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Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-15048-8
Abstract: Methylation of a conserved lysine in C-terminal domain of the molecular chaperone Hsp90 was shown previously to affect its in vivo function. However, the underlying mechanism remained elusive. Through a combined experimental and computational approach,…
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Keywords:
hsp90;
methylated lysine;
switch point;
chaperone hsp90 ... See more keywords
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0
Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-15050-0
Abstract: The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell. To elucidate how…
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Keywords:
conformational dynamics;
chaperone;
chaperone hsp90;
catalytic activity ... See more keywords
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3
Published in 2023 at "Cancer Research"
DOI: 10.1158/1538-7445.am2023-2272
Abstract: Low response rates and immune-related adverse events limit the impact of cancer immunotherapy. To improve clinical outcomes, preclinical studies have shown that combining immunotherapies with N-terminal Hsp90 inhibitors resulted in improved efficacy, even though induction…
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Keywords:
chaperone hsp90;
breast cancer;
targeting chaperone;
cancer ... See more keywords