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Eftekharzadeh, Bahareh

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Eftekharzadeh

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Bahareh

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Eftekharzadeh, Bahareh
Author's Publications: search.filters.isAuthorOfPublication.9aec81f0-adb4-4183-a3dd-c8f77554496d

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    Tau protein liquid–liquid phase separation can initiate tau aggregation
    (John Wiley and Sons Inc., 2018) Wegmann, Susanne; Eftekharzadeh, Bahareh; Tepper, Katharina; Zoltowska, Katarzyna; Bennett, Rachel; Dujardin, Simon; Laskowski, Pawel R; MacKenzie, Danny; Kamath, Tarun; Commins, Caitlin; Vanderburg, Charles; Roe, Allyson D; Fan, Zhanyun; Molliex, Amandine M; Hernandez‐Vega, Amayra; Muller, Daniel; Hyman, Anthony A; Mandelkow, Eckhard; Taylor, J Paul; Hyman, Bradley
    Abstract The transition between soluble intrinsically disordered tau protein and aggregated tau in neurofibrillary tangles in Alzheimer's disease is unknown. Here, we propose that soluble tau species can undergo liquid–liquid phase separation (LLPS) under cellular conditions and that phase‐separated tau droplets can serve as an intermediate toward tau aggregate formation. We demonstrate that phosphorylated or mutant aggregation prone recombinant tau undergoes LLPS, as does high molecular weight soluble phospho‐tau isolated from human Alzheimer brain. Droplet‐like tau can also be observed in neurons and other cells. We found that tau droplets become gel‐like in minutes, and over days start to spontaneously form thioflavin‐S‐positive tau aggregates that are competent of seeding cellular tau aggregation. Since analogous LLPS observations have been made for FUS, hnRNPA1, and TDP43, which aggregate in the context of amyotrophic lateral sclerosis, we suggest that LLPS represents a biophysical process with a role in multiple different neurodegenerative diseases.
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    Characterization of TauC3 antibody and demonstration of its potential to block tau propagation
    (Public Library of Science, 2017) Nicholls, Samantha B.; Devos, Sarah; Commins, Caitlin; Nobuhara, Chloe; Bennett, Rachel; Corjuc, Diana L.; Maury, Eduardo; Eftekharzadeh, Bahareh; Akingbade, Ololade; Fan, Zhanyun; Roe, Allyson D.; Takeda, Shuko; Wegmann, Susanne; Hyman, Bradley
    The spread of neurofibrillary tangle (NFT) pathology through the human brain is a hallmark of Alzheimer’s disease (AD), which is thought to be caused by the propagation of “seeding” competent soluble misfolded tau. “TauC3”, a C-terminally truncated form of tau that is generated by caspase-3 cleavage at D421, has previously been observed in NFTs and has been implicated in tau toxicity. Here we show that TauC3 is found in the seeding competent high molecular weight (HMW) protein fraction of human AD brain. Using a specific TauC3 antibody, we were able to substantially block the HMW tau seeding activity of human AD brain extracts in an in vitro tau seeding FRET assay. We propose that TauC3 could contribute to the templated tau misfolding that leads to NFT spread in AD brains.