Tau local structure shields an amyloid-forming motif and controls aggregation propensity

The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain of tau encodes a metastable local structure and per...

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Autores principales:	Dailu Chen, Kenneth W. Drombosky, Zhiqiang Hou, Levent Sari, Omar M. Kashmer, Bryan D. Ryder, Valerie A. Perez, DaNae R. Woodard, Milo M. Lin, Marc I. Diamond, Lukasz A. Joachimiak
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/03b30e34ee8f4915b39c71a3c1b8c803
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spelling	oai:doaj.org-article:03b30e34ee8f4915b39c71a3c1b8c8032021-12-02T15:35:35ZTau local structure shields an amyloid-forming motif and controls aggregation propensity10.1038/s41467-019-10355-12041-1723https://doaj.org/article/03b30e34ee8f4915b39c71a3c1b8c8032019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10355-1https://doaj.org/toc/2041-1723The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain of tau encodes a metastable local structure and perturbations through mutations and proline isomerization cause an aggregation phenotype in vitro and in cells.Dailu ChenKenneth W. DromboskyZhiqiang HouLevent SariOmar M. KashmerBryan D. RyderValerie A. PerezDaNae R. WoodardMilo M. LinMarc I. DiamondLukasz A. JoachimiakNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Dailu Chen Kenneth W. Drombosky Zhiqiang Hou Levent Sari Omar M. Kashmer Bryan D. Ryder Valerie A. Perez DaNae R. Woodard Milo M. Lin Marc I. Diamond Lukasz A. Joachimiak Tau local structure shields an amyloid-forming motif and controls aggregation propensity
description	The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain of tau encodes a metastable local structure and perturbations through mutations and proline isomerization cause an aggregation phenotype in vitro and in cells.
format	article
author	Dailu Chen Kenneth W. Drombosky Zhiqiang Hou Levent Sari Omar M. Kashmer Bryan D. Ryder Valerie A. Perez DaNae R. Woodard Milo M. Lin Marc I. Diamond Lukasz A. Joachimiak
author_facet	Dailu Chen Kenneth W. Drombosky Zhiqiang Hou Levent Sari Omar M. Kashmer Bryan D. Ryder Valerie A. Perez DaNae R. Woodard Milo M. Lin Marc I. Diamond Lukasz A. Joachimiak
author_sort	Dailu Chen
title	Tau local structure shields an amyloid-forming motif and controls aggregation propensity
title_short	Tau local structure shields an amyloid-forming motif and controls aggregation propensity
title_full	Tau local structure shields an amyloid-forming motif and controls aggregation propensity
title_fullStr	Tau local structure shields an amyloid-forming motif and controls aggregation propensity
title_full_unstemmed	Tau local structure shields an amyloid-forming motif and controls aggregation propensity
title_sort	tau local structure shields an amyloid-forming motif and controls aggregation propensity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/03b30e34ee8f4915b39c71a3c1b8c803
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Tau local structure shields an amyloid-forming motif and controls aggregation propensity

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