Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin
Integrated kinetic and structural investigations reveal that the ubiquitous co-chaperonin prefoldin interacts with its coiled-coil helices on the islet amyloid polypeptide fibril surface and fibril ends to inhibit fibril elongation and secondary nucleation.
Kaydedildi:
| Asıl Yazarlar: | , , , , , , , , , , |
|---|---|
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Nature Portfolio
2022-05-01
|
| Seri Bilgileri: | Nature Communications |
| Online Erişim: | https://doi.org/10.1038/s41467-022-30042-y |
| Etiketler: |
Etiket eklenmemiş, İlk siz ekleyin!
|