ArticleAngewandte Chemie (International ed. in English)2024
dGAE(297-391) Tau Fragment Promotes Formation of Chronic Traumatic Encephalopathy-Like Tau Filaments.
Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Rapid Fragment Screening byAngewandte Chemie (International ed. in English) · 2026Article
- Exploratory assessment of cerebrospinal fluid-related microdynamics after mild traumatic brain injury using intravoxel incoherent motion magnetic resonance imaging.Frontiers in neuroscience · 2026Article
- Macrocyclic β-arch peptides that mimic the structure and function of disease-associated tau folds.Nature chemistry · 2025Article
- A pathological phosphorylation pattern enhances tau cooperativity on microtubules and facilitates tau filament assembly.Research square · 2025Article
- dGAE(297-391) Tau Fragment Promotes Formation of Chronic Traumatic Encephalopathy-Like Tau Filaments.Angewandte Chemie (International ed. in English) · 2024Article
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Authors and funding
11 authors.
Funding
Abstract
The microtubule-associated protein tau forms disease-specific filamentous aggregates in several different neurodegenerative diseases. In order to understand how tau undergoes misfolding into a specific filament type and to control this process for drug development purposes, it is crucial to study in vitro tau aggregation methods and investigate the structures of the obtained filaments at the atomic level. Here, we used the tau fragment dGAE, which aggregates spontaneously, to seed the formation of full-length tau filaments. The structures of dGAE and full-length tau filaments were investigated by magic-angle spinning (MAS) solid-state NMR, showing that dGAE allows propagation of a chronic traumatic encephalopathy (CTE)-like fold to the full-length tau. The obtained filaments efficiently seeded tau aggregation in HEK293T cells. This work demonstrates that in vitro preparation of disease-specific types of full-length tau filaments is feasible.
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