A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
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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,… read more here.
Keywords: hsp90; methylated lysine; switch point; chaperone hsp90 ... See more keywords
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
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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… read more here.
Keywords: conformational dynamics; chaperone; chaperone hsp90; catalytic activity ... See more keywords
Abstract 2272: Targeting the chaperone Hsp90 to activate the immune system and eradicate the triple negative breast cancer
Sign Up to like & getrecommendations! 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… read more here.
Keywords: chaperone hsp90; breast cancer; targeting chaperone; cancer ... See more keywords