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NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90
The hsp90 chaperones govern the function of essential client proteins critical for normal cell function as well as cancer initiation and progression. Hsp90 activity is driven by ATP, which binds to the N-terminal domain and induces large conformational changes that are required for client maturation...
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| Yayımlandı: | J Biol Chem |
|---|---|
| Asıl Yazarlar: | , , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Biochemistry and Molecular Biology
2019
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6827299/ https://ncbi.nlm.nih.gov/pubmed/31501246 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009960 |
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