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The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.

https://doi.org/10.1101/500058
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Outgoing claims: the papers this work cites, builds on, or argues with.

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inferredcites →https://doi.org/10.1523/jneurosci.4650-14.2015openalex-snapshot
Definition of a Molecular Pathway Mediating α-Synuclein Neurotoxicity
inferredcites →https://doi.org/10.1523/jneurosci.4965-05.2006openalex-snapshot
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inferredcites →https://doi.org/10.2353/ajpath.2007.061232openalex-snapshot
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What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics
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inferred← citeshttps://doi.org/10.1016/j.molcel.2025.08.022openalex-snapshot
α-Synuclein aggregates inhibit ESCRT-III through sequestration and collateral degradation
inferred← citeshttps://doi.org/10.1016/j.nbd.2020.104876openalex-snapshot
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Selective neuronal vulnerability in Parkinson disease
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Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
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Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases
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Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation
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Regulation of α-synuclein by chaperones in mammalian cells
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O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology
inferred← citeshttps://doi.org/10.1038/s41593-019-0423-2openalex-snapshot
Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes
inferred← citeshttps://doi.org/10.1038/s41593-023-01341-4openalex-snapshot
Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
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The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration
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Post-fibrillization nitration of alpha-synuclein abolishes its seeding activity and pathology formation in primary neurons and in vivo
inferred← citeshttps://doi.org/10.1101/2024.11.29.625993openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2025.10.26.684610openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/470476openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/654582openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/740241openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/jnc.14707openalex-snapshot
In vitro models of synucleinopathies: informing on molecular mechanisms and protective strategies
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A simple, versatile and robust centrifugation‐based filtration protocol for the isolation and quantification of α‐synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α‐synuclein research
inferred← citeshttps://doi.org/10.1126/sciadv.abn0044openalex-snapshot
A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity
inferred← citeshttps://doi.org/10.1186/s40478-019-0865-5openalex-snapshot
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Multi-platform quantitation of alpha-synuclein human brain proteoforms suggests disease-specific biochemical profiles of synucleinopathies
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Widespread nuclear lamina injuries defeat proteostatic purposes of α-synuclein amyloid inclusions
inferred← citeshttps://doi.org/10.1515/tjb-2025-0031openalex-snapshot
Comparison of various fragmentation methods of alpha-synuclein fibrils for establishing a Parkinson’s disease-like model in cell culture
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