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Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
Refolding aggregated proteins is essential in combating cellular proteotoxic stress. Together with Hsp70, Hsp100 chaperones, including Escherichia coli ClpB, form a powerful disaggregation machine that threads aggregated polypeptides through the central pore of tandem adenosine triphosphatase (ATPas...
שמור ב:
| הוצא לאור ב: | Sci Adv |
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| Main Authors: | , , , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
American Association for the Advancement of Science
2017
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5544394/ https://ncbi.nlm.nih.gov/pubmed/28798962 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1126/sciadv.1701726 |
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