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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

The transmembrane domain of these chemosensors being exposed to a tighter evolutionary pressure lead to a relative evolutionary stability of the same 3-dimensional structure

g , Immunofluorescence images showing predominant nuclear localization of FLAG-tagged wild-type and Q27A mutant histone H4 proteins, in three independent biological replicates

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Transcriptome deregulation functional annotation (Fig