Title Protein Homeostasis, 2/e
Subtitle
Author Richard I. Morimoto, F. Ulrich Hartl, Jeffery W. Kelly
ISBN 9781621822967
List price USD 135.00
Price outside India Available on Request
Original price
Binding Hardbound
No of pages 552
Book size 178 X 260 mm
Publishing year 2019
Original publisher Cold Spring Harbor Laboratory Press
Published in India by .
Exclusive distributors Viva Books Private Limited
Sales territory India, Sri Lanka, Bangladesh, Pakistan, Nepal, .
Status New Arrival
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Description:

The entire life cycle of a protein—from synthesis and folding to transport and degradation—is carefully controlled by the proteostasis network. This network, consisting of many interconnected pathways and processes, manages protein homeostasis by dynamically responding to the needs of the cell. Stress and aging can challenge the proteostasis network, resulting in the aggregation of misfolded proteins—a feature of numerous neurodegenerative conditions.

Written and edited by experts in the field, this collection from Cold Spring Harbor Perspectives in Biology provides a comprehensive update on how the proteostasis network functions in healthy cells and the diseases that result when protein quality control goes awry. The contributors examine the relevant biochemical attributes of proteins (e.g., solubility), the functions of normal protein aggregates (e.g., biofilm formation in bacteria), and the various heat shock proteins, chaperones, translocation machineries, proteasomes, signaling factors, and transcriptional programs involved in proteostasis. The roles of specific subcellular structures—the endoplasmic reticulum, mitochondria, ribosomes, lysosomes, and cytoplasm—in protein quality control are covered, as is the regulation of proteostasis at the organismal level (e.g., via neuronal activity).

Discussions of the responses by cells when errors in protein quality control occur, the medical disorders that can result (e.g., Alzheimer disease), and pharmacologic approaches to ameliorate protein conformational disorders are also included. This book is therefore an essential reference for biochemists, cell biologists, and all biomedical scientists wishing to understand the pathological consequences of and potential therapies for proteostasis deficiencies in common human diseases.


Contents:

Preface

Chapter 1. Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis (Pietro Sormanni and Michele Vendruscolo)

Chapter 2. Functional Amyloids (Daniel Otzen and Roland Riek)

Chapter 3. The Amyloid Phenomenon and Its Significance in Biology and Medicine (Christopher M. Dobson, Tuomas P.J. Knowles, and Michele Vendruscolo)

Chapter 4. The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum (G. Elif Karagöz, Diego Acosta-Alvear, and Peter Walter)

Chapter 5. Early Events in the Endoplasmic Reticulum Unfolded Protein Response (Steffen Preissler and David Ron)

Chapter 6. Recognition and Degradation of Mislocalized Proteins in Health and Disease (Ramanujan S. Hegde and Eszter Zavodszky)

Chapter 7. Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis (Ryo Ushioda and Kazuhiro Nagata)

Chapter 8. Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational Diseases (Patrick G. Needham, Christopher J. Guerriero, and Jeffrey L. Brodsky)

Chapter 9. Mitochondrial Proteolysis and Metabolic Control (Sofia Ahola, Thomas Langer, and Thomas MacVicar)

Chapter 10. Signaling and Regulation of the Mitochondrial Unfolded Protein Response (Nandhitha Uma Naresh and Cole M. Haynes)

Chapter 11. Functional Modules of the Proteostasis Network (Gopal G. Jayaraj, Mark S. Hipp, and F. Ulrich Hartl)

Chapter 12. Modulation of Amyloid States by Molecular Chaperones (Anne Wentink, Carmen Nussbaum-Krammer, and Bernd Bukau)

Chapter 13. Chaperone Interactions at the Ribosome (Elke Deuerling, Martin Gamerdinger, and Stefan G. Kreft)

Chapter 14. The Proteasome and Its Network: Engineering for Adaptability (Daniel Finley and Miguel A. Prado)

Chapter 15. The Autophagy Lysosomal Pathway and Neurodegeneration (Steven Finkbeiner)

Chapter 16. The Nuclear and DNA-Associated Molecular Chaperone Network (Zlata Gvozdenov, Janhavi Kolhe, and Brian C. Freeman)

Chapter 17. Structure, Function, and Regulation of the Hsp90 Machinery (Maximilian M. Biebl and Johannes Buchner)

Chapter 18. Mechanisms of Small Heat Shock Proteins (Maria K. Janowska, Hannah E.R. Baughman, Christopher N. Woods, and Rachel E. Klevit)

Chapter 19. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase (James Shorter and Daniel R. Southworth)

Chapter 20. Role of Polyphosphate in Amyloidogenic Processes (Justine Lempart and Ursula Jakob)

Chapter 21. Protein Phase Separation as a Stress Survival Strategy (Titus M. Franzmann and Simon Alberti)

Chapter 22. Tailoring of Proteostasis Networks with Heat Shock Factors (Jenny Joutsen and Lea Sistonen)

Chapter 23. Cell-Nonautonomous Regulation of Proteostasis in Aging and Disease (Richard I. Morimoto)

Chapter 24. Proteostasis in Viral Infection: Unfolding the Complex Virus–Chaperone Interplay (Ranen Aviner and Judith Frydman)

Chapter 25. Pharmacologic Approaches for Adapting Proteostasis in the Secretory Pathway to Ameliorate Protein Conformational Diseases (Jeffery W. Kelly)

Chapter 26. A Chemical Biology Approach to the Chaperome in Cancer—HSP90 and Beyond (Tony Taldone, Tai Wang, Anna Rodina, Naga Vara Kishore Pillarsetty, Chander S. Digwal, Sahil Sharma,  Pengrong Yan, Suhasini Joshi, Piyusha P. Pagare, Alexander Bolaender, Gail J. Roboz, Monica L. Guzman, and Gabriela Chiosis)

Chapter 27. Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells (Isabel Lam, Erinc Hallacli, and Vikram Khurana)

Index


Target Audience:

People interested in protein and proteomics; human biology and disease. This book is an essential reference for biochemists, cell biologists, and all biomedical scientists wishing to understand the pathological consequences of and potential therapies for proteostasis deficiencies in common human diseases.

 

 

 
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