HSP90AA1 and cancer: By taking the expression levels of the epichaperome into consideration, Chiosis and colleagues were able to identify two different types of cancer cells that were named “Type 1” (enriched with HSP90 high-molecular-weight complexes) and “Type 2” cells (with low or no presence of the HSP90 complexes), which showed a different binding affinity and sensitivity to chaperone inhibitors, and thereby provided a proof of concept that the epichaperome can be targeted with a selective toxicity to the transformed cells that have an apparent higher dependence on the network [53].