` Error: this shopping cart has already been submitted and been approved Protein Homeostasis, Second Edition
   

Click to Enlarge

Protein Homeostasis, Second Edition


Book Series:  A Cold Spring Harbor Perspectives in Biology Collection
Subject Area(s):  Proteins and ProteomicsHuman Biology and Disease

Edited by Richard I. Morimoto, Northwestern University; F. Ulrich Hartl, Max Planck Institute of Biochemistry; Jeffery W. Kelly, The Scripps Research Institute

Download a Free Excerpt from Protein Homeostasis, Second Edition:

Preface
Functional Modules of the Proteostasis Network
Index


© 2019 • 552 pages, illustrated (109 color and 2 B&W), index
Hardcover • $135 94.50
ISBN  978-1-621822-96-7
You save: 30%
You will receive free shipping on this item at checkout.
Free shipping offer applies to direct website purchases by individual U.S. and Canada customers only.

Print Book + eBook
    Best value!
$210 $121.50 Add To Cart
Print Book$135 $94.50 Add To Cart
eBook$75 $60.00 Add To Cart

Bulk discounts available for your lab or class. Click here to inquire.

eBooks use Adobe Digital Editions software. Click here for more information.

  •     Description    
  •     Contents    

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
Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis
Pietro Sormanni and Michele Vendruscolo
Functional Amyloids
Daniel Otzen and Roland Riek
The Amyloid Phenomenon and Its Significance in Biology and Medicine
Christopher M. Dobson, Tuomas P.J. Knowles, and Michele Vendruscolo
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
Early Events in the Endoplasmic Reticulum Unfolded Protein Response
Steffen Preissler and David Ron
Recognition and Degradation of Mislocalized Proteins in Health and Disease
Ramanujan S. Hegde and Eszter Zavodszky
Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis
Ryo Ushioda and Kazuhiro Nagata
Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational Diseases
Patrick G. Needham, Christopher J. Guerriero, and Jeffrey L. Brodsky
Mitochondrial Proteolysis and Metabolic Control
Sofia Ahola, Thomas Langer, and Thomas MacVicar
Signaling and Regulation of the Mitochondrial Unfolded Protein Response
Nandhitha Uma Naresh and Cole M. Haynes
Functional Modules of the Proteostasis Network
Gopal G. Jayaraj, Mark S. Hipp, and F. Ulrich Hartl
Modulation of Amyloid States by Molecular Chaperones
Anne Wentink, Carmen Nussbaum-Krammer, and Bernd Bukau
Chaperone Interactions at the Ribosome
Elke Deuerling, Martin Gamerdinger, and Stefan G. Kreft
The Proteasome and Its Network: Engineering for Adaptability
Daniel Finley and Miguel A. Prado
The Autophagy Lysosomal Pathway and Neurodegeneration
Steven Finkbeiner
The Nuclear and DNA-Associated Molecular Chaperone Network
Zlata Gvozdenov, Janhavi Kolhe, and Brian C. Freeman
Structure, Function, and Regulation of the Hsp90 Machinery
Maximilian M. Biebl and Johannes Buchner
Mechanisms of Small Heat Shock Proteins
Maria K. Janowska, Hannah E.R. Baughman, Christopher N. Woods, and Rachel E. Klevit
Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase
James Shorter and Daniel R. Southworth
Role of Polyphosphate in Amyloidogenic Processes
Justine Lempart and Ursula Jakob
Protein Phase Separation as a Stress Survival Strategy
Titus M. Franzmann and Simon Alberti
Tailoring of Proteostasis Networks with Heat Shock Factors
Jenny Joutsen and Lea Sistonen
Cell-Nonautonomous Regulation of Proteostasis in Aging and Disease
Richard I. Morimoto
Proteostasis in Viral Infection: Unfolding the Complex Virus–Chaperone Interplay
Ranen Aviner and Judith Frydman
Pharmacologic Approaches for Adapting Proteostasis in the Secretory Pathway to Ameliorate Protein Conformational Diseases
Jeffery W. Kelly
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
Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells
Isabel Lam, Erinc Hallacli, and Vikram Khurana
Index