ArticleFrontiers in neuroscience2018
Tau's Three-Repeat Domain and EFhd2 Co-incubation Leads to Increased Thioflavin Signal.
Article in Frontiers in neuroscience, 2018. 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, 7 citations in OpenAlex.
- Investigating the role of EFhd2 protein in modulating tau pathology in a tauopathy mouse model.Frontiers in molecular neuroscience · 2026Article
- EFhd2 co-aggregates with monomeric and filamentous tauFrontiers in neuroscience · 2024Article
- EFhd2 brain interactome reveals its association with different cellular and molecular processes.Journal of neurochemistry · 2021Article
- Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.Protein science : a publication of the Protein Society · 2021Review
- EFhd2 Affects Tau Liquid-Liquid Phase Separation.Frontiers in neuroscience · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Aggregation of the protein tau is a pathological hallmark of Alzheimer's disease (AD) and related disorders. However, the molecular mechanisms that lead to tau protein aggregation are still unclear. Previously, we showed that EFhd2 protein is associated with pathological aggregated forms of tau in AD brain. Further, immuno-gold analyses of purified tau aggregates showed that EFhd2 co-localized with filamentous tau structures. We demonstrated that EFhd2's coiled-coil domain is required for its association with tau proteins. However, it is unknown the role that EFhd2 plays in tau aggregation. Here, we show that incubation of K19-tau with substoichiometric amount of EFhd2 promote the formation of amyloid structures
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