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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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Main Authors: Ungelenk, Sophia Maria (Author) , Moayed, Fatemeh (Author) , Ho, Chi-Ting (Author) , Grousl, Tomas (Author) , Scharf, Annette (Author) , Mashaghi, Alireza (Author) , Tans, Sander (Author) , Mayer, Matthias P. (Author) , Mogk, Axel (Author) , Bukau, Bernd (Author)
Format: Article (Journal)
Language:English
Published: 30 Nov 2016
In: Nature Communications
Year: 2016, Volume: 7, Pages: 1-14
ISSN:2041-1723
DOI:10.1038/ncomms13673
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncomms13673
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncomms13673
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Author Notes:Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer, Axel Mogk & Bernd Bukau
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Summary: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.
Item Description:Gesehen am 29.05.2020
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/ncomms13673

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