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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Vydáno v:J Biol Chem
Hlavní autoři: Huck, John D., Que, Nanette L. S., Immormino, Robert M., Shrestha, Liza, Taldone, Tony, Chiosis, Gabriela, Gewirth, Daniel T.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2019
Témata:
Protein Structure and Folding
On-line přístup: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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