NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90
Author:
Funder
HHS | NIH | National Cancer Institute
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference41 articles.
1. GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum;Marzec;Biochim. Biophys. Acta,2012
2. Evolution and function of diverse Hsp90 homologs and cochaperone proteins;Johnson;Biochim. Biophys. Acta,2012
3. HSP90 at the hub of protein homeostasis: emerging mechanistic insights;Taipale;Nat. Rev. Mol. Cell Biol,2010
4. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2;Patel;Nat. Chem. Biol,2013
5. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability;Randow;Nat. Cell Biol,2001
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