Wanping Xu

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Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of several conditionally activated and/or expressed signaling proteins as well as multiple mutated, chimeric, and/or overexpressed signaling proteins, which promote cancer cell growth and/or survival (see the Web site 1 maintained by D. Picard for an up-to-date(More)
The stability and activity of numerous signaling proteins in both normal and cancer cells depends on the dimeric molecular chaperone heat shock protein 90 (Hsp90). Hsp90's function is coupled to ATP binding and hydrolysis and requires a series of conformational changes that are regulated by cochaperones and numerous posttranslational modifications (PTMs).(More)
Heat shock protein 90 (Hsp90) is an essential molecular chaperone in eukaryotes that facilitates the conformational maturation and function of a diverse protein clientele, including aberrant and/or over-expressed proteins that are involved in cancer growth and survival. A role for Hsp90 in supporting the protein homeostasis of cancer cells has buoyed(More)
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