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Local unfolding of the HSP27 monomer regulates chaperone activity
The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here, we describe redox-induced changes to the structure, dynamics, and function of HSP27 and its conserved α-crystallin domain (ACD). While HSP27 assembles into oligomers, we sho...
שמור ב:
| הוצא לאור ב: | Nat Commun |
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| Main Authors: | , , , , , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
Nature Publishing Group UK
2019
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6403371/ https://ncbi.nlm.nih.gov/pubmed/30842409 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-019-08557-8 |
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