Integration with chaperome-wide functional RNA interference (RNAi) perturbation experiments in worm and in human cells led to the identification of a chaperome sub-network that safeguards proteostasis in aging and neurodegenerative diseases.
[4] Recently, a comprehensive literature survey reviewed the literature since the release of the human genome sequence in 2000 for systematic studies in small animal model systems and highlighted the power of model systems to unveil those key chaperone modifiers of proteotoxicity out of the large number represented in the wider human chaperome that could inform targets and strategies for therapeutic regulation of chaperone functionality.
[5] In 2016, a Nature article authored by Rodina et al. introduced a novel term, epichaperome, to refer to a network of existent chaperomes that are found only in cancer cells.
[7] What has been found is that this strengthened network amongst chaperomes is a mechanism for survival for cancer cells when adapting to stress[8] including hypoxia and heat.
The small molecule Hsp90 inhibitor, PU-H71, has been found to have a preferential binding to Hsp90 when it is in the highly integrated complexed form that is the epichaperome.