The unfolding story of a redox chaperone
Oxidative stress, especially in combination with heat stress, poses a life-threatening challenge to many organisms by causing protein misfolding and aggregation. In this issue, Reichmann et al. demonstrate how a destabilized linker region of the bacterial chaperone Hsp33 prevents aggregation of a de...
Gespeichert in:
| 1. Verfasser: | |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2 March 2012
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| In: |
Cell
Year: 2012, Jahrgang: 148, Heft: 5, Pages: 843-844 |
| ISSN: | 1097-4172 |
| DOI: | 10.1016/j.cell.2012.02.029 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1016/j.cell.2012.02.029 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0092867412002292 
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| Verfasserangaben: | Matthias P. Mayer |
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| 520 | |a Oxidative stress, especially in combination with heat stress, poses a life-threatening challenge to many organisms by causing protein misfolding and aggregation. In this issue, Reichmann et al. demonstrate how a destabilized linker region of the bacterial chaperone Hsp33 prevents aggregation of a denatured protein by stabilizing structural elements. | ||
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