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    Proteostasis and Chaperone Surveillance

    Proteostasis and Chaperone Surveillance by Singh, Laishram Rajendrakumar; Dar, Tanveer Ali; Ahmad, Parvaiz;

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      • Publisher's listprice EUR 106.99
      • The price is estimated because at the time of ordering we do not know what conversion rates will apply to HUF / product currency when the book arrives. In case HUF is weaker, the price increases slightly, in case HUF is stronger, the price goes lower slightly.

        45 385 Ft (43 223 Ft + 5% VAT)
      • Discount 8% (cc. 3 631 Ft off)
      • Discounted price 41 753 Ft (39 765 Ft + 5% VAT)

    45 385 Ft

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    Product details:

    • Edition number Softcover reprint of the original 1st ed. 2015
    • Publisher Springer
    • Date of Publication 23 August 2016
    • Number of Volumes 1 pieces, Previously published in hardcover

    • ISBN 9788132234548
    • Binding Paperback
    • No. of pages180 pages
    • Size 254x178 mm
    • Weight 3714 g
    • Language English
    • Illustrations 9 Illustrations, black & white; 17 Illustrations, color
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    Short description:

    Proteostasis is central to the development of various human diseases caused due to excessive protein misfolding and the disregulation of the protein quality control system. In this book, respected researchers from many leading institutions contribute their insights on proteostasis maintenance. The coverage mainly focuses on the basics of maintaining proteostasis, the consequences of proteostatic system failure, and how chaperone systems constantly maintain proteostasis. In addition, the book presents in detail different treatment strategies for diseases caused by proteostatic system failure, as well as the inhibition of proteostatic failure using small molecule compounds. It examines advances in the modulation of proteopathies, providing a comprehensive source of key mechanistic insights on these diseases. As such, the book offers a valuable resource for beginners and more experienced investigators alike who are looking for detailed and reliable information on protein homeostasis, the diseases that can develop due to related imbalances, and the essential role of molecular and chemical chaperones.

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    Long description:

    Proteostasis is central to the development of various human diseases caused due to excessive protein misfolding and the disregulation of the protein quality control system. In this book, respected researchers from many leading institutions contribute their insights on proteostasis maintenance. The coverage mainly focuses on the basics of maintaining proteostasis, the consequences of proteostatic system failure, and how chaperone systems constantly maintain proteostasis. In addition, the book presents in detail different treatment strategies for diseases caused by proteostatic system failure, as well as the inhibition of proteostatic failure using small molecule compounds. It examines advances in the modulation of proteopathies, providing a comprehensive source of key mechanistic insights on these diseases. As such, the book offers a valuable resource for beginners and more experienced investigators alike who are looking for detailed and reliable information on protein homeostasis, the diseases that can develop due to related imbalances and the essential role of molecular and chemical chaperones.

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    Table of Contents:

    Part 1: Maintaining Proteostasis.- 1. Structural Allostery and Protein-Protein Interactions of Sin3.- 2. Protein Posttranslational Modifications: Role in Protein Structure, Function and Stability.- 3. Protein Folding and Aggregation: A revisit of basic conception.- Part 2: Proteopathy: Failure of proteostasis.- 4. Protein Folding: From Normal Cellular Function to Pathophysiology.- 5. Protein Misfolding Diseases: In perspective of Gain and loss-of-function.- 6. Amyloid formation in Alzheimer?s disease.- 7. Advances in modulation of Proteopathies, the devil spread from head to toe.- Part 3: Chaperone surveillance of proteopathy.- 8. Small Molecule Osmolytes can Modulate Proteostasis.- 9. Pharmacological Chaperones in Protein Aggregation Disorders.

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