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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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書目名稱HSF1 and Molecular Chaperones in Biology and Cancer
編輯Marc Laurence Mendillo,David Pincus,Ruth Scherz-Sh
視頻videohttp://file.papertrans.cn/421/420330/420330.mp4
概述This volume details how the proteostasis network– the systems of the cell that synthesize, fold, and degrade cellular proteins– functions to impact the tumor ecosystem.Brings together an extraordinary
叢書名稱Advances in Experimental Medicine and Biology
圖書封面Titlebook: HSF1 and Molecular Chaperones in Biology and Cancer;  Marc Laurence Mendillo,David Pincus,Ruth Scherz-Sh Book 2020 Springer Nature Switzerl
描述.Protein homeostasis, or “Proteostasis”, lies at the heart of human health and disease. From the folding of single polypeptide chains into functional proteins, to the regulation of intracellular signaling pathways, to the secreted signals that coordinate cells in tissues and throughout the body, the proteostasis network operates to support cell health and physiological fitness. However, cancer cells also hijack the proteostasis network and many of these same processes to sustain the growth and spread of tumors..The chapters in this book are written by world experts in the many facets of the proteostasis network. They describe cutting-edge insights into the structure and function of the major chaperone and degradation systems in healthy cells and how these systems are co-opted in cancer cells and the cells of the tumor microenvironment. The chapters also cover therapeutic interventions such as the?FDA-approved proteasome inhibitors Velcade and Krypolis as well as other therapies currently under?clinical investigation to disarm the ability of the proteostasis network to support malignancy. This compendium is the first of its kind and aims to serve as a reference manual for active inv
出版日期Book 2020
關(guān)鍵詞chaperones; cancer; HSF1; Hsp40/Hsp70; Hsp90; tumor microenvironment; Proteomics; Protein Structure
版次1
doihttps://doi.org/10.1007/978-3-030-40204-4
isbn_softcover978-3-030-40206-8
isbn_ebook978-3-030-40204-4Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightSpringer Nature Switzerland AG 2020
The information of publication is updating

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Book 2020proteins, to the regulation of intracellular signaling pathways, to the secreted signals that coordinate cells in tissues and throughout the body, the proteostasis network operates to support cell health and physiological fitness. However, cancer cells also hijack the proteostasis network and many o
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https://doi.org/10.1007/978-1-349-13445-8the various members of this network. In this chapter we describe the emerging working principles of the Hsp70 machine and its co-chaperones, and highlight how mechanistic aspects of this network are tied to distinct protein folding functions.
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https://doi.org/10.1007/978-3-031-05017-6 from Hsf1, releasing Hsf1 to induce the full arsenal of cellular chaperones to restore protein homeostasis. In metazoans, this cell-autonomous feedback loop is modulated by the microenvironment and neuronal cues to enable tissue-level and organism-wide coordination.
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https://doi.org/10.1057/9780230273979ancer-cell-autonomous activity of chaperones in human patients and mouse models of cancer, discuss the mechanisms by which this non-cell-autonomous activity is mediated and provide an evolutionary perspective on the basis of this phenomenon.
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