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Neurosci."},{"key":"10.1016\/j.nbd.2022.105966_bb0335","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1126\/science.290.5493.985","article-title":"Oxidative damage linked to neurodegeneration by selective \u03b1-synuclein nitration in synucleinopathy lesions","volume":"290","author":"Giasson","year":"2000","journal-title":"Science."},{"key":"10.1016\/j.nbd.2022.105966_bb0340","doi-asserted-by":"crossref","first-page":"2168","DOI":"10.3390\/biomedicines10092168","article-title":"Rational generation of monoclonal antibodies selective for pathogenic forms of alpha-synuclein","volume":"10","author":"Gibbs","year":"2022","journal-title":"Biomedicines."},{"key":"10.1016\/j.nbd.2022.105966_bb0345","doi-asserted-by":"crossref","first-page":"E115","DOI":"10.1038\/35017124","article-title":"Is there a cause-and-effect relationship between \u03b1-synuclein fibrillization and Parkinson\u2019s disease?","volume":"2","author":"Goldberg","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0350","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1006\/jmbi.1998.2299","article-title":"Watching amyloid fibrils grow by time-lapse atomic force microscopy","volume":"285","author":"Goldsbury","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0355","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jsb.2010.09.018","article-title":"Amyloid structure and assembly: insights from scanning transmission electron microscopy","volume":"173","author":"Goldsbury","year":"2011","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0360","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/j.tibs.2010.05.007","article-title":"Zooming into protein oligomerization in neurodegeneration using BiFC","volume":"35","author":"Goncalves","year":"2010","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0365","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1005995","article-title":"shRNA-based screen identifies endocytic recycling pathway components that act as genetic modifiers of alpha-synuclein aggregation, secretion and toxicity","volume":"12","author":"Gon\u00e7alves","year":"2016","journal-title":"PLoS Genet."},{"key":"10.1016\/j.nbd.2022.105966_bb0370","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.36402","article-title":"Cryo-EM structure of alpha-synuclein fibrils","volume":"7","author":"Guerrero-Ferreira","year":"2018","journal-title":"elife."},{"key":"10.1016\/j.nbd.2022.105966_bb0375","doi-asserted-by":"crossref","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":"10.1016\/j.nbd.2022.105966_bb0380","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bpc.2015.07.003","article-title":"Solid-state NMR: an emerging technique in structural biology of self-assemblies","volume":"210","author":"Habenstein","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0385","doi-asserted-by":"crossref","first-page":"1584","DOI":"10.1039\/C5OB02329G","article-title":"Comparison of strategies for non-perturbing labeling of \u03b1-synuclein to study amyloidogenesis","volume":"14","author":"Haney","year":"2016","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0390","doi-asserted-by":"crossref","first-page":"15871","DOI":"10.1073\/pnas.0506109102","article-title":"Molecular-level secondary structure, polymorphism, and dynamics of full-length \u03b1-synuclein fibrils studied by solid-state NMR","volume":"102","author":"Heise","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0395","doi-asserted-by":"crossref","first-page":"eabc2487","DOI":"10.1126\/sciadv.abc2487","article-title":"Determinants of seeding and spreading of \u03b1-synuclein pathology in the brain","volume":"6","author":"Henrich","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.nbd.2022.105966_bb0400","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jmb.2008.08.039","article-title":"Structural characteristics of \u03b1-synuclein oligomers stabilized by the flavonoid baicalein","volume":"383","author":"Hong","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0405","article-title":"A guide to studying protein aggregation","author":"Housmans","year":"2021","journal-title":"FEBS J"},{"key":"10.1016\/j.nbd.2022.105966_bb0410","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. 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Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0430","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1021\/jacs.8b13094","article-title":"A \u201cclickable\u201d photoconvertible small fluorescent molecule as a minimalist probe for tracking individual biomolecule complexes","volume":"141","author":"Jun","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"4","key":"10.1016\/j.nbd.2022.105966_bb0435","doi-asserted-by":"crossref","first-page":"e314","DOI":"10.1038\/emm.2017.1","article-title":"Amplification of distinct \u03b1-synuclein fibril conformers through protein misfolding cyclic amplification","volume":"49","author":"Jung","year":"2017","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.nbd.2022.105966_bb0440","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1002\/cphc.201000996","article-title":"A FRET sensor for non-invasive imaging of amyloid formation in vivo","volume":"12","author":"Kaminski Schierle","year":"2011","journal-title":"ChemPhysChem."},{"key":"10.1016\/j.nbd.2022.105966_bb0445","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.bbapap.2005.06.005","article-title":"How to study proteins by circular dichroism","volume":"1751","author":"Kelly","year":"2005","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"issue":"2862\u20132874","key":"10.1016\/j.nbd.2022.105966_bb0450","article-title":"In vivo protein complementation demonstrates presynaptic \u03b1-synuclein oligomerization and age-dependent accumulation of 8\u201316-mer oligomer species","volume":"29","author":"Kiechle","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.nbd.2022.105966_bb0455","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1080\/15548627.2016.1207014","article-title":"Anti-aging treatments slow propagation of synucleinopathy by restoring lysosomal function","volume":"12","author":"Kim","year":"2016","journal-title":"Autophagy."},{"key":"10.1016\/j.nbd.2022.105966_bb0460","doi-asserted-by":"crossref","first-page":"5155","DOI":"10.1002\/ejoc.201800524","article-title":"Synthesis of a fluorescent probe for sensing multiple protein states","volume":"2018","author":"Kucherak","year":"2018","journal-title":"Eur. J. Org. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0465","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1126\/science.1251652","article-title":"The resolution revolution","volume":"343","author":"K\u00fchlbrandt","year":"2014","journal-title":"Science."},{"key":"10.1016\/j.nbd.2022.105966_bb0470","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/s41570-021-00254-9","article-title":"Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases","volume":"5","author":"Kulenkampff","year":"2021","journal-title":"Nat. Rev. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0475","doi-asserted-by":"crossref","first-page":"16891","DOI":"10.1074\/jbc.M117.795617","article-title":"Modulation of the extent of structural heterogeneity in \u03b1-synuclein fibrils by the small molecule thioflavin T","volume":"292","author":"Kumar","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0480","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2020.105086","volume":"146","author":"Kumar","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.nbd.2022.105966_bb0485","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1080\/19336896.2019.1704612","article-title":"Proteinase K resistant cores of prions and amyloids","volume":"14","author":"Kushnirov","year":"2020","journal-title":"Prion."},{"key":"10.1016\/j.nbd.2022.105966_bb0490","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1021\/acs.analchem.5b02747","article-title":"High fluorescence anisotropy of thioflavin T in aqueous solution resulting from its molecular rotor nature","volume":"88","author":"Kuznetsova","year":"2016","journal-title":"Anal. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0495","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1038\/s41593-018-0294-y","article-title":"TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates","volume":"22","author":"Laferri\u00e8re","year":"2019","journal-title":"Nat. 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Biol. Chem."},{"key":"10.1016\/j.nbd.2022.105966_bb0515","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2020.104876","article-title":"Do Lewy bodies contain alpha-synuclein fibrils? And does it matter? A brief history and critical analysis of recent reports","volume":"141","author":"Lashuel","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.nbd.2022.105966_bb0520","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0196056","article-title":"ELISA method to detect \u03b1-synuclein oligomers in cell and animal models","volume":"13","author":"Lassen","year":"2018","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2022.105966_bb0525","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1038\/s41593-019-0541-x","article-title":"\u03b1-Synuclein strains target distinct brain regions and cell types","volume":"23","author":"Lau","year":"2020","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.nbd.2022.105966_bb0530","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40478-016-0402-8","article-title":"The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation","volume":"4","author":"L\u00e1zaro","year":"2016","journal-title":"Acta Neuropathol. Commun."},{"issue":"797\u2013801","key":"10.1016\/j.nbd.2022.105966_bb0535","article-title":"Site-specific three-color labeling of \u03b1-synuclein via conjugation to uniquely reactive cysteines during assembly by native chemical ligation","volume":"25","author":"Lee","year":"2018","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0540","doi-asserted-by":"crossref","DOI":"10.1016\/j.expneurol.2021.113810","article-title":"Memantine exerts neuroprotective effects by modulating \u03b1-synuclein transmission in a parkinsonian model","volume":"344","author":"Lee","year":"2021","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.nbd.2022.105966_bb0545","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer\u2019s disease \u03b2-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"Levine","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0550","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"[18] Quantification of \u03b2-sheet amyloid fibril structures with thioflavin T","author":"LeVine","year":"1999"},{"key":"10.1016\/j.nbd.2022.105966_bb0555","first-page":"1","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":"10.1016\/j.nbd.2022.105966_bb0560","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1038\/s41422-018-0075-x","article-title":"Amyloid fibril structure of \u03b1-synuclein determined by cryo-electron microscopy","volume":"28","author":"Li","year":"2018","journal-title":"Cell Res."},{"key":"10.1016\/j.nbd.2022.105966_bb0565","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1002\/2211-5463.13110","article-title":"Seeded assembly in vitro does not replicate the structures of \u03b1-synuclein filaments from multiple system atrophy","volume":"11","author":"L\u00f6vestam","year":"2021","journal-title":"FEBS Open Bio."},{"key":"10.1016\/j.nbd.2022.105966_bb0570","doi-asserted-by":"crossref","first-page":"20051","DOI":"10.1073\/pnas.0908005106","article-title":"Exogenous \u03b1-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."},{"key":"10.1016\/j.nbd.2022.105966_bb0575","doi-asserted-by":"crossref","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":"10.1016\/j.nbd.2022.105966_bb0580","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1021\/bi501188a","article-title":"Purification of \u03b1-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity","volume":"54","author":"Luth","year":"2015","journal-title":"Biochemistry."},{"key":"10.1016\/j.nbd.2022.105966_bb0585","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.jmb.2012.04.009","article-title":"Structural comparison of mouse and human \u03b1-synuclein amyloid fibrils by solid-state NMR","volume":"420","author":"Lv","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0590","doi-asserted-by":"crossref","first-page":"4971","DOI":"10.1073\/pnas.1913904117","article-title":"The process of Lewy body formation, rather than simply \u03b1-synuclein fibrillization, is one of the major drivers of neurodegeneration","volume":"117","author":"Mahul-Mellier","year":"2020","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0595","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1002\/mds.27907","article-title":"\u03b1-Synuclein real-time quaking-induced conversion in the submandibular glands of Parkinson\u2019s disease patients","volume":"35","author":"Manne","year":"2020","journal-title":"Mov. Disord."},{"key":"10.1016\/j.nbd.2022.105966_bb0600","doi-asserted-by":"crossref","first-page":"3232","DOI":"10.1021\/acsnano.8b08932","article-title":"Vibrational circular dichroism reveals supramolecular chirality inversion of \u03b1-synuclein peptide assemblies upon interactions with anionic membranes","volume":"13","author":"Martial","year":"2019","journal-title":"ACS Nano"},{"key":"10.1016\/j.nbd.2022.105966_bb0605","doi-asserted-by":"crossref","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":"10.1016\/j.nbd.2022.105966_bb0610","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.jneumeth.2016.03.016","article-title":"Purification of \u03b1-synuclein containing inclusions from human post mortem brain tissue","volume":"266","author":"Mccormack","year":"2016","journal-title":"J. Neurosci. Methods"},{"key":"10.1016\/j.nbd.2022.105966_bb0615","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/S0306-4522(01)00113-0","article-title":"\u03b1-Synuclein\u2013enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons","volume":"104","author":"McLean","year":"2001","journal-title":"Neuroscience."},{"key":"10.1016\/j.nbd.2022.105966_bb0620","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/j.tibs.2017.08.001","article-title":"Emerging structural understanding of amyloid fibrils by solid-state NMR","volume":"42","author":"Meier","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0625","doi-asserted-by":"crossref","first-page":"147","DOI":"10.3390\/life10080147","article-title":"Alpha-synuclein FRET biosensors reveal early alpha-synuclein aggregation in the endoplasmic reticulum","volume":"10","author":"Miraglia","year":"2020","journal-title":"Life."},{"key":"10.1016\/j.nbd.2022.105966_bb0630","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0025954","article-title":"Effect of surfaces on amyloid fibril formation","volume":"6","author":"Moores","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2022.105966_bb0635","series-title":"Alpha-Synuclein","first-page":"221","article-title":"Single-molecule fret detection of early-stage conformations in \u03b1-synuclein aggregation","author":"Moosa","year":"2019"},{"key":"10.1016\/j.nbd.2022.105966_bb0640","series-title":"Amyloid Proteins","first-page":"121","article-title":"X-ray fibre diffraction studies of amyloid fibrils","author":"Morris","year":"2012"},{"key":"10.1016\/j.nbd.2022.105966_bb0645","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1016\/j.bbapap.2016.07.007","article-title":"The effect of fluorescent labeling on \u03b1-synuclein fibril morphology","volume":"1864","author":"Mu\u010dibabi\u0107","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"10.1016\/j.nbd.2022.105966_bb0650","doi-asserted-by":"crossref","first-page":"12305","DOI":"10.1523\/JNEUROSCI.3088-08.2008","article-title":"Optical reporters for the conformation of \u03b1-synuclein reveal a specific interaction with mitochondria","volume":"28","author":"Nakamura","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.nbd.2022.105966_bb0655","doi-asserted-by":"crossref","first-page":"4578","DOI":"10.1039\/C9SC04730A","article-title":"ThX\u2013a next-generation probe for the early detection of amyloid aggregates","volume":"11","author":"Needham","year":"2020","journal-title":"Chem. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0660","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1111\/j.1471-4159.2008.05407.x","article-title":"Accumulation and clearance of \u03b1-synuclein aggregates demonstrated by time-lapse imaging","volume":"106","author":"Opazo","year":"2008","journal-title":"J. Neurochem."},{"key":"10.1016\/j.nbd.2022.105966_bb0665","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1016\/j.celrep.2015.01.060","article-title":"Progressive aggregation of alpha-synuclein and selective degeneration of lewy inclusion-bearing neurons in a mouse model of parkinsonism","volume":"10","author":"Osterberg","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.nbd.2022.105966_bb0670","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1126\/science.1090439","article-title":"Yeast cells provide insight into alpha-synuclein biology and pathobiology","volume":"302","author":"Outeiro","year":"2003","journal-title":"Science."},{"key":"10.1016\/j.nbd.2022.105966_bb0675","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/9282f173-df82-4b70-9120-b4e62b3dacb1","article-title":"Formation of toxic oligomeric \u03b1-synuclein species in living cells","volume":"3","author":"Outeiro","year":"2008","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2022.105966_bb0680","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1093\/brain\/awn349","article-title":"Detection of elevated levels of soluble \u03b1-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies","volume":"132","author":"Paleologou","year":"2009","journal-title":"Brain."},{"key":"10.1016\/j.nbd.2022.105966_bb0685","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1021\/acschembio.9b01038","article-title":"Chemoenzymatic semisynthesis of phosphorylated \u03b1-synuclein enables identification of a bidirectional effect on fibril formation","volume":"15","author":"Pan","year":"2020","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0690","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/0022-510X(92)90286-T","article-title":"Accumulation of tubular structures in oligodendroglial and neuronal cells as the basic alteration in multiple system atrophy","volume":"107","author":"Papp","year":"1992","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0695","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/nature14547","article-title":"\u03b1-Synuclein strains cause distinct synucleinopathies after local and systemic administration","volume":"522","author":"Peelaerts","year":"2015","journal-title":"Nature."},{"key":"10.1016\/j.nbd.2022.105966_bb0700","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/s41586-018-0104-4","article-title":"Cellular milieu imparts distinct pathological \u03b1-synuclein strains in \u03b1-synucleinopathies","volume":"557","author":"Peng","year":"2018","journal-title":"Nature."},{"key":"10.1016\/j.nbd.2022.105966_bb0705","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1042\/bse0560011","article-title":"The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation","volume":"56","author":"Perrett","year":"2014","journal-title":"Essays Biochem."},{"issue":"916\u2013927","key":"10.1016\/j.nbd.2022.105966_bb0710","article-title":"Quantitative characterization of \u03b1-synuclein aggregation in living cells through automated microfluidics feedback control","volume":"27","author":"Perrino","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.nbd.2022.105966_bb0715","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.tibs.2007.08.003","article-title":"Fluorescent protein FRET: the good, the bad and the ugly","volume":"32","author":"Piston","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0720","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1093\/brain\/awab431","article-title":"Diagnostic value of cerebrospinal fluid alpha-synuclein seed quantification in synucleinopathies","volume":"145","author":"Poggiolini","year":"2022","journal-title":"Brain."},{"key":"10.1016\/j.nbd.2022.105966_bb0725","first-page":"67","article-title":"Vibrational circular dichroism studies of biological macromolecules and their complexes","author":"Polyanichko","year":"2011","journal-title":"Circ. Dichroism: Theory Spectroscopy."},{"key":"10.1016\/j.nbd.2022.105966_bb0730","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1096\/fj.201800148RRR","article-title":"Monitoring \u03b1-synuclein multimerization in vivo","volume":"33","author":"Prasad","year":"2019","journal-title":"FASEB J."},{"key":"10.1016\/j.nbd.2022.105966_bb0735","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-10525-5","article-title":"Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins","volume":"7","author":"Raskatov","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.nbd.2022.105966_bb0740","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1002\/ana.24066","article-title":"Lewy body extracts from Parkinson disease brains trigger \u03b1-synuclein pathology and neurodegeneration in mice and monkeys","volume":"75","author":"Recasens","year":"2014","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.nbd.2022.105966_bb0745","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s43586-020-00002-1","article-title":"Solid-state NMR spectroscopy","volume":"1","author":"Reif","year":"2021","journal-title":"Nat. Rev. Methods Primers."},{"key":"10.1016\/j.nbd.2022.105966_bb0750","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1111\/j.1747-0285.2011.01110.x","article-title":"Insight into amyloid structure using chemical probes","volume":"77","author":"Reinke","year":"2011","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.nbd.2022.105966_bb0755","doi-asserted-by":"crossref","DOI":"10.1111\/jnc.15601","article-title":"Plasma \u03b1-synuclein and phosphorylated tau 181 as a diagnostic biomarker panel for de novo Parkinson\u2019s disease","author":"Ren","year":"2022","journal-title":"J. Neurochem161: 506-515"},{"key":"10.1016\/j.nbd.2022.105966_bb0760","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1038\/nmeth1026","article-title":"Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged \u03b1-synuclein","volume":"4","author":"Roberti","year":"2007","journal-title":"Nat. Methods"},{"key":"10.1016\/j.nbd.2022.105966_bb0765","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0023338","article-title":"Confocal fluorescence anisotropy and FRAP imaging of \u03b1-synuclein amyloid aggregates in living cells","volume":"6","author":"Roberti","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2022.105966_bb0770","doi-asserted-by":"crossref","first-page":"1642","DOI":"10.1093\/brain\/awv040","article-title":"Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson\u2019s disease brain","volume":"138","author":"Roberts","year":"2015","journal-title":"Brain."},{"key":"10.1016\/j.nbd.2022.105966_bb0775","doi-asserted-by":"crossref","first-page":"E4758","DOI":"10.1073\/pnas.1800690115","article-title":"Developing a molecular dynamics force field for both folded and disordered protein states","volume":"115","author":"Robustelli","year":"2018","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0780","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":"10.1016\/j.nbd.2022.105966_bb0785","series-title":"Alpha-Synuclein","first-page":"123","article-title":"Circular dichroism and isothermal titration calorimetry to study the interaction of \u03b1-synuclein with membranes","author":"Rovere","year":"2019"},{"key":"10.1016\/j.nbd.2022.105966_bb0790","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1111\/nan.12486","article-title":"Detection of alpha-synuclein conformational variants from gastro-intestinal biopsy tissue as a potential biomarker for Parkinson\u2019s disease","volume":"44","author":"Ruffmann","year":"2018","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.nbd.2022.105966_bb0795","doi-asserted-by":"crossref","first-page":"5213","DOI":"10.1021\/acsnano.9b09676","article-title":"The influence of pathogenic mutations in \u03b1-synuclein on biophysical and structural characteristics of amyloid fibrils","volume":"14","author":"Ruggeri","year":"2020","journal-title":"ACS Nano"},{"key":"10.1016\/j.nbd.2022.105966_bb0800","doi-asserted-by":"crossref","first-page":"12247","DOI":"10.1021\/acsnano.8b06047","article-title":"Combined use of unnatural amino acids enables dual-color super-resolution imaging of proteins via click chemistry","volume":"12","author":"Saal","year":"2018","journal-title":"ACS Nano"},{"key":"10.1016\/j.nbd.2022.105966_bb0805","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1006\/exnr.2002.7961","article-title":"Heterogeneity of nigral and cortical Lewy bodies differentiated by amplified triple-labeling for alpha-synuclein, ubiquitin, and thiazin red","volume":"177","author":"Sakamoto","year":"2002","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.nbd.2022.105966_bb0810","doi-asserted-by":"crossref","first-page":"8407","DOI":"10.1021\/ja101645g","article-title":"NMR characterization of long-range order in intrinsically disordered proteins","volume":"132","author":"Salmon","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.nbd.2022.105966_bb0815","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s42003-021-02126-w","article-title":"Super-resolution imaging reveals \u03b1-synuclein seeded aggregation in SH-SY5Y cells","volume":"4","author":"Sang","year":"2021","journal-title":"Commun. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0820","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamem.2013.04.012","article-title":"ATR-FTIR: a \u201crejuvenated\u201d tool to investigate amyloid proteins","volume":"1828","author":"Sarroukh","year":"2013","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembranes."},{"key":"10.1016\/j.nbd.2022.105966_bb0825","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40478-020-01026-0","article-title":"Trans-synaptic and retrograde axonal spread of Lewy pathology following pre-formed fibril injection in an in vivo A53T alpha-synuclein mouse model of synucleinopathy","volume":"8","author":"Schaser","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.nbd.2022.105966_bb0830","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.3390\/vaccines10091432","article-title":"A novel C-type lectin receptor-targeted \u03b1-synuclein-based Parkinson vaccine induces potent immune responses and therapeutic efficacy in mice","volume":"10","author":"Schmidhuber","year":"2022","journal-title":"Vaccines."},{"key":"10.1016\/j.nbd.2022.105966_bb0835","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1007\/s12551-016-0234-6","article-title":"Analytical methods for structural ensembles and dynamics of intrinsically disordered proteins","volume":"8","author":"Schor","year":"2016","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.nbd.2022.105966_bb0840","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1038\/s41586-020-2317-6","article-title":"Structures of \u03b1-synuclein filaments from multiple system atrophy","volume":"585","author":"Schweighauser","year":"2020","journal-title":"Nature."},{"key":"10.1016\/j.nbd.2022.105966_bb0845","doi-asserted-by":"crossref","first-page":"8842","DOI":"10.1039\/C8CS00185E","article-title":"Excited-state intramolecular proton-transfer (ESIPT) based fluorescence sensors and imaging agents","volume":"47","author":"Sedgwick","year":"2018","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.nbd.2022.105966_bb0850","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1007\/s00401-019-01961-w","article-title":"Wide distribution of alpha-synuclein oligomers in multiple system atrophy brain detected by proximity ligation","volume":"137","author":"Sekiya","year":"2019","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.nbd.2022.105966_bb0855","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40478-022-01440-6","article-title":"Discrepancy between distribution of alpha-synuclein oligomers and Lewy-related pathology in Parkinson\u2019s disease","volume":"10","author":"Sekiya","year":"2022","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.nbd.2022.105966_bb0860","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.jsb.2007.04.001","article-title":"Looking into live cells with in-cell NMR spectroscopy","volume":"158","author":"Selenko","year":"2007","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0865","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1073\/pnas.97.9.4897","article-title":"Fiber diffraction of synthetic \u03b1-synuclein filaments shows amyloid-like cross-\u03b2 conformation","volume":"97","author":"Serpell","year":"2000","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0870","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":"10.1016\/j.nbd.2022.105966_bb0875","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/s41586-020-1984-7","article-title":"Discriminating \u03b1-synuclein strains in Parkinson\u2019s disease and multiple system atrophy","volume":"578","author":"Shahnawaz","year":"2020","journal-title":"Nature."},{"key":"10.1016\/j.nbd.2022.105966_bb0880","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.01345","article-title":"Three-dimensional electron crystallography of protein microcrystals","volume":"2","author":"Shi","year":"2013","journal-title":"Elife."},{"key":"10.1016\/j.nbd.2022.105966_bb0885","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.cbpa.2021.04.011","article-title":"New strategies for fluorescently labeling proteins in the study of amyloids","volume":"64","author":"Shimogawa","year":"2021","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0890","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1016\/j.bpj.2020.01.022","article-title":"Differential membrane binding and seeding of distinct \u03b1-synuclein fibrillar polymorphs","volume":"118","author":"Shrivastava","year":"2020","journal-title":"Biophys. J."},{"key":"10.1016\/j.nbd.2022.105966_bb0895","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/13506129.2018.1517736","article-title":"Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in \u03b1-synuclein fibrils","volume":"25","author":"Sidhu","year":"2018","journal-title":"Amyloid."},{"key":"10.1016\/j.nbd.2022.105966_bb0900","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/nmeth1131","article-title":"Prion strain discrimination using luminescent conjugated polymers","volume":"4","author":"Sigurdson","year":"2007","journal-title":"Nat. Methods"},{"key":"10.1016\/j.nbd.2022.105966_bb0905","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1038\/nmeth947","article-title":"Direct observation of individual endogenous protein complexes in situ by proximity ligation","volume":"3","author":"S\u00f6derberg","year":"2006","journal-title":"Nat. Methods"},{"key":"10.1016\/j.nbd.2022.105966_bb0910","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":"10.1016\/j.nbd.2022.105966_bb0915","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."},{"key":"10.1016\/j.nbd.2022.105966_bb0920","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-13564-w","article-title":"Structural heterogeneity of \u03b1-synuclein fibrils amplified from patient brain extracts","volume":"10","author":"Stroh\u00e4ker","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.nbd.2022.105966_bb0925","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41422-020-0299-4","article-title":"Cryo-EM structure of full-length \u03b1-synuclein amyloid fibril with Parkinson\u2019s disease familial A53T mutation","volume":"30","author":"Sun","year":"2020","journal-title":"Cell Res."},{"key":"10.1016\/j.nbd.2022.105966_bb0930","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0935","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1007\/s13311-021-01070-1","article-title":"FRET-based screening identifies p38 MAPK and PKC inhibition as targets for prevention of seeded \u03b1-Synuclein aggregation","volume":"18","author":"Svanbergsson","year":"2021","journal-title":"Neurotherapeutics."},{"key":"10.1016\/j.nbd.2022.105966_bb0940","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuint.2022.105345","article-title":"Evolution of \u03b1-synuclein conformation ensemble toward amyloid fibril via liquid-liquid phase separation (LLPS) as investigated by dynamic nuclear polarization-enhanced solid-state MAS NMR","volume":"157","author":"Takamuku","year":"2022","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.nbd.2022.105966_bb0945","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1038\/nchembio.1818","article-title":"Layers of structure and function in protein aggregation","volume":"11","author":"Tanaka","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0950","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1093\/brain\/awab374","article-title":"Brain injections of glial cytoplasmic inclusions induce a multiple system atrophy-like pathology","volume":"145","author":"Teil","year":"2022","journal-title":"Brain."},{"key":"10.1016\/j.nbd.2022.105966_bb0955","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/nature16531","article-title":"Structural disorder of monomeric \u03b1-synuclein persists in mammalian cells","volume":"530","author":"Theillet","year":"2016","journal-title":"Nature."},{"key":"10.1016\/j.nbd.2022.105966_bb0960","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1111\/j.0953-816X.2004.03139.x","article-title":"Risk factors for dopaminergic neuron loss in human \u03b1-synuclein transgenic mice","volume":"19","author":"Thiruchelvam","year":"2004","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.nbd.2022.105966_bb0965","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-22108-0","article-title":"In situ architecture of neuronal \u03b1-Synuclein inclusions","volume":"12","author":"Trinkaus","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.nbd.2022.105966_bb0970","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nsmb.3194","article-title":"Solid-state NMR structure of a pathogenic fibril of full-length human \u03b1-synuclein","volume":"23","author":"Tuttle","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb0975","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-07383-6","article-title":"Novel animal model defines genetic contributions for neuron-to-neuron transfer of \u03b1-synuclein","volume":"7","author":"Tyson","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.nbd.2022.105966_bb0980","doi-asserted-by":"crossref","first-page":"11282","DOI":"10.1073\/pnas.90.23.11282","article-title":"Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease","volume":"90","author":"Ueda","year":"1993","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb0985","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0010589","article-title":"In vivo imaging of \u03b1-synuclein in mouse cortex demonstrates stable expression and differential subcellular compartment mobility","volume":"5","author":"Unni","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.nbd.2022.105966_bb0990","first-page":"1","article-title":"Alpha-synuclein oligomers and small nerve fiber pathology in skin are potential biomarkers of Parkinson\u2019s disease","volume":"7","author":"Vacchi","year":"2021","journal-title":"NPJ Parkinson\u2019s Dis."},{"key":"10.1016\/j.nbd.2022.105966_bb0995","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.nbd.2015.04.009","article-title":"Generation and characterization of novel conformation-specific monoclonal antibodies for \u03b1-synuclein pathology","volume":"79","author":"Vaikath","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.nbd.2022.105966_bb1000","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1111\/jnc.14713","article-title":"Antibodies against alpha-synuclein: tools and therapies","volume":"150","author":"Vaikath","year":"2019","journal-title":"J. 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Mol. Biol."},{"key":"10.1016\/j.nbd.2022.105966_bb1020","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2022.853050","article-title":"Real-time quaking-induced conversion assays for prion diseases, synucleinopathies, and tauopathies","volume":"14","author":"Vascellari","year":"2022","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.nbd.2022.105966_bb1025","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of \u03b1-synuclein fibrils","volume":"105","author":"Vilar","year":"2008","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.nbd.2022.105966_bb1030","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1111\/jnc.13249","article-title":"Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies","volume":"139","author":"Villar-Piqu\u00e9","year":"2016","journal-title":"J. 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