{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T17:14:40Z","timestamp":1788455680753,"version":"build-2803163510"},"reference-count":64,"publisher":"American Chemical Society (ACS)","issue":"34","license":[{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM151251"],"award-info":[{"award-number":["R35GM151251"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Intrinsically disordered proteins (IDPs) drive many neurodegenerative disorders, but their structures remain difficult to define because they populate dynamic ensembles that change with the chemical environment. This problem is central for \u03b1-synuclein (aSyn), a Parkinson\u2019s disease-linked IDP in which S129 phosphorylation is highly enriched in disease-associated aggregates. Although S129 phosphorylation stabilizes a more compact aSyn ensemble in dilute solution, whether this structural effect persists across other biochemical environments has remained unknown. Here, we developed a quantitative cross-linking mass spectrometry framework to determine how WT and pS129 aSyn respond to chemically distinct environments. We compared dilute buffer with two perturbations relevant to aSyn biology: trimethylamine N-oxide (TMAO), a gut-microbiome-derived metabolite associated with Parkinson\u2019s disease that can also act as a compacting osmolyte at high concentration, and octyl glucoside (OG) micelles, which provide a membrane-mimetic surface. TMAO rewired the phosphorylation-dependent structural response in a concentration-dependent manner: 1.8 M TMAO shifted WT aSyn toward the dilute pS129 contact pattern by increasing long-range contacts between the N-terminal and C-terminal regions, whereas 3.4 M TMAO collapsed both proteoforms and reduced their structural differences. In OG micelles, the proteoforms diverged. WT favored an extended-helix-like contact pattern with stronger contacts between the C-terminal tail and micelle-bound N-terminal region, whereas pS129 favored contacts between the N-terminal and NAC regions and fewer contacts to the C-terminal tail, consistent with a broken-helix-like topology. By integrating regional contact counts, normalized cross-link intensities, and geometric compatibility analysis, this workflow distinguishes broad contact accessibility from the residue-level contacts that dominate each condition. These results establish a proteoform-by-environment model for IDP structure, in which phosphorylation effects are not fixed but are rewritten by the surrounding chemical environment.<\/jats:p>","DOI":"10.1021\/jacs.6c10987","type":"journal-article","created":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T09:57:36Z","timestamp":1787392656000},"page":"37102-37109","source":"Crossref","is-referenced-by-count":0,"title":["Proteoform-Resolved\nCross-Linking Reveals Environment-Dependent\nStructural Effects of \u03b1-Synuclein S129 Phosphorylation"],"prefix":"10.1021","volume":"148","author":[{"given":"Ashlyn N.","family":"Dollar","sequence":"first","affiliation":[{"name":"Indiana University Indianapolis , , , ,","place":["Indianapolis, Indiana, United States, 46202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel W.","family":"Kelley","sequence":"additional","affiliation":[{"name":"Indiana University Indianapolis , , , ,","place":["Indianapolis, Indiana, United States, 46202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7223-8729","authenticated-orcid":true,"given":"Ian K.","family":"Webb","sequence":"additional","affiliation":[{"name":"Indiana University Indianapolis , , , ,","place":["Indianapolis, Indiana, United States, 46202"]},{"name":"Indiana University School of Medicine , , , ,","place":["Indianapolis, Indiana, United States, 46202"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,21]]},"reference":[{"key":"2026090312080723100_cit1","first-page":"1","article-title":"Protein intrinsic\ndisorder and structure-function continuum","volume-title":"Progress in Molecular Biology and Translational Science","author":"Uversky","year":"2019"},{"issue":"1","key":"2026090312080723100_cit2","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1186\/s12964-021-00774-3","article-title":"On the roles of intrinsically disordered\nproteins and regions in cell communication and signaling","volume":"19","author":"Bondos","year":"2021","journal-title":"Cell Commun. Signal."},{"issue":"22","key":"2026090312080723100_cit3","doi-asserted-by":"publisher","first-page":"14050","DOI":"10.3390\/ijms232214050","article-title":"Intrinsically Disordered Proteins:\nAn Overview","volume":"23","author":"Trivedi","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"5","key":"2026090312080723100_cit4","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1111\/jnc.14810","article-title":"The physiological\nrole of \u03b1-synuclein and its\nrelationship to Parkinson\u2019s Disease","volume":"150","author":"Sulzer","year":"2019","journal-title":"J. Neurochem."},{"issue":"3","key":"2026090312080723100_cit5","doi-asserted-by":"publisher","first-page":"176","DOI":"10.1038\/s41419-023-05672-9","article-title":"Alpha-synuclein in Parkinson\u2019s\ndisease and other synucleinopathies: from overt neurodegeneration\nback to early synaptic dysfunction","volume":"14","author":"Calabresi","year":"2023","journal-title":"Cell Death\nDis."},{"issue":"2","key":"2026090312080723100_cit6","doi-asserted-by":"publisher","first-page":"a009399","DOI":"10.1101\/cshperspect.a009399","article-title":"\u03b1- Synuclein\nin Parkinson\u2019s disease","volume":"2","author":"Stefanis","year":"2012","journal-title":"Cold Spring Harbor\nPesrpect. Med."},{"issue":"40","key":"2026090312080723100_cit7","doi-asserted-by":"publisher","first-page":"E4274","DOI":"10.1073\/pnas.1416598111","article-title":"\u03b1-Synuclein assembles into\nhigher-order multimers upon membrane binding to promote SNARE complex\nformation","volume":"111","author":"Burre\u0301","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090312080723100_cit8","doi-asserted-by":"publisher","first-page":"29","DOI":"10.4103\/1735-1995.181989","article-title":"Alpha-synuclein\nstructure, functions, and interactions","volume":"21","author":"Emamzadeh","year":"2016","journal-title":"J. Res.\nMed. Sci."},{"issue":"6","key":"2026090312080723100_cit9","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1021\/acschemneuro.9b00527","article-title":"Role of \u03b1-Synuclein Regions\nin Nucleation and Elongation of Amyloid Fiber Assembly","volume":"11","author":"Gallardo","year":"2020","journal-title":"ACS Chem. Neurosci."},{"issue":"11","key":"2026090312080723100_cit10","doi-asserted-by":"publisher","first-page":"6216","DOI":"10.3390\/ijms23116216","article-title":"Pathogenic Impact of \u03b1-Synuclein\nPhosphorylation and Its Kinases in \u03b1-Synucleinopathies","volume":"23","author":"Kawahata","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"2","key":"2026090312080723100_cit11","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1515\/revneuro-2012-0071","article-title":"The role of Ser129 phosphorylation\nof \u03b1-synuclein in neurodegeneration of Parkinson\u2019s disease:\na review of in vivo models","volume":"24","author":"Sato","year":"2013","journal-title":"Rev. Neurosci."},{"issue":"2","key":"2026090312080723100_cit12","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/ncb748","article-title":"\u03b1-Synuclein is phosphorylated in synucleinopathy\nlesions","volume":"4","author":"Fujiwara","year":"2002","journal-title":"Nat. Cell Biol."},{"issue":"1","key":"2026090312080723100_cit13","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1038\/s41531-023-00444-w","article-title":"Dynamic\nphysiological\n\u03b1-synuclein S129 phosphorylation is driven by neuronal activity","volume":"9","author":"Ramalingam","year":"2023","journal-title":"npj Parkinson's Disease"},{"issue":"7","key":"2026090312080723100_cit14","doi-asserted-by":"publisher","first-page":"480","DOI":"10.1016\/j.tins.2024.05.005","article-title":"Physiological roles\nof \u03b1-synuclein\nserine-129 phosphorylation - not an oxymoron","volume":"47","author":"Ramalingam","year":"2024","journal-title":"Trends Neurosci."},{"key":"2026090312080723100_cit15","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2021.105291","article-title":"In vivo\naggregation of presynaptic alpha-synuclein\nis not influenced by its phosphorylation at serine-129","volume":"152","author":"Weston","year":"2021","journal-title":"Neurobiology of Disease"},{"issue":"10","key":"2026090312080723100_cit16","doi-asserted-by":"publisher","first-page":"7098","DOI":"10.1074\/jbc.M111.237131","article-title":"Phosphorylation\nof \u03b1-Synuclein Protein at Ser-129 Reduces Neuronal Dysfunction\nby Lowering Its Membrane Binding Property in Caenorhabditis elegans","volume":"287","author":"Kuwahara","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"2","key":"2026090312080723100_cit17","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1002\/jnr.22537","article-title":"Characterization of kinases involved in the phosphorylation\nof aggregated \u03b1-synuclein","volume":"89","author":"Waxman","year":"2011","journal-title":"J. Neurosci.\nRes."},{"issue":"24","key":"2026090312080723100_cit18","doi-asserted-by":"publisher","first-page":"16895","DOI":"10.1074\/jbc.M800747200","article-title":"Phosphorylation at Ser-129\nbut Not the Phosphomimics S129E\/D Inhibits the Fibrillation of \u03b1-Synuclein","volume":"283","author":"Paleologou","year":"2008","journal-title":"J. Biol. Chem."},{"issue":"5","key":"2026090312080723100_cit19","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1038\/nn1443","article-title":"\u03b1-Synuclein\nphosphorylation controls neurotoxicity\nand inclusion formation in a Drosophila model of Parkinson disease","volume":"8","author":"Chen","year":"2005","journal-title":"Nat. Neurosci."},{"issue":"1","key":"2026090312080723100_cit20","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1016\/j.acthis.2009.07.007","article-title":"Phosphorylation of \u03b1-synuclein\nupregulates tyrosine hydroxylase activity in MN9D cells","volume":"113","author":"Wu","year":"2011","journal-title":"Acta Histochemica"},{"issue":"2","key":"2026090312080723100_cit21","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1073\/pnas.0711053105","article-title":"The phosphorylation\nstate of Ser-129 in human \u03b1-synuclein determines neurodegeneration\nin a rat model of Parkinson disease","volume":"105","author":"Gorbatyuk","year":"2008","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"36","key":"2026090312080723100_cit22","doi-asserted-by":"publisher","first-page":"9227","DOI":"10.1523\/JNEUROSCI.0341-06.2006","article-title":"The Role of G-Protein-Coupled Receptor Kinase\n5 in Pathogenesis of Sporadic Parkinson\u2019s Disease","volume":"26","author":"Arawaka","year":"2006","journal-title":"J. Neurosci."},{"issue":"9","key":"2026090312080723100_cit23","doi-asserted-by":"publisher","first-page":"1421","DOI":"10.1016\/j.neurobiolaging.2006.06.013","article-title":"Age-dependent\ncognitive\ndecline and amygdala pathology in \u03b1-synuclein transgenic mice","volume":"28","author":"Freichel","year":"2007","journal-title":"Neurobiol. Aging"},{"issue":"6","key":"2026090312080723100_cit24","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1093\/embo-reports\/kvf109","article-title":"Hyperphosphorylation\nand insolubility of \u03b1-synuclein in transgenic mouse oligodendrocytes","volume":"3","author":"Kahle","year":"2002","journal-title":"EMBO Reports"},{"issue":"47","key":"2026090312080723100_cit25","doi-asserted-by":"publisher","first-page":"20051","DOI":"10.1073\/pnas.0908005106","article-title":"Exogenous \u03b1-synuclein\nfibrils seed the formation of Lewy body-like intracellular inclusions\nin cultured cells","volume":"106","author":"Luk","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"1","key":"2026090312080723100_cit26","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.neuron.2011.08.033","article-title":"Exogenous \u03b1-Synuclein Fibrils Induce Lewy Body\nPathology Leading to Synaptic Dysfunction and Neuron Death","volume":"72","author":"Volpicelli-Daley","year":"2011","journal-title":"Neuron"},{"issue":"21","key":"2026090312080723100_cit27","doi-asserted-by":"publisher","first-page":"8215","DOI":"10.1021\/acs.jcim.4c01172","article-title":"Impact of Phosphorylation\non the Physiological Form of Human alpha-Synuclein in Aqueous Solution","volume":"64","author":"de Bruyn","year":"2024","journal-title":"J. Chem. Inf. Model."},{"issue":"1","key":"2026090312080723100_cit28","doi-asserted-by":"publisher","DOI":"10.1038\/srep37130","article-title":"Phosphorylation\ninduces distinct alpha-synuclein strain formation","volume":"6","author":"Ma","year":"2016","journal-title":"Sci. Rep."},{"issue":"24","key":"2026090312080723100_cit29","doi-asserted-by":"publisher","first-page":"4006","DOI":"10.1016\/j.neuron.2023.11.020","article-title":"Serine-129 phosphorylation\nof \u03b1-synuclein is an activity-dependent trigger for physiologic\nprotein-protein interactions and synaptic function","volume":"111","author":"Parra-Rivas","year":"2023","journal-title":"Neuron"},{"issue":"2","key":"2026090312080723100_cit30","doi-asserted-by":"publisher","first-page":"101552","DOI":"10.1016\/j.jbc.2021.101552","article-title":"Phosphorylation\nof the aggregate-forming\nprotein alpha-synuclein on serine-129 inhibits its DNA-bending properties","volume":"298","author":"Dent","year":"2022","journal-title":"J. Biol. Chem."},{"key":"2026090312080723100_cit31","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpc.2024.107196","article-title":"Alpha-synuclein\nphosphorylation induces amyloid conversion via enhanced electrostatic\nbridging: Insights from molecular modeling of the full-length protein","volume":"307","author":"Semenyuk","year":"2024","journal-title":"Biophys. Chem."},{"issue":"4","key":"2026090312080723100_cit32","doi-asserted-by":"publisher","first-page":"2765","DOI":"10.1021\/acs.analchem.5c05078","article-title":"Cross-Linking and Covalent Labeling\nMass Spectrometry\nReveal Proteoform-Driven Conformational Changes in Alpha Synuclein","volume":"98","author":"Dollar","year":"2026","journal-title":"Anal. Chem."},{"issue":"7588","key":"2026090312080723100_cit33","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1038\/nature16531","article-title":"Structural\ndisorder\nof monomeric \u03b1-synuclein persists in mammalian cells","volume":"530","author":"Theillet","year":"2016","journal-title":"Nature"},{"issue":"5","key":"2026090312080723100_cit34","doi-asserted-by":"publisher","first-page":"1998","DOI":"10.1111\/j.1471-4159.2008.05510.x","article-title":"Volume-dependent\nosmolyte efflux from neural tissues: regulation by G-protein-coupled\nreceptors","volume":"106","author":"Fisher","year":"2008","journal-title":"J. Neurochem."},{"issue":"32","key":"2026090312080723100_cit35","doi-asserted-by":"publisher","first-page":"18977","DOI":"10.1073\/pnas.2006291117","article-title":"Unroofing site-specific\n\u03b1-synuclein-lipid interactions\nat the plasma membrane","volume":"117","author":"Kaur","year":"2020","journal-title":"Proc. Natl. Acad. Sci.\nU.S.A."},{"issue":"23","key":"2026090312080723100_cit36","doi-asserted-by":"publisher","first-page":"7364","DOI":"10.1021\/ja078326w","article-title":"Effects of trimethylamine N-oxide\n(TMAO) and crowding agents on the stability of RNA hairpins","volume":"130","author":"Pincus","year":"2008","journal-title":"J. Am. Chem. Soc."},{"issue":"23","key":"2026090312080723100_cit37","doi-asserted-by":"publisher","first-page":"8476","DOI":"10.1073\/pnas.1403224111","article-title":"Microscopic\ninsights into the protein-stabilizing\neffect of trimethylamine N-oxide (TMAO)","volume":"111","author":"Ma","year":"2014","journal-title":"Proc.\nNatl. Acad. Sci. U.S.A."},{"issue":"15","key":"2026090312080723100_cit38","doi-asserted-by":"publisher","DOI":"10.1063\/5.0045492","article-title":"Smaller molecules\ncrowd better: Crowder size dependence revealed by single-molecule\nFRET studies and depletion force modeling analysis","volume":"154","author":"Sung","year":"2021","journal-title":"J. Chem. Phys."},{"issue":"13","key":"2026090312080723100_cit39","doi-asserted-by":"publisher","first-page":"2546","DOI":"10.1021\/acs.jpclett.5b00957","article-title":"Biomolecular Crowding Arising from\nSmall Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement","volume":"6","author":"Hilaire","year":"2015","journal-title":"J. Phys. Chem. Lett."},{"issue":"1","key":"2026090312080723100_cit40","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1038\/s41531-024-00816-w","article-title":"\u03b1-synuclein overexpression\nand the microbiome\nshape the gut and brain metabolome in mice","volume":"10","author":"Morais","year":"2024","journal-title":"npj Parkinson's Disease"},{"issue":"1","key":"2026090312080723100_cit41","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1038\/s41392-024-01743-1","article-title":"Microbiota\u2013gut\u2013brain\naxis and its therapeutic\napplications in neurodegenerative diseases","volume":"9","author":"Loh","year":"2024","journal-title":"Signal Transduction and Targeted Therapy"},{"issue":"11","key":"2026090312080723100_cit42","doi-asserted-by":"publisher","first-page":"2115","DOI":"10.1002\/mds.28246","article-title":"The Gut Metabolite\nTrimethylamine N-oxide Is Associated With Parkinson\u2019s Disease\nSeverity and Progression","volume":"35","author":"Chen","year":"2020","journal-title":"Movement Disorders"},{"key":"2026090312080723100_cit43","doi-asserted-by":"publisher","DOI":"10.1016\/j.nut.2020.111090","article-title":"Gut microbiota-derived\nmetabolite trimethylamine N-oxide\nas a biomarker in early Parkinson\u2019s disease","volume":"83","author":"Chung","year":"2021","journal-title":"Nutrition"},{"issue":"1","key":"2026090312080723100_cit44","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1016\/S0014-5793(01)03121-0","article-title":"Trimethylamine-N-oxide-induced\nfolding of alpha-synuclein","volume":"509","author":"Uversky","year":"2001","journal-title":"FEBS Lett."},{"key":"2026090312080723100_cit45","doi-asserted-by":"publisher","first-page":"684","DOI":"10.3389\/fnins.2017.00684","article-title":"Conformational\nEnsembles of \u03b1-Synuclein Derived Peptide with Different Osmolytes\nfrom Temperature Replica Exchange Sampling","volume":"11","author":"Jamal","year":"2017","journal-title":"Front. Neurosci."},{"issue":"9","key":"2026090312080723100_cit46","doi-asserted-by":"publisher","first-page":"101563","DOI":"10.1016\/j.xcrp.2023.101563","article-title":"An N-terminal alpha-synuclein\nfragment binds lipid\nvesicles to modulate lipid-induced aggregation","volume":"4","author":"Meade","year":"2023","journal-title":"Cell Reports Physical Science"},{"issue":"9","key":"2026090312080723100_cit47","doi-asserted-by":"publisher","first-page":"2452","DOI":"10.3390\/cells10092452","article-title":"Alpha-Synuclein\nand Lipids: The Elephant in the Room?","volume":"10","author":"Sarchione","year":"2021","journal-title":"Cells"},{"issue":"10","key":"2026090312080723100_cit48","doi-asserted-by":"publisher","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and Dynamics of Micelle-bound\nHuman \u03b1-Synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"36","key":"2026090312080723100_cit49","doi-asserted-by":"publisher","first-page":"28261","DOI":"10.1074\/jbc.M110.157214","article-title":"The Lipid-binding\nDomain of Wild Type and Mutant \u03b1-Synuclein: Compactness and\nInterconversion Between the Broken and Extended Helix Forms","volume":"285","author":"Georgieva","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"8","key":"2026090312080723100_cit50","doi-asserted-by":"publisher","first-page":"1287","DOI":"10.1038\/s41556-024-01456-1","article-title":"VAMP2\nchaperones \u03b1-synuclein in synaptic vesicle co-condensates","volume":"26","author":"Wang","year":"2024","journal-title":"Nat. Cell Biol."},{"issue":"15","key":"2026090312080723100_cit51","doi-asserted-by":"publisher","first-page":"8213","DOI":"10.1021\/acs.analchem.4c03978","article-title":"Strategies for Acid\nand Amine Cross-linking and Labeling\nfor Protein Structural Characterization Using Mass Spectrometry","volume":"97","author":"Dollar","year":"2025","journal-title":"Anal. Chem."},{"issue":"2","key":"2026090312080723100_cit52","doi-asserted-by":"publisher","first-page":"898","DOI":"10.1021\/pr400953w","article-title":"Enhanced identification\nof zero-length chemical cross-links using label-free quantitation\nand high-resolution fragment ion spectra","volume":"13","author":"Sriswasdi","year":"2014","journal-title":"J.\nProteome Res."},{"issue":"8","key":"2026090312080723100_cit53","doi-asserted-by":"publisher","first-page":"7500","DOI":"10.1021\/acs.chemrev.1c00786","article-title":"Cross-Linking Mass\nSpectrometry for Investigating Protein Conformations and Protein\u2013Protein\nInteractions\u2500A Method for All Seasons","volume":"122","author":"Piersimoni","year":"2022","journal-title":"Chem. Rev."},{"issue":"46","key":"2026090312080723100_cit54","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202205726","article-title":"Direct Observation\nof \u2033Elongated\u2033 Conformational States in \u03b1-Synuclein\nupon Liquid-Liquid Phase Separation","volume":"61","author":"Ubbiali","year":"2022","journal-title":"Angew.\nChem., Int. Ed."},{"issue":"3","key":"2026090312080723100_cit55","doi-asserted-by":"publisher","DOI":"10.1063\/1.4813502","article-title":"Interactions\nof S-peptide analogue\nin aqueous urea and trimethylamine-N-oxide solutions: A molecular\ndynamics simulation study","volume":"139","author":"Sarma","year":"2013","journal-title":"J. Chem. Phys."},{"issue":"1","key":"2026090312080723100_cit56","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/0021-9797(90)90037-O","article-title":"Micellar properties of octylglucoside in aqueous solutions","volume":"137","author":"Kameyama","year":"1990","journal-title":"J. Colloid Interface Sci."},{"issue":"24","key":"2026090312080723100_cit57","doi-asserted-by":"publisher","first-page":"21450","DOI":"10.1074\/jbc.M111.224055","article-title":"\u03b1-Synuclein\nPopulates Both Elongated and Broken\nHelix States on Small Unilamellar Vesicles","volume":"286","author":"Lokappa","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"8108","key":"2026090312080723100_cit58","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1038\/s41586-026-10141-2","article-title":"Accurate\npredictions of disordered protein ensembles with STARLING","volume":"652","author":"Novak","year":"2026","journal-title":"Nature"},{"issue":"1","key":"2026090312080723100_cit59","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2022.167714","article-title":"Functional\nand Pathological Effects of \u03b1-Synuclein on Synaptic SNARE Complexes","volume":"435","author":"Gao","year":"2023","journal-title":"J. Mol. 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