Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

Small heat shock proteins (sHsps) contribute to cellular recovery and survival following stress causing elevated levels of misfolded or unfolded proteins. Here the authors demonstrate that sHsps function by maintaining aggregating proteins in close-to-native conformations to facilitate chaperone-med...

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Autores principales:	Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer, Axel Mogk, Bernd Bukau
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d064b25e594849efb795495f07d85f93
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spelling	oai:doaj.org-article:d064b25e594849efb795495f07d85f932021-12-02T16:49:42ZSmall heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding10.1038/ncomms136732041-1723https://doaj.org/article/d064b25e594849efb795495f07d85f932016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13673https://doaj.org/toc/2041-1723Small heat shock proteins (sHsps) contribute to cellular recovery and survival following stress causing elevated levels of misfolded or unfolded proteins. Here the authors demonstrate that sHsps function by maintaining aggregating proteins in close-to-native conformations to facilitate chaperone-mediated refolding.Sophia UngelenkFatemeh MoayedChi-Ting HoTomas GrouslAnnette ScharfAlireza MashaghiSander TansMatthias P. MayerAxel MogkBernd BukauNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sophia Ungelenk Fatemeh Moayed Chi-Ting Ho Tomas Grousl Annette Scharf Alireza Mashaghi Sander Tans Matthias P. Mayer Axel Mogk Bernd Bukau Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
description	Small heat shock proteins (sHsps) contribute to cellular recovery and survival following stress causing elevated levels of misfolded or unfolded proteins. Here the authors demonstrate that sHsps function by maintaining aggregating proteins in close-to-native conformations to facilitate chaperone-mediated refolding.
format	article
author	Sophia Ungelenk Fatemeh Moayed Chi-Ting Ho Tomas Grousl Annette Scharf Alireza Mashaghi Sander Tans Matthias P. Mayer Axel Mogk Bernd Bukau
author_facet	Sophia Ungelenk Fatemeh Moayed Chi-Ting Ho Tomas Grousl Annette Scharf Alireza Mashaghi Sander Tans Matthias P. Mayer Axel Mogk Bernd Bukau
author_sort	Sophia Ungelenk
title	Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
title_short	Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
title_full	Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
title_fullStr	Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
title_full_unstemmed	Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
title_sort	small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/d064b25e594849efb795495f07d85f93
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Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

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