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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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Hauptverfasser: Ungelenk, Sophia Maria (VerfasserIn) , Moayed, Fatemeh (VerfasserIn) , Ho, Chi-Ting (VerfasserIn) , Grousl, Tomas (VerfasserIn) , Scharf, Annette (VerfasserIn) , Mashaghi, Alireza (VerfasserIn) , Tans, Sander (VerfasserIn) , Mayer, Matthias P. (VerfasserIn) , Mogk, Axel (VerfasserIn) , Bukau, Bernd (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 30 Nov 2016
In: Nature Communications
Year: 2016, Jahrgang: 7, Pages: 1-14
ISSN:2041-1723
DOI:10.1038/ncomms13673
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncomms13673
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncomms13673
Volltext
Verfasserangaben:Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer, Axel Mogk & Bernd Bukau
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 29.05.2020
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/ncomms13673

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