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446 These inhibitors, such as geldanamycin, bind to the N-terminal nucleotide-binding pocket of HSP90 with higher affinity than ATP, leading to the proteasomal degradation of HSP90-dependent client proteins

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345,346 FOXO4-DRI, a cell-permeable peptide, disrupted the FOXO4-p53 interaction, thereby reducing senescence-induced FOXO4 activity and selectively targeting SnCs for p53-dependent apoptosis (Table 1)

When metabolites and proteins expressed by these pathogens are created, they interfere with host transcription, translation, and DNA repair processes, leaving infected immune cells unable to express human metabolites