{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T19:05:52Z","timestamp":1780599952656,"version":"3.54.1"},"reference-count":92,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T00:00:00Z","timestamp":1722211200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T00:00:00Z","timestamp":1722211200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeckfonden","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002808","name":"Carlsbergfondet","doi-asserted-by":"publisher","award":["CF19-0337"],"award-info":[{"award-number":["CF19-0337"]}],"id":[{"id":"10.13039\/501100002808","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002808","name":"Carlsbergfondet","doi-asserted-by":"publisher","award":["CF20-0610"],"award-info":[{"award-number":["CF20-0610"]}],"id":[{"id":"10.13039\/501100002808","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["npj Parkinsons Dis."],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\u03b1-Synuclein (\u03b1-syn) accumulates as insoluble amyloid but also forms soluble \u03b1-syn oligomers (\u03b1SOs), thought to be even more cytotoxic than fibrils. To detect and block the unwanted activities of these \u03b1SOs, we have raised 30 monoclonal antibodies (mAbs) against different forms of \u03b1SOs, ranging from unmodified \u03b1SOs to species stabilized by lipid peroxidation products and polyphenols, \u03b1SOs formed by C-terminally truncated \u03b1-syn, and multivalent display of \u03b1-syn on capsid virus-like particles (cVLPs). While the mAbs generally show a preference for \u03b1SOs, they also bind fibrils, but to variable extents. Overall, we observe great diversity in the mAbs\u2019 relative affinities for monomers and \u03b1SOs, varied requirements for the C-terminal extension of \u03b1-syn, and only a modest effect on \u03b1-syn fibrillation. Several mAbs show several orders of magnitude preference for \u03b1SOs over monomers in in-solution studies, while the commercial antibody MJF14 only bound 10-fold more strongly to \u03b1SOs than monomeric \u03b1-syn. Gratifyingly, seven mAbs almost completely block \u03b1SO permeabilization of membrane vesicles. Five selected mAbs identified \u03b1-syn-related pathologies like Lewy bodies (LBs) and Lewy Neurites, as well as Glial Cytoplasmic Inclusions in postmortem brains from people diagnosed for PD, dementia with LBs or multiple system atrophy, although to different extents. Three mAbs were particularly useful for pathological evaluation of postmortem brain human tissue, including early stages of PD. Although there was no straightforward connection between the mAbs\u2019 biophysical and immunohistochemical properties, it is encouraging that this comprehensive collection of mAbs able to recognize different aggregated \u03b1-syn species in vitro also holds diagnostic potential.<\/jats:p>","DOI":"10.1038\/s41531-024-00747-6","type":"journal-article","created":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T05:03:10Z","timestamp":1722229390000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic \u03b1-synuclein oligomers"],"prefix":"10.1038","volume":"10","author":[{"given":"Janni","family":"Nielsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johanne","family":"Lauritsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jannik N.","family":"Pedersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan S.","family":"Nowak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-8505-9994","authenticated-orcid":false,"given":"Malthe K.","family":"Bendtsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-3209-2482","authenticated-orcid":false,"given":"Giulia","family":"Kleijwegt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9354-4986","authenticated-orcid":false,"given":"Kaija","family":"Lusser","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laia C.","family":"Pitarch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juli\u00e1n V.","family":"Moreno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1894-1859","authenticated-orcid":false,"given":"Matthias M.","family":"Schneider","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Georg","family":"Krainer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louise","family":"Goks\u00f8yr","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6160-4674","authenticated-orcid":false,"given":"Paul","family":"Khalif\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8975-1825","authenticated-orcid":false,"given":"Sanne Simone","family":"Kaalund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7940-6246","authenticated-orcid":false,"given":"Susana","family":"Aznar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magnus","family":"Kj\u00e6rgaard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vita","family":"Sereikait\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristian","family":"Str\u00f8mgaard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tuomas P. J.","family":"Knowles","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Morten Agertoug","family":"Nielsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam F.","family":"Sander","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0970-578X","authenticated-orcid":false,"given":"Marina","family":"Romero-Ramos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2918-8989","authenticated-orcid":false,"given":"Daniel E.","family":"Otzen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,7,29]]},"reference":[{"key":"747_CR1","doi-asserted-by":"publisher","first-page":"612","DOI":"10.1111\/jnc.14713","volume":"150","author":"NN Vaikath","year":"2019","unstructured":"Vaikath, N. N. et al. Antibodies against \u03b1-synuclein: tools and therapies. J. Neurochem 150, 612\u2013625 (2019).","journal-title":"J. Neurochem"},{"key":"747_CR2","doi-asserted-by":"publisher","first-page":"168","DOI":"10.3390\/biom12020168","volume":"12","author":"J Folke","year":"2022","unstructured":"Folke, J. et al. Passive Immunization in \u03b1-synuclein Preclinical Animal Models. Biomolecules 12, 168 (2022).","journal-title":"Biomolecules"},{"key":"747_CR3","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/j.brainres.2018.01.010","volume":"1693","author":"RodgerA Liddle","year":"2018","unstructured":"Liddle, Rodger A. Parkinson\u2019s disease from the gut. Brain Res. 1693, 201\u2013206 (2018).","journal-title":"Brain Res."},{"key":"747_CR4","doi-asserted-by":"publisher","first-page":"363","DOI":"10.3389\/fneur.2019.00363","volume":"10","author":"JJ Mendoza-Vel squez","year":"2019","unstructured":"Mendoza-Vel squez, J. J. et al. Autonomic dysfunction in \u03b1-Synucleinopathies. Front. Neurol. 10, 363 (2019).","journal-title":"Front. Neurol."},{"key":"747_CR5","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1007\/s00702-023-02633-6","volume":"130","author":"P Borghammer","year":"2023","unstructured":"Borghammer, P. The brain-first vs. body-first model of Parkinson\u2019s disease with comparison to alternative models. J. Neural Transm. 130, 737\u2013753 (2023).","journal-title":"J. Neural Transm."},{"key":"747_CR6","doi-asserted-by":"publisher","first-page":"S281","DOI":"10.3233\/JPD-191721","volume":"9","author":"P Borghammer","year":"2019","unstructured":"Borghammer, P. et al. Brain-first versus gut-first Parkinson\u2019s disease: A Hypothesis. J. Parkinsons Dis. 9, S281\u2013S295 (2019).","journal-title":"J. Parkinsons Dis."},{"key":"747_CR7","doi-asserted-by":"publisher","first-page":"433","DOI":"10.3233\/JPD-171103","volume":"7","author":"C Galvagnion","year":"2017","unstructured":"Galvagnion, C. The role of lipids interacting with \u03b1-synuclein in the Pathogenesis of Parkinson\u2019s disease. J. Parkinsons Dis. 7, 433\u2013450 (2017).","journal-title":"J. Parkinsons Dis."},{"key":"747_CR8","doi-asserted-by":"publisher","first-page":"9364","DOI":"10.1523\/JNEUROSCI.4787-13.2014","volume":"34","author":"KJ Vargas","year":"2014","unstructured":"Vargas, K. J. et al. Synucleins regulate the kinetics of synaptic vesicle endocytosis. J. Neurosci. 34, 9364\u20139376 (2014).","journal-title":"J. Neurosci."},{"key":"747_CR9","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1126\/science.1129462","volume":"313","author":"AA Cooper","year":"2006","unstructured":"Cooper, A. A. et al. \u03b1-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson\u2019s models. Science 313, 234\u2013238 (2006).","journal-title":"Science"},{"key":"747_CR10","doi-asserted-by":"publisher","first-page":"2857","DOI":"10.1016\/j.bpj.2008.12.3940","volume":"96","author":"L Kj\u00e6r","year":"2009","unstructured":"Kj\u00e6r, L. et al. The influence of vesicle composition and size on \u03b1-synuclein structure and stability. Biophys. J. 96, 2857\u20132870 (2009).","journal-title":"Biophys. J."},{"key":"747_CR11","doi-asserted-by":"publisher","first-page":"852","DOI":"10.1136\/jnnp.74.7.852","volume":"74","author":"C Colosimo","year":"2003","unstructured":"Colosimo, C. et al. Lewy body cortical involvement may not always predict dementia in Parkinson\u2019s disease. J. Neurol. Neurosurg. Psychiatry 74, 852\u2013856 (2003).","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"747_CR12","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1002\/ana.20321","volume":"57","author":"L Parkkinen","year":"2005","unstructured":"Parkkinen, L. et al. \u03b1-Synuclein pathology does not predict extrapyramidal symptoms or dementia. Ann. Neurol. 57, 82\u201391 (2005).","journal-title":"Ann. Neurol."},{"key":"747_CR13","first-page":"6838965","volume":"2018","author":"KK Johansen","year":"2018","unstructured":"Johansen, K. K. et al. A case of Parkinson\u2019s disease with no lewy body pathology due to a homozygous exon deletion in Parkin. Case Rep. Neurol. Med. 2018, 6838965 (2018).","journal-title":"Case Rep. Neurol. Med."},{"key":"747_CR14","doi-asserted-by":"publisher","first-page":"1089","DOI":"10.1016\/S0022-2836(02)00735-0","volume":"322","author":"HA Lashuel","year":"2002","unstructured":"Lashuel, H. A. et al. \u03b1-synuclein, especially the Parkinson\u2019s Disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322, 1089\u20131102 (2002).","journal-title":"J. Mol. Biol."},{"key":"747_CR15","doi-asserted-by":"publisher","first-page":"1766","DOI":"10.1212\/WNL.0b013e3181fd613b","volume":"75","author":"T Tokuda","year":"2010","unstructured":"Tokuda, T. et al. Detection of elevated levels of \u03b1-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 75, 1766\u20131772 (2010).","journal-title":"Neurology"},{"key":"747_CR16","doi-asserted-by":"publisher","first-page":"1945","DOI":"10.1096\/fj.03-0098fje","volume":"17","author":"OMA El-Agnaf","year":"2003","unstructured":"El-Agnaf, O. M. A. et al. \u03b1-synuclein implicated in Parkinson\u2019s disease is present in extracellular biological fluids, including human plasma. FASEB J. 17, 1945\u20131947 (2003).","journal-title":"FASEB J."},{"key":"747_CR17","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1016\/S0896-6273(03)00024-2","volume":"37","author":"R Sharon","year":"2003","unstructured":"Sharon, R. et al. The formation of highly soluble oligomers of \u03b1-synuclein is regulated by fatty acids and enhanced in Parkinson\u2019s disease. Neuron 37, 583\u2013595 (2003).","journal-title":"Neuron"},{"key":"747_CR18","doi-asserted-by":"publisher","first-page":"1642","DOI":"10.1093\/brain\/awv040","volume":"138","author":"RF Roberts","year":"2015","unstructured":"Roberts, R. F. et al. Direct visualization of \u03b1-synuclein oligomers reveals previously undetected pathology in Parkinson\u2019s disease brain. Brain 138, 1642\u20131657 (2015).","journal-title":"Brain"},{"key":"747_CR19","doi-asserted-by":"publisher","first-page":"7560","DOI":"10.1002\/anie.201400491","volume":"53","author":"W Paslawski","year":"2014","unstructured":"Paslawski, W. et al. Co-existence of two different \u03b1-synuclein oligomers with different core structures determined by Hydrogen\/Deuterium Exchange Mass Spectrometry. Angew. Chem. Int Ed. Engl. 53, 7560\u20137563 (2014).","journal-title":"Angew. Chem. Int Ed. Engl."},{"key":"747_CR20","doi-asserted-by":"publisher","first-page":"6252","DOI":"10.1021\/bi5007833","volume":"53","author":"W Paslawski","year":"2014","unstructured":"Paslawski, W. et al. High stability and cooperative unfolding of cytotoxic \u03b1-synuclein oligomers. Biochemistry 53, 6252\u20136263 (2014).","journal-title":"Biochemistry"},{"key":"747_CR21","doi-asserted-by":"publisher","first-page":"3859","DOI":"10.1021\/ja411577t","volume":"136","author":"N Lorenzen","year":"2014","unstructured":"Lorenzen, N. et al. The role of stable \u03b1-synuclein oligomers in the molecular events underlying amyloid formation. J. Am. Chem. Soc. 136, 3859\u20133868 (2014).","journal-title":"J. Am. Chem. Soc."},{"key":"747_CR22","doi-asserted-by":"publisher","first-page":"7812","DOI":"10.1021\/bi0102398","volume":"40","author":"MJ Volles","year":"2001","unstructured":"Volles, M. J. et al. Vesicle permeabilization by protofibrillar \u03b1-synuclein: implications for the pathogenesis and treatment of Parkinson\u2019s disease. Biochemistry 40, 7812\u20137819 (2001).","journal-title":"Biochemistry"},{"key":"747_CR23","doi-asserted-by":"publisher","first-page":"21299","DOI":"10.1074\/jbc.M114.554667","volume":"289","author":"N Lorenzen","year":"2014","unstructured":"Lorenzen, N. et al. How epigallogatechin gallate can inhibit \u03b1-synuclein oligomer toxicity in vitro. J. Biol. Chem. 289, 21299\u201321310 (2014).","journal-title":"J. Biol. Chem."},{"key":"747_CR24","doi-asserted-by":"publisher","first-page":"9220","DOI":"10.1523\/JNEUROSCI.2617-07.2007","volume":"27","author":"KM Danzer","year":"2007","unstructured":"Danzer, K. M. et al. Different species of \u03b1-synuclein oligomers induce calcium influx and seeding. J. Neurosci. 27, 9220\u20139232 (2007).","journal-title":"J. Neurosci."},{"key":"747_CR25","doi-asserted-by":"publisher","first-page":"3301","DOI":"10.1523\/JNEUROSCI.5368-11.2012","volume":"32","author":"E Colla","year":"2012","unstructured":"Colla, E. et al. Accumulation of toxic \u03b1-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J. Neurosci. 32, 3301\u20133305 (2012).","journal-title":"J. Neurosci."},{"key":"747_CR26","doi-asserted-by":"publisher","first-page":"3306","DOI":"10.1523\/JNEUROSCI.5367-11.2012","volume":"32","author":"E Colla","year":"2012","unstructured":"Colla, E. et al. Endoplasmic reticulum stress is important for the manifestations of \u03b1-synucleinopathy in vivo. J. Neurosci. 32, 3306\u20133320 (2012).","journal-title":"J. Neurosci."},{"key":"747_CR27","doi-asserted-by":"publisher","first-page":"2015","DOI":"10.1016\/j.biocel.2009.05.008","volume":"41","author":"M Parihar","year":"2009","unstructured":"Parihar, M. et al. \u03b1-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells. Int. J. Biochem. Cell Biol. 41, 2015\u20132024 (2009).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"747_CR28","doi-asserted-by":"publisher","first-page":"522","DOI":"10.1111\/jnc.14808","volume":"150","author":"P Alam","year":"2019","unstructured":"Alam, P. et al. \u03b1-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities. J. Neurochem 150, 522\u2013534 (2019).","journal-title":"J. Neurochem"},{"key":"747_CR29","doi-asserted-by":"publisher","first-page":"e0213663","DOI":"10.1371\/journal.pone.0213663","volume":"14","author":"F van Diggelen","year":"2019","unstructured":"van Diggelen, F. et al. Two conformationally distinct \u03b1-synuclein oligomers share common epitopes and the ability to impair long-term potentiation. PLoS One 14, e0213663 (2019).","journal-title":"PLoS One"},{"key":"747_CR30","doi-asserted-by":"publisher","first-page":"2417","DOI":"10.1021\/acs.biochem.3c00114","volume":"62","author":"CB Andersen","year":"2023","unstructured":"Andersen, C. B. et al. 4-Oxo-2-nonenal-Induced \u03b1-Synuclein Oligomers Interact with Membranes in the Cell, Leading to Mitochondrial Fragmentation. Biochemistry 62, 2417\u20132425 (2023).","journal-title":"Biochemistry"},{"key":"747_CR31","doi-asserted-by":"publisher","first-page":"3644","DOI":"10.1021\/acs.biochem.1c00478","volume":"60","author":"C Andersen","year":"2021","unstructured":"Andersen, C. et al. Lipid Peroxidation Products HNE and ONE Promote and Stabilize \u03b1-synuclein Oligomers by Chemical Modifications. Biochemistry 60, 3644\u20133658 (2021).","journal-title":"Biochemistry"},{"key":"747_CR32","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1096\/fj.03-1449com","volume":"20","author":"OMA El-Agnaf","year":"2006","unstructured":"El-Agnaf, O. M. A. et al. Detection of oligomeric forms of \u03b1-synuclein protein in human plasma as a potential biomarker for Parkinson\u2019s disease. FASEB J. 20, 419\u2013425 (2006).","journal-title":"FASEB J."},{"key":"747_CR33","doi-asserted-by":"publisher","first-page":"e0151156","DOI":"10.1371\/journal.pone.0151156","volume":"11","author":"G Vivacqua","year":"2016","unstructured":"Vivacqua, G. et al. Abnormal Salivary Total and Oligomeric \u03b1-synuclein in Parkinson\u2019s Disease. PLOS ONE 11, e0151156 (2016).","journal-title":"PLOS ONE"},{"key":"747_CR34","doi-asserted-by":"publisher","first-page":"1263","DOI":"10.1111\/j.1471-4159.2010.06695.x","volume":"113","author":"A Jang","year":"2010","unstructured":"Jang, A. et al. Non-classical exocytosis of \u03b1-synuclein is sensitive to folding states and promoted under stress conditions. J. Neurochem. 113, 1263\u20131274 (2010).","journal-title":"J. Neurochem."},{"key":"747_CR35","doi-asserted-by":"publisher","first-page":"1835","DOI":"10.1016\/j.biocel.2008.01.017","volume":"40","author":"H-J Lee","year":"2008","unstructured":"Lee, H.-J. et al. Assembly-dependent endocytosis and clearance of extracellular \u03b1-synuclein. Int. J. Biochem. Cell Biol. 40, 1835\u20131849 (2008).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"747_CR36","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1186\/1750-1326-7-42","volume":"7","author":"KM Danzer","year":"2012","unstructured":"Danzer, K. M. et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol. Neurodegen. 7, 42 (2012).","journal-title":"Mol. Neurodegen."},{"key":"747_CR37","doi-asserted-by":"publisher","first-page":"13010","DOI":"10.1073\/pnas.0903691106","volume":"106","author":"P Desplats","year":"2009","unstructured":"Desplats, P. et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of \u03b1-synuclein. Proc. Natl Acad. Sci. 106, 13010\u201313015 (2009).","journal-title":"Proc. Natl Acad. Sci."},{"key":"747_CR38","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-33252-6","volume":"13","author":"D Emin","year":"2022","unstructured":"Emin, D. et al. Small soluble \u03b1-synuclein aggregates are the toxic species in Parkinson\u2019s disease. Nat. Commun. 13, 5512 (2022).","journal-title":"Nat. Commun."},{"key":"747_CR39","doi-asserted-by":"publisher","first-page":"e2213157119","DOI":"10.1073\/pnas.2213157119","volume":"119","author":"D Shea","year":"2022","unstructured":"Shea, D. et al. SOBA: Development and testing of a soluble oligomer binding assay for detection of amyloidogenic toxic oligomers. Proc. Natl Acad. Sci. 119, e2213157119 (2022).","journal-title":"Proc. Natl Acad. Sci."},{"key":"747_CR40","doi-asserted-by":"publisher","first-page":"342559","DOI":"10.1016\/j.aca.2024.342559","volume":"1304","author":"JF Giarola","year":"2024","unstructured":"Giarola, J. F. et al. An \u03b1-helical peptide-based plasmonic biosensor for highly specific detection of \u03b1-synuclein toxic oligomers. Anal. Chim. Acta 1304, 342559 (2024).","journal-title":"Anal. Chim. Acta"},{"key":"747_CR41","doi-asserted-by":"publisher","first-page":"2164459","DOI":"10.1080\/19420862.2022.2164459","volume":"15","author":"H Svilenov","year":"2023","unstructured":"Svilenov, H. et al. Approaches to expand the conventional toolbox for discovery and selection of antibodies with drug-like physicochemical properties. mAbs 15, 2164459 (2023).","journal-title":"mAbs"},{"key":"747_CR42","doi-asserted-by":"publisher","first-page":"1131","DOI":"10.3390\/biom11081131","volume":"11","author":"E Ruiz-L\u00f3pez","year":"2021","unstructured":"Ruiz-L\u00f3pez, E. et al. Transportation of single-domain antibodies through the blood\u2013brain barrier. Biomolecules 11, 1131 (2021).","journal-title":"Biomolecules"},{"key":"747_CR43","doi-asserted-by":"publisher","first-page":"105086","DOI":"10.1016\/j.nbd.2020.105086","volume":"146","author":"ST Kumar","year":"2020","unstructured":"Kumar, S. T. et al. How specific are the conformation-specific \u03b1-synuclein antibodies? Characterization and validation of 16 \u03b1-synuclein conformation-specific antibodies using well-characterized preparations of \u03b1-synuclein monomers, fibrils and oligomers with distinct structures and morphology. Neurobiol. Dis. 146, 105086 (2020).","journal-title":"Neurobiol. Dis."},{"key":"747_CR44","doi-asserted-by":"publisher","first-page":"134899","DOI":"10.1016\/j.neulet.2020.134899","volume":"725","author":"M Fayyad","year":"2020","unstructured":"Fayyad, M. et al. Generation of monoclonal antibodies against phosphorylated \u03b1-synuclein at serine 129: Research tools for synucleinopathies. Neurosci. Lett. 725, 134899 (2020).","journal-title":"Neurosci. Lett."},{"key":"747_CR45","first-page":"879","volume":"152","author":"M Baba","year":"1998","unstructured":"Baba, M. et al. Aggregation of \u03b1-synuclein in Lewy bodies of sporadic Parkinson\u2019s disease and dementia with Lewy bodies. Am. J. Pathol. 152, 879\u2013884 (1998).","journal-title":"Am. J. Pathol."},{"key":"747_CR46","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.nbd.2015.04.009","volume":"79","author":"NN Vaikath","year":"2015","unstructured":"Vaikath, N. N. et al. Generation and characterization of novel conformation-specific monoclonal antibodies for \u03b1-synuclein pathology. Neurobiol. Dis. 79, 81\u201399 (2015).","journal-title":"Neurobiol. Dis."},{"key":"747_CR47","unstructured":"J. Santos et al., The structural architecture of an \u03b1-synuclein toxic oligomer, bioRxiv, 2023.2002.2010.527650. (2023)."},{"key":"747_CR48","doi-asserted-by":"publisher","first-page":"140943","DOI":"10.1016\/j.bbapap.2023.140943","volume":"1872","author":"DE Otzen","year":"2024","unstructured":"Otzen, D. E. Antibodies and \u03b1-synuclein: What to target against Parkinson\u2019s Disease? Biochim. Biophys. Acta Proteins Proteom. 1872, 140943 (2024).","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"747_CR49","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/s42003-022-03059-8","volume":"5","author":"A Farzadfard","year":"2022","unstructured":"Farzadfard, A. et al. The C-terminal tail of \u03b1-synuclein protects against aggregate replication but is critical for oligomerization. Commun. Biol. 5, 123 (2022).","journal-title":"Commun. Biol."},{"key":"747_CR50","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1186\/s12951-016-0181-1","volume":"14","author":"S Thrane","year":"2016","unstructured":"Thrane, S. et al. Bacterial superglue enables easy development of efficient virus-like particle based vaccines. J. Nanobiotechnol. 14, 30 (2016).","journal-title":"J. Nanobiotechnol."},{"key":"747_CR51","doi-asserted-by":"publisher","first-page":"E690","DOI":"10.1073\/pnas.1115485109","volume":"109","author":"B Zakeri","year":"2012","unstructured":"Zakeri, B. et al. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc. Natl Acad. Sci. USA 109, E690\u2013E697 (2012).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"747_CR52","doi-asserted-by":"publisher","first-page":"e14745","DOI":"10.15252\/emmm.202114745","volume":"13","author":"M Emmenegger","year":"2021","unstructured":"Emmenegger, M. et al. LAG3 is not expressed in human and murine neurons and does not modulate \u03b1-synucleinopathies. EMBO Mol. Med. 13, e14745 (2021).","journal-title":"EMBO Mol. Med."},{"key":"747_CR53","doi-asserted-by":"publisher","first-page":"115196","DOI":"10.1016\/j.bios.2023.115196","volume":"228","author":"MM Schneider","year":"2023","unstructured":"Schneider, M. M. et al. Microfluidic antibody affinity profiling of alloantibody-HLA interactions in human serum. Biosens. Bioelectron. 228, 115196 (2023).","journal-title":"Biosens. Bioelectron."},{"key":"747_CR54","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1186\/s40478-022-01468-8","volume":"10","author":"MF Altay","year":"2022","unstructured":"Altay, M. F. et al. Prominent astrocytic \u03b1-synuclein pathology with unique post-translational modification signatures unveiled across Lewy body disorders. Acta Neuropathol. Commun. 10, 163 (2022).","journal-title":"Acta Neuropathol. Commun."},{"key":"747_CR55","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.sbi.2021.02.006","volume":"70","author":"DE Otzen","year":"2021","unstructured":"Otzen, D. E. et al. Microfluidics and the quantification of biomolecular interactions. Curr. Opin. Struct. Biol. 70, 8\u201315 (2021).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"747_CR56","doi-asserted-by":"publisher","first-page":"14733","DOI":"10.1074\/jbc.M413024200","volume":"280","author":"MM Dedmon","year":"2005","unstructured":"Dedmon, M. M. et al. Heat shock protein 70 inhibits \u03b1-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280, 14733\u201314740 (2005).","journal-title":"J. Biol. Chem."},{"key":"747_CR57","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1039\/C3AN01616A","volume":"139","author":"P Lopes","year":"2014","unstructured":"Lopes, P. et al. Electrochemical analysis of the fibrillation of Parkinson\u2019s disease \u03b1-synuclein. Analyst 139, 749\u2013756 (2014).","journal-title":"Analyst"},{"key":"747_CR58","doi-asserted-by":"publisher","first-page":"43179","DOI":"10.1074\/jbc.M507624200","volume":"280","author":"TS Ulmer","year":"2005","unstructured":"Ulmer, T. S. et al. Comparison of structure and dynamics of micelle-bound human \u03b1-synuclein and Parkinson disease variants. J. Biol. Chem. 280, 43179\u201343187 (2005).","journal-title":"J. Biol. Chem."},{"key":"747_CR59","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-25966-w","volume":"12","author":"MM Schneider","year":"2021","unstructured":"Schneider, M. M. et al. The Hsc70 disaggregation machinery removes monomer units directly from \u03b1-synuclein fibril ends. Nat. Commun. 12, 5999 (2021).","journal-title":"Nat. Commun."},{"key":"747_CR60","doi-asserted-by":"publisher","first-page":"e0196056","DOI":"10.1371\/journal.pone.0196056","volume":"13","author":"L Lassen","year":"2018","unstructured":"Lassen, L. et al. ELISA method to detect \u03b1-synuclein oligomers in cell and animal models. PLOS ONE 13, e0196056 (2018).","journal-title":"PLOS ONE"},{"key":"747_CR61","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-017-06724-9","volume":"7","author":"J-A Phan","year":"2017","unstructured":"Phan, J.-A. et al. Early synaptic dysfunction induced by \u03b1-synuclein in a rat model of Parkinson\u2019s disease. Sci. Rep. 7, 6363 (2017).","journal-title":"Sci. Rep."},{"key":"747_CR62","doi-asserted-by":"publisher","first-page":"105229","DOI":"10.1016\/j.nbd.2020.105229","volume":"149","author":"MB Thomsen","year":"2021","unstructured":"Thomsen, M. B. et al. PET imaging reveals early and progressive dopaminergic deficits after intra-striatal injection of preformed alpha-synuclein fibrils in rats. Neurobiol. Dis. 149, 105229 (2021).","journal-title":"Neurobiol. Dis."},{"key":"747_CR63","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1016\/S0197-4580(02)00065-9","volume":"24","author":"H Braak","year":"2003","unstructured":"Braak, H. et al. Staging of brain pathology related to sporadic Parkinson\u2019s disease. Neurobiol. Aging 24, 197\u2013211 (2003).","journal-title":"Neurobiol. Aging"},{"key":"747_CR64","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1007\/s00401-021-02329-9","volume":"142","author":"T Moors","year":"2021","unstructured":"Moors, T. et al. The subcellular arrangement of alpha-synuclein proteoforms in the Parkinson\u2019s disease brain as revealed by multicolor STED microscopy. Acta Neuropathol. 142, 423\u2013448 (2021).","journal-title":"Acta Neuropathol."},{"key":"747_CR65","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1038\/s41531-023-00604-y","volume":"9","author":"MF Altay","year":"2023","unstructured":"Altay, M. F. et al. Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases. NPJ Parkinsons Dis. 9, 161 (2023).","journal-title":"NPJ Parkinsons Dis."},{"key":"747_CR66","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1007\/PL00007400","volume":"99","author":"K Wakabayashi","year":"2000","unstructured":"Wakabayashi, K. et al. NACP\/\u03b1-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson\u2019s disease brains. Acta Neuropathol. 99, 14\u201320 (2000).","journal-title":"Acta Neuropathol."},{"key":"747_CR67","doi-asserted-by":"publisher","first-page":"2168","DOI":"10.3390\/biomedicines10092168","volume":"10","author":"E Gibbs","year":"2022","unstructured":"Gibbs, E. et al. Rational Generation of Monoclonal Antibodies Selective for Pathogenic Forms of \u03b1-synuclein. Biomedicines 10, 2168 (2022).","journal-title":"Biomedicines"},{"key":"747_CR68","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.bpc.2016.11.002","volume":"220","author":"C Sahin","year":"2017","unstructured":"Sahin, C. et al. Antibodies against the C-terminus of \u03b1-synuclein modulate its fibrillation. Biophys. Chem. 220, 34\u201341 (2017).","journal-title":"Biophys. Chem."},{"key":"747_CR69","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.1038\/s41589-021-00832-4","volume":"17","author":"A Wellner","year":"2021","unstructured":"Wellner, A. et al. Rapid generation of potent antibodies by autonomous hypermutation in yeast. Nat. Chem. Biol. 17, 1057\u20131064 (2021).","journal-title":"Nat. Chem. Biol."},{"key":"747_CR70","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms10759","volume":"7","author":"D Sehlin","year":"2016","unstructured":"Sehlin, D. et al. Antibody-based PET imaging of amyloid beta in mouse models of Alzheimer\u2019s disease. Nat. Commun. 7, 10759 (2016).","journal-title":"Nat. Commun."},{"key":"747_CR71","doi-asserted-by":"publisher","first-page":"1298","DOI":"10.1001\/jama.2024.0792","volume":"331","author":"CH Gibbons","year":"2024","unstructured":"Gibbons, C. H. et al. Skin Biopsy Detection of Phosphorylated \u03b1-Synuclein in Patients With Synucleinopathies. JAMA 331, 1298\u20131306 (2024).","journal-title":"JAMA"},{"key":"747_CR72","doi-asserted-by":"publisher","first-page":"1263","DOI":"10.3390\/biom13081263","volume":"13","author":"F Jim\u00e9nez-Jim\u00e9nez","year":"2023","unstructured":"Jim\u00e9nez-Jim\u00e9nez, F. et al. Alpha-Synuclein in Peripheral Tissues as a Possible Marker for Neurological Diseases and Other Medical Conditions. Biomolecules 13, 1263 (2023).","journal-title":"Biomolecules"},{"key":"747_CR73","doi-asserted-by":"publisher","first-page":"5613","DOI":"10.1007\/s00415-023-11893-x","volume":"270","author":"F Angius","year":"2023","unstructured":"Angius, F. et al. Combined measure of salivary alpha-synuclein species as diagnostic biomarker for Parkinson\u2019s disease. J. Neurol. 270, 5613\u20135621 (2023).","journal-title":"J. Neurol."},{"key":"747_CR74","doi-asserted-by":"publisher","first-page":"13454","DOI":"10.1523\/JNEUROSCI.1292-12.2012","volume":"32","author":"E-J Bae","year":"2012","unstructured":"Bae, E.-J. et al. Antibody-Aided Clearance of Extracellular \u03b1-Synuclein Prevents Cell-to-Cell Aggregate Transmission. J. Neurosci. 32, 13454 (2012).","journal-title":"J. Neurosci."},{"key":"747_CR75","doi-asserted-by":"publisher","first-page":"1489","DOI":"10.1007\/s13311-022-01288-7","volume":"19","author":"L Knecht","year":"2022","unstructured":"Knecht, L. et al. Alpha-synuclein Immunization Strategies for Synucleinopathies in Clinical Studies: A Biological Perspective. Neurotherapeutics 19, 1489\u20131502 (2022).","journal-title":"Neurotherapeutics"},{"key":"747_CR76","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1186\/s40478-022-01440-6","volume":"10","author":"H Sekiya","year":"2022","unstructured":"Sekiya, H. et al. Discrepancy between distribution of \u03b1-synuclein oligomers and Lewy-related pathology in Parkinson\u2019s disease. Acta Neuropathol. Commun. 10, 133 (2022).","journal-title":"Acta Neuropathol. Commun."},{"key":"747_CR77","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1007\/s00401-019-01961-w","volume":"137","author":"H Sekiya","year":"2019","unstructured":"Sekiya, H. et al. Wide distribution of \u03b1-synuclein oligomers in multiple system atrophy brain detected by proximity ligation. Acta Neuropathol. 137, 455\u2013466 (2019).","journal-title":"Acta Neuropathol."},{"key":"747_CR78","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1002\/mds.28984","volume":"37","author":"OM Alzghool","year":"2022","unstructured":"Alzghool, O. M. et al. \u03b1-Synuclein Radiotracer development and in vivo imaging: recent advancements and new perspectives. Mov. Disord. 37, 936\u2013948 (2022).","journal-title":"Mov. Disord."},{"key":"747_CR79","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1007\/s11307-013-0634-y","volume":"15","author":"K Neal","year":"2013","unstructured":"Neal, K. et al. Development and screening of contrast agents for in vivo imaging of Parkinson\u2019s disease. Mol. Imaging Biol. 15, 585\u2013595 (2013).","journal-title":"Mol. Imaging Biol."},{"key":"747_CR80","doi-asserted-by":"publisher","first-page":"13815","DOI":"10.1039\/D2SC00066K","volume":"13","author":"K Kulenkampff","year":"2022","unstructured":"Kulenkampff, K. et al. An antibody scanning method for the detection of \u03b1-synuclein oligomers in the serum of Parkinson\u2019s disease patients. Chem. Sci. 13, 13815\u201313828 (2022).","journal-title":"Chem. Sci."},{"key":"747_CR81","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","volume":"41","author":"F Studier","year":"2005","unstructured":"Studier, F. William Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 41, 207\u2013234 (2005).","journal-title":"Protein Expr. Purif."},{"key":"747_CR82","doi-asserted-by":"publisher","first-page":"167855","DOI":"10.1016\/j.jmb.2022.167855","volume":"434","author":"AL Gronnemose","year":"2022","unstructured":"Gronnemose, A. L. et al. EGCG has dual and opposing effects on the N-terminal region of self-associating \u03b1-synuclein Oligomers. J. Mol. Biol. 434, 167855 (2022).","journal-title":"J. Mol. Biol."},{"key":"747_CR83","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/0022-1759(90)90029-U","volume":"132","author":"Y Aida","year":"1990","unstructured":"Aida, Y. et al. Removal of endotoxin from protein solutions by phase separation using triton X-114. J. Immunol. Methods 132, 191\u2013195 (1990).","journal-title":"J. Immunol. Methods"},{"key":"747_CR84","doi-asserted-by":"publisher","first-page":"168194","DOI":"10.1016\/j.jmb.2023.168194","volume":"435","author":"H\u00d8 Rasmussen","year":"2023","unstructured":"Rasmussen, H. \u00d8. et al. Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation. J. Mol. Biol. 435, 168194 (2023).","journal-title":"J. Mol. Biol."},{"key":"747_CR85","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-021-84113-z","volume":"11","author":"ME Pedersen","year":"2021","unstructured":"Pedersen, M. E. et al. Size-based characterization of adalimumab and TNF-\u03b1 interactions using flow induced dispersion analysis: assessment of avidity-stabilized multiple bound species. Sci. Rep. 11, 4754 (2021).","journal-title":"Sci. Rep."},{"key":"747_CR86","doi-asserted-by":"publisher","first-page":"4975","DOI":"10.1021\/acs.analchem.9b00537","volume":"91","author":"ME Pedersen","year":"2019","unstructured":"Pedersen, M. E. et al. Protein characterization in 3D: Size, folding, and functional assessment in a unified approach. Anal. Chem. 91, 4975\u20134979 (2019).","journal-title":"Anal. Chem."},{"key":"747_CR87","doi-asserted-by":"publisher","first-page":"1069","DOI":"10.1002\/qsar.200640130","volume":"25","author":"A Dikmans","year":"2006","unstructured":"Dikmans, A. et al. SC2: A novel process for manufacturing multipurpose high-density chemical microarrays. QSAR Comb. Sci. 25, 1069\u20131080 (2006).","journal-title":"QSAR Comb. Sci."},{"key":"747_CR88","doi-asserted-by":"crossref","unstructured":"M\u00fcller, T. et al. Particle-based Monte-Carlo simulations of steady-state mass transport at intermediate P\u00e9clet numbers. Int. J. Nonlinear Sci. Numer. Simul. 17, 175\u2013183 (2016).","DOI":"10.1515\/ijnsns-2015-0056"},{"key":"747_CR89","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1016\/j.ab.2010.02.001","volume":"400","author":"L Giehm","year":"2010","unstructured":"Giehm, L. et al. Strategies to increase the reproducibility of \u03b1-synuclein fibrillation in plate reader assays. Anal. Biochem. 400, 270\u2013281 (2010).","journal-title":"Anal. Biochem."},{"key":"747_CR90","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1007\/978-1-4939-2978-8_9","volume":"1345","author":"W Paslawski","year":"2016","unstructured":"Paslawski, W. et al. Formation and characterization of \u03b1-synuclein oligomers. Methods Mol. Biol. 1345, 133\u2013150 (2016).","journal-title":"Methods Mol. Biol."},{"key":"747_CR91","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1016\/S0896-6273(02)00682-7","volume":"34","author":"B Giasson","year":"2002","unstructured":"Giasson, B. et al. Neuronal \u03b1-Synucleinopathy with severe movement disorder in mice expressing A53T Human \u03b1-Synuclein. Neuron 34, 521\u2013533 (2002).","journal-title":"Neuron"},{"key":"747_CR92","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1111\/bpa.12883","volume":"31","author":"L Reimer","year":"2021","unstructured":"Reimer, L. et al. PKR kinase directly regulates tau expression and Alzheimer\u2019s disease-related tau phosphorylation. Brain Pathol. 31, 103\u2013119 (2021).","journal-title":"Brain Pathol."}],"container-title":["npj Parkinson's Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41531-024-00747-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41531-024-00747-6","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41531-024-00747-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T05:05:23Z","timestamp":1722229523000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41531-024-00747-6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,7,29]]},"references-count":92,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["747"],"URL":"https:\/\/doi.org\/10.1038\/s41531-024-00747-6","relation":{"has-preprint":[{"id-type":"doi","id":"10.21203\/rs.3.rs-3778118\/v1","asserted-by":"object"}]},"ISSN":["2373-8057"],"issn-type":[{"value":"2373-8057","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,7,29]]},"assertion":[{"value":"19 December 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 July 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 July 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The Authors declare no Competing Financial Interests. MRR is Associate Editor of npj Parkinson\u2019s Disease. MRR was not involved in the journal\u2019s review of, or decisions related to, this manuscript. The remaining authors declare no competing financial or non-financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"139"}}