Titlebook: HSF1 and Molecular Chaperones in Biology and Cancer; Marc Laurence Mendillo,David Pincus,Ruth Scherz-Sh Book 2020 Springer Nature Switzerl

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https://doi.org/10.1007/978-1-349-04524-2e Proteostasis Network (PN) are molecular chaperones that serve widely in protein biogenesis under physiological conditions, and prevent protein misfolding and aggregation enhanced by conditions of cellular stress. For Alzheimer’s, Parkinson’s, Huntington’s diseases and ALS, multiple classes of mole

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https://doi.org/10.1007/978-1-349-14942-1 organisms have paved the road to how we currently understand the complex organization of this large family into protein networks. The goal of this chapter is to provide an overview of chaperome networks in cancer cells, with a focus on two cellular states defined by chaperome network organization.

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https://doi.org/10.1057/9780230273979 and barriers imposed by a hostile microenvironment. To achieve this, cancer cells recruit and rewire cells in their microenvironment to become pro-tumorigenic. We propose that chaperones are vital players in this process, and that activation of stress responses helps tumors adapt and evolve into ag

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https://doi.org/10.1057/978-1-137-36238-4he unfolded protein response (UPR). This adaptive response is mediated by the transmembrane signal transducers IRE1, PERK, and ATF6 to decide cell fate of recovery or death. In malignant cells, UPR signalling may be required to maintain ER homeostasis and survival in the tumor microenvironment chara

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The Inexorable Evolution of Financialisationicult to bring to clinical practice, with one major exception: proteasome inhibition. These small molecules have dramatically transformed outcomes for patients with the blood cancer multiple myeloma. However, these agents have failed to make an impact in more common solid tumors. Major questions rem

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