ArticleACS chemical neuroscience2026
Inhibiting Disulfide Bonding in Truncated Tau297-391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies.
Article in ACS chemical neuroscience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.Research square · 2026Article
- Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.bioRxiv : the preprint server for biology · 2026Article
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Authors and funding
12 authors.
Funding
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Abstract
Tau undergoes fibrillogenesis in a group of neurodegenerative diseases, termed tauopathies. Each tauopathy is characterized by tau fibrils with disease-specific conformations, highlighting the complexity of tau self-assembly. This has led to debate surrounding the precise mechanisms that govern the self-assembly of tau in disease, especially the involvement of disulfide bonding (DSB) between cysteine residues. In this study, we use a truncated form of tau, dGAE, capable of forming filaments identical to those in disease. We reveal the impact of DSB on dGAE assembly and propagation by resolving the global mechanisms that dominate its assembly. We found evidence of surface-mediated secondary nucleation and fragmentation being active in dGAE assembly. The inhibition of DSB during dGAE assembly leads to an enhanced aggregation rate through a reduced lag phase but with no effect on the global assembly mechanisms. We suggest this is due to the formation of a dominant, seed-competent species in the absence of DSB that facilitates elongation and secondary nucleation, resulting in enhanced assembly.
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