Titlebook: Heat Shock Protein 90 in Human Diseases and Disorders; Alexzander A. A. Asea,Punit Kaur Book 2019 Springer Nature Switzerland AG 2019 Immu

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p53-Hsp90 Axis in Human Cancer folding and functions of a variety of oncogenic clients. Hsp90 is up-regulated in response to cellular stresses that cancer cells encounter, such as heat, hypoxia and nutrient deprivation, conditions commonly associated with the tumor microenvironment. P53 is the tumor suppressor gene that is mutat

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Targeting Hsp-90 Related Disease Entities for Therapeutic Developmenteat effort has been expended in the development of specific inhibitors of the N-terminal and C-terminal domains. Inhibitors of post-translational modification have also been developed. Herein, we explore the available inhibitors and those in development, discuss the relevant disease processes, and e

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Hsp90 and Its Role in Heme-Maturation of Client Proteins: Implications for Human Diseasesate heme and become active, but knowledge of this essential cellular process remains incomplete. However recent studies on chaperon Hsp90 has revealed that it drives functional heme insertion in vital hemeproteins like inducible nitric oxide synthase (iNOS), soluble guanylate cyclase (sGC) and hemog

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Moonlighting Functions of Heat Shock Protein 90of co-chaperones. Its functions in folding, stabilizing, assembling and disassembling proteins and complexes that are involved in many key processes in the cell, including antigen cross-presentation, stabilization of the cytoskeleton, signaling pathways, stabilization of steroid receptors and other

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