Inhibition of heat shock protein 90 (Hsp90) results in the degradation of oncoproteins that
drive malignant progression, inducing cell death, making Hsp90 a target of substantial …

Heat-shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
the stability and function of multiple mutated, chimeric and overexpressed signalling proteins …

Abstract Heat shock protein 90 (HSP90) is a ubiquitously expressed chaperone that is
involved in the posttranslational folding and stability of proteins. Inhibition at the NH2 …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is
required for the stability and function of multiple mutated, chimeric and over-expressed …

Due to the critical role of heat shock protein 90 (HSP90) in regulating the stability, activity
and intracellular sorting of its client proteins involved in multiple oncogenic processes …

Heat-shock protein 90 (HSP90) has diverse functions in mammalian cells. It acts as
molecular chaperone, together with several co-chaperone molecules (such as Hop, Hip …

Heat-shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
stability and function of a growing number of signalling proteins that have been implicated in …

Abstract Heat shock protein 90 (Hsp90) is a ubiquitously expressed molecular chaperone
with ATPase activity involved in the conformational maturation and stability of key signaling …

Hsp90 inhibitors may circumvent the characteristic genetic plasticity that has allowed cancer
cells to eventually evade the toxic effects of most molecularly targeted agents. The …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability
and function of a number of conditionally activated and/or expressed signaling proteins, as …