":"116","author":"Imberdis","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2021111806111839700_ref43","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1038\/s41531-019-0103-7","article-title":"Parkinson\u2019s disease: proteinopathy or lipidopathy?","volume":"6","author":"Fanning","year":"2020","journal-title":"NPJ Park. Dis."},{"key":"2021111806111839700_ref44","doi-asserted-by":"crossref","first-page":"2742","DOI":"10.1016\/j.celrep.2018.11.028","article-title":"Inhibiting stearoyl-CoA desaturase ameliorates \u03b1-synuclein cytotoxicity","volume":"25","author":"Vincent","year":"2018","journal-title":"Cell Rep."},{"key":"2021111806111839700_ref45","doi-asserted-by":"crossref","first-page":"207","DOI":"10.3389\/fnagi.2019.00207","article-title":"Genetic silencing of fatty acid desaturases modulates \u03b1-synuclein toxicity and neuronal loss in Parkinson-like models of C. elegans","volume":"11","author":"Maulik","year":"2019","journal-title":"Front. Aging Neurosci."},{"key":"2021111806111839700_ref46","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1016\/j.jmb.2006.12.044","article-title":"Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity","volume":"366","author":"Volles","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021111806111839700_ref47","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/s41589-020-0480-6","article-title":"Deep mutational scanning reveals the structural basis for \u03b1-synuclein activity","volume":"16","author":"Newberry","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"2021111806111839700_ref48","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1091\/mbc.e07-08-0827","article-title":"Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae","volume":"19","author":"Soper","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"2021111806111839700_ref49","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1126\/science.1129462","article-title":"Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson\u2019s models","volume":"313","author":"Cooper","year":"2006","journal-title":"Science"},{"key":"2021111806111839700_ref50","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1126\/science.1245296","article-title":"Identification and rescue of \u03b1-synuclein toxicity in Parkinson patient-derived neurons","volume":"342","author":"Chung","year":"2013","journal-title":"Science"},{"key":"2021111806111839700_ref51","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":"2021111806111839700_ref52","doi-asserted-by":"crossref","first-page":"21966","DOI":"10.1074\/jbc.M401076200","article-title":"Alpha-synuclein has a high affinity for packing defects in a bilayer membrane: a thermodynamics study","volume":"279","author":"Nuscher","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021111806111839700_ref53","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.1021\/acschemneuro.0c00405","article-title":"Effect of disease-associated P123H and V70M mutations on \u03b2-synuclein fibrillation","volume":"11","author":"Sharma","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"2021111806111839700_ref54","doi-asserted-by":"crossref","first-page":"15164","DOI":"10.1038\/srep15164","article-title":"Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein","volume":"5","author":"Janowska","year":"2015","journal-title":"Sci. Rep."},{"key":"2021111806111839700_ref55","doi-asserted-by":"crossref","first-page":"36010","DOI":"10.1038\/srep36010","article-title":"\u03b2-Synuclein suppresses both the initiation and amplification steps of \u03b1-synuclein aggregation via competitive binding to surfaces","volume":"6","author":"Brown","year":"2016","journal-title":"Sci. Rep."},{"key":"2021111806111839700_ref56","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1016\/j.jmb.2018.05.024","article-title":"Multi-pronged interactions underlie inhibition of \u03b1-synuclein aggregation by \u03b2-synuclein","volume":"430","author":"Williams","year":"2018","journal-title":"J. Mol. Biol."},{"key":"2021111806111839700_ref57","doi-asserted-by":"crossref","first-page":"17579","DOI":"10.1038\/s41598-019-54063-8","article-title":"Increased dynamics of \u03b1-synuclein fibrils by \u03b2-synuclein leads to reduced seeding and cytotoxicity","volume":"9","author":"Yang","year":"2019","journal-title":"Sci. Rep."},{"key":"2021111806111839700_ref58","doi-asserted-by":"crossref","first-page":"334","DOI":"10.3390\/ijms19020334","article-title":"Unveiling a selective mechanism for the inhibition of \u03b1-synuclein aggregation by \u03b2-synuclein","volume":"19","author":"Leitao","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"2021111806111839700_ref59","doi-asserted-by":"crossref","first-page":"623","DOI":"10.3389\/fnins.2018.00623","article-title":"Rationally designed variants of \u03b1-synuclein illuminate its in vivo structural properties in health and disease","volume":"12","author":"Dettmer","year":"2018","journal-title":"Front. Neurosci."},{"key":"2021111806111839700_ref60","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/978-1-4939-9124-2_8","article-title":"Studying \u03b1-synuclein conformation by intact-cell cross-linking","volume":"1948","author":"Imberdis","year":"2019","journal-title":"Methods Mol. Biol. Clifton NJ"},{"key":"2021111806111839700_ref61","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.mcn.2004.06.014","article-title":"Dimerization of Parkinson\u2019s disease-causing DJ-1 and formation of high molecular weight complexes in human brain","volume":"27","author":"Baulac","year":"2004","journal-title":"Mol. Cell. 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