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Heat shock protein HSP90-alpha (HSP90AA1) is a highly conserved and essential molecular chaperone involved in the folding, stabilization, and regulation of a wide array of client proteins, many of which are critical for cell signaling, growth, and survival. It functions as an ATP-dependent chaperone, assisting in protein folding, refolding, and stabilization. HSP90-alpha plays a central role in cancer due to its stabilization of multiple oncogenic signaling molecules, making it a therapeutic target for anti-cancer agents.
Inhibition of ATPase activity, leading to destabilization and degradation of client proteins.
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