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  Doxycycline Interferes With Tau Aggregation and Reduces Its Neuronal Toxicity

Medina, L., González-Lizárraga, F., Dominguez-Meijide, A., Ploper, D., Parrales, V., Sequeira, S., et al. (2021). Doxycycline Interferes With Tau Aggregation and Reduces Its Neuronal Toxicity. Frontiers in Aging Neuroscience, 13: 635760. doi:10.3389/fnagi.2021.635760.

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 Creators:
Medina, L., Author
González-Lizárraga, F., Author
Dominguez-Meijide, A., Author
Ploper, D., Author
Parrales, V., Author
Sequeira, S., Author
Cima-Omori, M.-S., Author
Zweckstetter, M.1, Author              
Bel, E. Del, Author
Michel, P. P., Author
Outeiro, T. Fleming, Author
Raisman-Vozari, R., Author
Chehín, R., Author
Socias, S. B., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: tauopathies, Alzheimer's disease, doxycycline, protein aggregation, tau
 Abstract: Tauopathies are neurodegenerative disorders with increasing incidence and still without cure. The extensive time required for development and approval of novel therapeutics highlights the need for testing and repurposing known safe molecules. Since doxycycline impacts α-synuclein aggregation and toxicity, herein we tested its effect on tau. We found that doxycycline reduces amyloid aggregation of the 2N4R and K18 isoforms of tau protein in a dose-dependent manner. Furthermore, in a cell free system doxycycline also prevents tau seeding and in cell culture reduces toxicity of tau aggregates. Overall, our results expand the spectrum of action of doxycycline against aggregation-prone proteins, opening novel perspectives for its repurposing as a disease-modifying drug for tauopathies.

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Language(s): eng - English
 Dates: 2021-03-22
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fnagi.2021.635760
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Title: Frontiers in Aging Neuroscience
Source Genre: Journal
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Pages: 13 Volume / Issue: 13 Sequence Number: 635760 Start / End Page: - Identifier: -