Načítá se...
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...
Uloženo v:
| Vydáno v: | Nat Commun |
|---|---|
| Hlavní autoři: | , , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group UK
2019
|
| Témata: | |
| On-line přístup: | 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 |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!
|