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: | , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
30 Nov 2016
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| 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 
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| Verfasserangaben: | 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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| 520 | |a 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. | ||
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