{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:57:09Z","timestamp":1790841429184,"version":"4.1.0"},"reference-count":99,"publisher":"The Royal Society","issue":"1960","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"European Union Joint Programme on Neurodegenerative Disease","id":[{"id":"https:\/\/ror.org\/019w4f821","id-type":"ROR","asserted-by":"crossref"}]},{"name":"EraPerMed"},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-23-JPW2-0006"],"award-info":[{"award-number":["ANR-23-JPW2-0006"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-21-HBPR-0003-01"],"award-info":[{"award-number":["ANR-21-HBPR-0003-01"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-22-PERM-0006"],"award-info":[{"award-number":["ANR-22-PERM-0006"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>This short review discusses the structural and molecular events at the origin of diverse debilitating neurodegenerative diseases. The pathological consequences owing to the primary, secondary, tertiary and quaternary structural diversity of alpha-synuclein and tau proteins and the aggregates they form are presented. The crosstalk between alpha-synuclein and tau proteins aggregates structural heterogeneity and cellular homeostasis, and more precisely the proteostasis network is next considered. Overall, the proteostasis network appears as the master regulator of distinct synucleinopathies and tauopathies progression depending on its capacity to clear and\/or disassemble to completion structurally diverse alpha-synuclein or tau fibrillar aggregates or not.<\/jats:p>\n                  <jats:p>This article is part of the Theo Murphy meeting issue \u2018ProteostaSys: a systems view of proteostasis\u2019.<\/jats:p>","DOI":"10.1098\/rstb.2025.0272","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:08:09Z","timestamp":1790838489000},"source":"Crossref","is-referenced-by-count":0,"title":["Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies"],"prefix":"10.1098","volume":"381","author":[{"given":"Virginie","family":"Redeker","sequence":"first","affiliation":[{"name":"Laboratory of Neurodegenerative Diseases, CNRS 1 , Paris, \u00cele-de-France, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0000-7096","authenticated-orcid":false,"given":"Ronald","family":"Melki","sequence":"additional","affiliation":[{"name":"MIRcen, CEA 2 , Fontenay-aux-Roses, \u00cele-de-France, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"175","published-online":{"date-parts":[[2026,10,1]]},"reference":[{"key":"2026100103075550200_RSTB-2025-0272.R1C1","volume-title":"Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding","author":"Fersht","year":"1999"},{"key":"2026100103075550200_RSTB-2025-0272.R1C2","doi-asserted-by":"crossref","first-page":"e4","DOI":"10.1017\/S0033583523000045","article-title":"From covalent transition states in chemistry to noncovalent in biology: from \u03b2- to \u03a6-value analysis of protein folding","volume":"57","author":"Fersht","year":"2024","journal-title":"Q. Rev. Biophys."},{"key":"2026100103075550200_RSTB-2025-0272.R1C3","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s12551-017-0346-7","article-title":"Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins","volume":"10","author":"Arai","year":"2018","journal-title":"Biophys. Rev."},{"key":"2026100103075550200_RSTB-2025-0272.R1C4","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1016\/j.jmb.2018.04.003","article-title":"Expanding the paradigm: intrinsically disordered proteins and allosteric regulation","volume":"430","author":"Berlow","year":"2018","journal-title":"J. Mol. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C5","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.semcdb.2003.12.008","article-title":"Principles of protein folding, misfolding and aggregation","volume":"15","author":"Dobson","year":"2004","journal-title":"Semin. Cell. Dev. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C6","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev-biochem-060614-033955","article-title":"The biology of proteostasis in aging and disease","volume":"84","author":"Labbadia","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C7","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1021\/bi011711s","article-title":"Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from \u03b1-synuclein in vitro","volume":"41","author":"Cohlberg","year":"2002","journal-title":"Biochemistry"},{"key":"2026100103075550200_RSTB-2025-0272.R1C8","doi-asserted-by":"crossref","first-page":"10223","DOI":"10.1021\/bi980537d","article-title":"Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution","volume":"37","author":"Friedhoff","year":"1998","journal-title":"Biochemistry"},{"key":"2026100103075550200_RSTB-2025-0272.R1C9","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/S0014-5793(96)01386-5","article-title":"RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments","volume":"399","author":"Kampers","year":"1996","journal-title":"FEBS Lett."},{"key":"2026100103075550200_RSTB-2025-0272.R1C10","doi-asserted-by":"crossref","first-page":"44284","DOI":"10.1074\/jbc.M105343200","article-title":"Metal-triggered structural transformations, aggregation, and fibrillation of human \u03b1-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C11","doi-asserted-by":"crossref","first-page":"336","DOI":"10.3390\/ijms19020336","article-title":"Insights into the molecular mechanisms of Alzheimer's and Parkinson's diseases with molecular simulations: understanding the roles of artificial and pathological missense mutations in intrinsically disordered proteins related to pathology","volume":"19","author":"Coskuner-Weber","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C12","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.tips.2014.12.004","article-title":"Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases","volume":"36","author":"Ciryam","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C13","volume-title":"Thermodynamics of the polymerization of protein","author":"Oosawa","year":"1975"},{"key":"2026100103075550200_RSTB-2025-0272.R1C14","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1146\/annurev-genet-112618-043527","article-title":"Liquid\u2013liquid phase separation in disease","volume":"53","author":"Alberti","year":"2019","journal-title":"Annu. Rev. Genet."},{"key":"2026100103075550200_RSTB-2025-0272.R1C15","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1038\/s41580-020-00326-6","article-title":"Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing","volume":"22","author":"Alberti","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C16","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tcb.2018.02.004","article-title":"Protein phase separation: a new phase in cell biology","volume":"28","author":"Boeynaems","year":"2018","journal-title":"Trends Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C17","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","article-title":"Liquid\u2013liquid phase separation in biology","volume":"30","author":"Hyman","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C18","doi-asserted-by":"crossref","first-page":"5473","DOI":"10.1039\/C9CS00199A","article-title":"Half a century of amyloids: past, present and future","volume":"49","author":"Ke","year":"2020","journal-title":"Chem. Soc. Rev."},{"key":"2026100103075550200_RSTB-2025-0272.R1C19","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1007\/s000180050107","article-title":"The molecular basis of amyloidosis","volume":"53","author":"Serpell","year":"1997","journal-title":"Cell. Mol. Life Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C20","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1098\/rstb.1992.0048","article-title":"Nucleotide hydrolysis regulates the dynamics of actin filaments and microtubules","volume":"336","author":"Carlier","year":"1992","journal-title":"Phil. Trans. R. Soc. B"},{"key":"2026100103075550200_RSTB-2025-0272.R1C21","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1038\/s41467-021-23682-z","article-title":"Phenotypic manifestation of \u03b1-synuclein strains derived from Parkinson's disease and multiple system atrophy in human dopaminergic neurons","volume":"12","author":"Tanudjojo","year":"2021","journal-title":"Nat. Commun."},{"key":"2026100103075550200_RSTB-2025-0272.R1C22","doi-asserted-by":"crossref","first-page":"4588","DOI":"10.3390\/molecules27144588","article-title":"Supersaturation-dependent formation of amyloid fibrils","volume":"27","author":"Goto","year":"2022","journal-title":"Molecules"},{"key":"2026100103075550200_RSTB-2025-0272.R1C23","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1016\/j.bbapap.2013.08.013","article-title":"Acceleration of the depolymerization of amyloid \u03b2 fibrils by ultrasonication","volume":"1834","author":"Yagi","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"2026100103075550200_RSTB-2025-0272.R1C24","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1002\/cm.21812","article-title":"Tau and neurodegeneration","volume":"81","author":"Goedert","year":"2024","journal-title":"Cytoskeleton"},{"key":"2026100103075550200_RSTB-2025-0272.R1C25","doi-asserted-by":"crossref","first-page":"S51","DOI":"10.3233\/JPD-179005","article-title":"The synucleinopathies: twenty years on","volume":"7","author":"Goedert","year":"2017","journal-title":"J. Parkinsons Dis."},{"key":"2026100103075550200_RSTB-2025-0272.R1C26","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1016\/S0140-6736(25)01637-X","article-title":"Burden of 375 diseases and injuries, risk-attributable burden of 88 risk factors, and healthy life expectancy in 204 countries and territories, including 660 subnational locations, 1990\u20132023: a systematic analysis for the Global Burden of Disease Study 2023","volume":"406","author":"GBD 2023 Disease and Injury and Risk Factor Collaborators","year":"2025","journal-title":"Lancet"},{"key":"2026100103075550200_RSTB-2025-0272.R1C27","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s00401-011-0852-9","article-title":"Neuropathology underlying clinical variability in patients with synucleinopathies","volume":"122","author":"Halliday","year":"2011","journal-title":"Acta Neuropathol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C28","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1093\/jnen\/nlae134","article-title":"Unraveling the clinical\u2013pathological correlations of subjects with isolated and mixed neurodegenerative processes in the National Alzheimer's Coordinating Center dataset","volume":"84","author":"Hiya","year":"2025","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C29","doi-asserted-by":"crossref","first-page":"1394","DOI":"10.1111\/jnc.15471","article-title":"Basal forebrain cholinergic system in the dementias: vulnerability, resilience, and resistance","volume":"158","author":"Geula","year":"2021","journal-title":"J. Neurochem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C30","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.tibs.2007.03.005","article-title":"Life on the edge: a link between gene expression levels and aggregation rates of human proteins","volume":"32","author":"Tartaglia","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C31","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0197-4580(02)00065-9","article-title":"Staging of brain pathology related to sporadic Parkinson's disease","volume":"24","author":"Braak","year":"2003","journal-title":"Neurobiol. Aging"},{"key":"2026100103075550200_RSTB-2025-0272.R1C32","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0165-0270(98)00173-3","article-title":"Silver staining method for demonstrating Lewy bodies in Parkinson's disease and argyrophilic oligodendrocytes in multiple system atrophy","volume":"87","author":"Braak","year":"1999","journal-title":"J. Neurosci. Methods"},{"key":"2026100103075550200_RSTB-2025-0272.R1C33","volume-title":"Greenfield's neuropathology","author":"Smith","year":"2025","edition":"10th edn."},{"key":"2026100103075550200_RSTB-2025-0272.R1C34","doi-asserted-by":"crossref","first-page":"e70308","DOI":"10.1111\/jnc.70308","article-title":"Local protein synthesis at synapses: a driver for synapse diversification","volume":"169","author":"Daskin","year":"2025","journal-title":"J. Neurochem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C35","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.tins.2025.08.002","article-title":"The integrated stress response in the brain: cell type-specific functions in health and neurological disorders","volume":"48","author":"Ho-Tieng","year":"2025","journal-title":"Trends Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C36","doi-asserted-by":"crossref","first-page":"101489","DOI":"10.1016\/j.mcpro.2025.101489","article-title":"An ultrasensitive spatial tissue proteomics workflow exceeding 100 proteomes per day","volume":"25","author":"Klingeberg","year":"2025","journal-title":"Mol. Cell. Proteomics"},{"key":"2026100103075550200_RSTB-2025-0272.R1C37","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1002\/mds.30097","article-title":"New multiomic studies shed light on cellular diversity and neuronal susceptibility in Parkinson's disease","volume":"40","author":"Liang","year":"2025","journal-title":"Mov. Disord."},{"key":"2026100103075550200_RSTB-2025-0272.R1C38","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1038\/s41583-024-00888-w","article-title":"Understanding the molecular diversity of synapses","volume":"26","author":"van Oostrum","year":"2025","journal-title":"Nat. Rev. Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C39","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1038\/s41587-025-02659-z","article-title":"A tissue-specific atlas of protein\u2013protein associations enables prioritization of candidate disease genes","volume":"44","author":"Laman Trip","year":"2025","journal-title":"Nat. Biotechnol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C40","doi-asserted-by":"crossref","first-page":"5092","DOI":"10.1038\/s41467-025-60185-7","article-title":"Atlas of proteomic signatures of brain structure and its links to brain disorders","volume":"16","author":"Ren","year":"2025","journal-title":"Nat. Commun."},{"key":"2026100103075550200_RSTB-2025-0272.R1C41","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1042\/bj0292351","article-title":"The X-ray interpretation of denaturation, the structure of the seed globulins","volume":"29","author":"Astbury","year":"1935","journal-title":"Biochem. J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C42","volume-title":"Introduction to protein structure","author":"Branden","year":"1999","edition":"2nd edn."},{"key":"2026100103075550200_RSTB-2025-0272.R1C43","doi-asserted-by":"crossref","first-page":"5950","DOI":"10.1111\/j.1742-4658.2005.05025.x","article-title":"Structures for amyloid fibrils","volume":"272","author":"Makin","year":"2005","journal-title":"FEBS J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C44","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1126\/science.1150057","article-title":"Role of intermolecular forces in defining material properties of protein nanofibrils","volume":"318","author":"Knowles","year":"2007","journal-title":"Science"},{"key":"2026100103075550200_RSTB-2025-0272.R1C45","doi-asserted-by":"crossref","first-page":"37970","DOI":"10.1038\/srep37970","article-title":"Nanomechanical properties of distinct fibrillar polymorphs of the protein \u03b1-synuclein","volume":"6","author":"Makky","year":"2016","journal-title":"Sci. Rep."},{"key":"2026100103075550200_RSTB-2025-0272.R1C46","doi-asserted-by":"crossref","first-page":"2497","DOI":"10.1016\/j.bpj.2020.10.045","article-title":"Atomic force microscopy imaging and nanomechanical properties of six tau isoform assemblies","volume":"119","author":"Makky","year":"2020","journal-title":"Biophys. J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C47","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1021\/jacs.8b10142","article-title":"Inverse correlation between amyloid stiffness and size","volume":"141","author":"Nassar","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"2026100103075550200_RSTB-2025-0272.R1C48","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1021\/ja208316h","article-title":"\u03b1-Synuclein induces both positive mean curvature and negative Gaussian curvature in membranes","volume":"134","author":"Braun","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"2026100103075550200_RSTB-2025-0272.R1C49","doi-asserted-by":"crossref","first-page":"9962","DOI":"10.1021\/ja5016958","article-title":"\u03b1-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry","volume":"136","author":"Braun","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"2026100103075550200_RSTB-2025-0272.R1C50","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1038\/nn.4529","article-title":"\u03b1-Synuclein promotes dilation of the exocytotic fusion pore","volume":"20","author":"Logan","year":"2017","journal-title":"Nat. Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C51","doi-asserted-by":"crossref","first-page":"29301","DOI":"10.1074\/jbc.M112.365817","article-title":"Remodeling of lipid vesicles into cylindrical micelles by \u03b1-synuclein in an extended \u03b1-helical conformation","volume":"287","author":"Mizuno","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C52","doi-asserted-by":"crossref","first-page":"21966","DOI":"10.1074\/jbc.M401076200","article-title":"\u03b1-Synuclein has a high affinity for packing defects in a bilayer membrane: a thermodynamics study","volume":"279","author":"Nuscher","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C53","doi-asserted-by":"crossref","first-page":"20883","DOI":"10.1074\/jbc.M113.478297","article-title":"\u03b1-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling","volume":"288","author":"Ouberai","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C54","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1083\/jcb.201011118","article-title":"\u03b1-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding","volume":"194","author":"Pranke","year":"2011","journal-title":"J. Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C55","doi-asserted-by":"crossref","first-page":"32486","DOI":"10.1074\/jbc.M110.139576","article-title":"Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins","volume":"285","author":"Varkey","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C56","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.tins.2022.11.007","article-title":"\u03b1-Synuclein in synaptic function and dysfunction","volume":"46","author":"Sharma","year":"2023","journal-title":"Trends Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C57","doi-asserted-by":"crossref","first-page":"167775","DOI":"10.1016\/j.jmb.2022.167775","article-title":"The role of \u03b1-synuclein in SNARE-mediated synaptic vesicle fusion","volume":"435","author":"Yoo","year":"2023","journal-title":"J. Mol. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C58","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.3389\/fneur.2020.01056","article-title":"Nuclear transport deficits in tau-related neurodegenerative diseases","volume":"11","author":"Diez","year":"2020","journal-title":"Front. Neurol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C59","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1111\/j.1749-6632.1996.tb34407.x","article-title":"Structure, microtubule interactions, and phosphorylation of tau protein","volume":"777","author":"Mandelkow","year":"1996","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C60","doi-asserted-by":"crossref","first-page":"725241","DOI":"10.3389\/fcell.2021.725241","article-title":"Tau and membranes: interactions that promote folding and condensation","volume":"9","author":"Sallaberry","year":"2021","journal-title":"Front. Cell. Dev. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C61","doi-asserted-by":"crossref","first-page":"7264","DOI":"10.1523\/JNEUROSCI.6194-10.2011","article-title":"Functional alterations to the nigrostriatal system in mice lacking all three members of the synuclein family","volume":"31","author":"Anwar","year":"2011","journal-title":"J. Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C62","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1242\/jcs.114.6.1179","article-title":"Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice","volume":"114","author":"Dawson","year":"2001","journal-title":"J. Cell Sci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C63","doi-asserted-by":"crossref","first-page":"19573","DOI":"10.1073\/pnas.1005005107","article-title":"\u03b1\u03b2\u03b3-Synuclein triple knockout mice reveal age-dependent neuronal dysfunction","volume":"107","author":"Greten-Harrison","year":"2010","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026100103075550200_RSTB-2025-0272.R1C64","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/369488a0","article-title":"Altered microtubule organization in small-calibre axons of mice lacking tau protein","volume":"369","author":"Harada","year":"1994","journal-title":"Nature"},{"key":"2026100103075550200_RSTB-2025-0272.R1C65","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1111\/jnc.14810","article-title":"The physiological role of \u03b1-synuclein and its relationship to Parkinson's disease","volume":"150","author":"Sulzer","year":"2019","journal-title":"J. Neurochem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C66","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med."},{"key":"2026100103075550200_RSTB-2025-0272.R1C67","doi-asserted-by":"crossref","first-page":"E1481","DOI":"10.1073\/pnas.1321811111","article-title":"Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition","volume":"111","author":"Yu","year":"2014","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026100103075550200_RSTB-2025-0272.R1C68","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.15252\/embj.201591397","article-title":"\u03b1-Synuclein assemblies sequester neuronal \u03b13-Na+\/K+-ATPase and impair Na+ gradient","volume":"34","author":"Shrivastava","year":"2015","journal-title":"EMBO J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C69","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.neuron.2017.05.026","article-title":"Physico-pathologic mechanisms involved in neurodegeneration: misfolded protein-plasma membrane interactions","volume":"95","author":"Shrivastava","year":"2017","journal-title":"Neuron"},{"key":"2026100103075550200_RSTB-2025-0272.R1C70","doi-asserted-by":"crossref","first-page":"201899871","DOI":"10.15252\/embj.201899871","article-title":"Clustering of tau fibrils impairs the synaptic composition of \u03b13-Na+\/K+-ATPase and AMPA receptors","volume":"38","author":"Shrivastava","year":"2019","journal-title":"EMBO J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C71","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/nrm2873","article-title":"Prion-like transmission of protein aggregates in neurodegenerative diseases","volume":"11","author":"Brundin","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C72","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/nrn2786","article-title":"Prion-like mechanisms in neurodegenerative diseases","volume":"11","author":"Frost","year":"2010","journal-title":"Nat. Rev. Neurosci."},{"key":"2026100103075550200_RSTB-2025-0272.R1C73","doi-asserted-by":"crossref","first-page":"e1003351","DOI":"10.1371\/journal.pgen.1003351","article-title":"Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans","volume":"9","author":"Nussbaum-Krammer","year":"2013","journal-title":"PLoS Genet."},{"key":"2026100103075550200_RSTB-2025-0272.R1C74","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s40478-025-01958-5","article-title":"Proximity proteomics reveals unique and shared pathological features between multiple system atrophy and Parkinson's disease","volume":"13","author":"Choi","year":"2025","journal-title":"Acta Neuropathol. Commun."},{"key":"2026100103075550200_RSTB-2025-0272.R1C75","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1186\/s13024-022-00572-6","article-title":"Tau interactome and RNA binding proteins in neurodegenerative diseases","volume":"17","author":"Kavanagh","year":"2022","journal-title":"Mol. Neurodegener."},{"key":"2026100103075550200_RSTB-2025-0272.R1C76","doi-asserted-by":"crossref","first-page":"e2114405119","DOI":"10.1073\/pnas.2114405119","article-title":"In situ proximity labeling identifies Lewy pathology molecular interactions in the human brain","volume":"119","author":"Killinger","year":"2022","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026100103075550200_RSTB-2025-0272.R1C77","doi-asserted-by":"crossref","first-page":"101458","DOI":"10.1016\/j.mcpro.2025.101458","article-title":"Proximity labeling of the tau repeat domain enriches RNA-binding Proteins that are altered in Alzheimer's disease and related tauopathies","volume":"25","author":"Shapley","year":"2025","journal-title":"Mol. Cell. Proteom."},{"key":"2026100103075550200_RSTB-2025-0272.R1C78","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.dib.2016.02.018","article-title":"Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar \u03b1-synuclein assemblies by mass spectrometry","volume":"7","author":"Shrivastava","year":"2016","journal-title":"Data Brief"},{"key":"2026100103075550200_RSTB-2025-0272.R1C79","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/s41531-025-01084-y","article-title":"Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation","volume":"11","author":"Mahul-Mellier","year":"2025","journal-title":"NPJ Parkinsons Dis."},{"key":"2026100103075550200_RSTB-2025-0272.R1C80","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1042\/BST20230596","article-title":"Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein","volume":"52","author":"Alhadidy","year":"2024","journal-title":"Biochem. Soc. Trans."},{"key":"2026100103075550200_RSTB-2025-0272.R1C81","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1038\/s44320-026-00199-5","article-title":"Structure\u2013function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies","volume":"22","author":"Serdiuk","year":"2026","journal-title":"Mol. Syst. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C82","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.1141448","article-title":"Adapting proteostasis for disease intervention","volume":"319","author":"Balch","year":"2008","journal-title":"Science"},{"key":"2026100103075550200_RSTB-2025-0272.R1C83","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.sbi.2009.11.001","article-title":"A cellular perspective on conformational disease: the role of genetic background and proteostasis networks","volume":"20","author":"Gidalevitz","year":"2010","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C84","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1007\/978-1-4419-7002-2_11","volume-title":"Protein metabolism and homeostasis in aging","author":"Kikis","year":"2010"},{"key":"2026100103075550200_RSTB-2025-0272.R1C85","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1101\/sqb.2012.76.010637","article-title":"The heat shock response: systems biology of proteotoxic stress in aging and disease","volume":"76","author":"Morimoto","year":"2011","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C86","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1083\/jcb.201612111","article-title":"Shaping proteostasis at the cellular, tissue, and organismal level","volume":"216","author":"Sala","year":"2017","journal-title":"J. Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C87","doi-asserted-by":"crossref","first-page":"2803","DOI":"10.1093\/brain\/awaa223","article-title":"Phosphorylated tau interactome in the human Alzheimer's disease brain","volume":"143","author":"Drummond","year":"2020","journal-title":"Brain"},{"key":"2026100103075550200_RSTB-2025-0272.R1C88","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.nbd.2010.05.007","article-title":"Chaperone networks: tipping the balance in protein folding diseases","volume":"40","author":"Voisine","year":"2010","journal-title":"Neurobiol. Dis."},{"key":"2026100103075550200_RSTB-2025-0272.R1C89","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1126\/science.1124514","article-title":"Progressive disruption of cellular protein folding in models of polyglutamine diseases","volume":"311","author":"Gidalevitz","year":"2006","journal-title":"Science"},{"key":"2026100103075550200_RSTB-2025-0272.R1C90","doi-asserted-by":"crossref","first-page":"2577406","DOI":"10.1080\/27694127.2025.2577406","article-title":"The role of autophagy in synucleinopathy: clearance versus spread of \u03b1-synuclein","volume":"4","author":"Birnbaum","year":"2025","journal-title":"Autophagy Rep."},{"key":"2026100103075550200_RSTB-2025-0272.R1C91","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.pneurobio.2013.03.001","article-title":"Tau degradation: the ubiquitin\u2013proteasome system versus the autophagy\u2013lysosome system","volume":"105","author":"Lee","year":"2013","journal-title":"Prog. Neurobiol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C92","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1038\/s41580-024-00757-5","article-title":"Mechanisms of autophagy\u2013lysosome dysfunction in neurodegenerative diseases","volume":"25","author":"Nixon","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C93","doi-asserted-by":"crossref","first-page":"108895","DOI":"10.1016\/j.celrep.2021.108895","article-title":"TNF-\u03b1 and \u03b1-synuclein fibrils differently regulate human astrocyte immune reactivity and impair mitochondrial respiration","volume":"34","author":"Russ","year":"2021","journal-title":"Cell Rep."},{"key":"2026100103075550200_RSTB-2025-0272.R1C94","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.4049\/jimmunol.2100035","article-title":"Microglial NLRP3 inflammasome activation upon TLR2 and TLR5 ligation by distinct \u03b1-synuclein assemblies","volume":"207","author":"Scheiblich","year":"2021","journal-title":"J. Immunol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C95","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1038\/s41586-019-1769-z","article-title":"NLRP3 inflammasome activation drives tau pathology.","volume":"575","author":"Ising","year":"2019","journal-title":"Nature"},{"key":"2026100103075550200_RSTB-2025-0272.R1C96","doi-asserted-by":"crossref","first-page":"6499","DOI":"10.1038\/s44318-025-00573-3","article-title":"Structural polymorphism of \u03b1-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation","volume":"44","author":"J\u00e4ger","year":"2025","journal-title":"EMBO J."},{"key":"2026100103075550200_RSTB-2025-0272.R1C97","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1038\/s42003-022-04289-6","article-title":"Dissecting aggregation and seeding dynamics of \u03b1-Syn polymorphs using the phasor approach to FLIM","volume":"5","author":"Tittelmeier","year":"2022","journal-title":"Commun. Biol."},{"key":"2026100103075550200_RSTB-2025-0272.R1C98","doi-asserted-by":"crossref","first-page":"9676","DOI":"10.1074\/jbc.RA120.013478","article-title":"Disassembly of tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species.","volume":"295","author":"Nachman","year":"2020","journal-title":"J. Biol. Chem."},{"key":"2026100103075550200_RSTB-2025-0272.R1C99","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1039\/D5SC04927J","article-title":"Thermodynamic stability modulates chaperone-mediated disaggregation of \u03b1-synuclein fibrils","volume":"17","author":"Fricke","year":"2025","journal-title":"Chem. Sci."}],"container-title":["Philosophical Transactions of the Royal Society B: Biological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/royalsocietypublishing.org\/rstb\/article-pdf\/doi\/10.1098\/rstb.2025.0272\/6168526\/rstb.2025.0272.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/royalsocietypublishing.org\/rstb\/article-pdf\/doi\/10.1098\/rstb.2025.0272\/6168526\/rstb.2025.0272.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:08:21Z","timestamp":1790838501000},"score":1,"resource":{"primary":{"URL":"https:\/\/royalsocietypublishing.org\/rstb\/article\/381\/1960\/20250272\/483476\/Differential-proteostasis-imbalance-and-the"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,1]]},"references-count":99,"journal-issue":{"issue":"1960","published-online":{"date-parts":[[2026,10,1]]},"published-print":{"date-parts":[[2026,10,1]]}},"URL":"https:\/\/doi.org\/10.1098\/rstb.2025.0272","relation":{},"ISSN":["0962-8436","1471-2970"],"issn-type":[{"value":"0962-8436","type":"print"},{"value":"1471-2970","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,1]]},"article-number":"20250272"}}