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Cell Stress Proteins

  • Book
  • © 2007

Overview

Editors:
  1. Stuart K. Calderwood

    1. Department of Radiation Oncology, Harbard Medical School, Beth, Israel
      Deaconess Medical Center, Boston

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

  • Provides overview of the diversity and complex evolutionary history of cell stress proteins

Part of the book series: Protein Reviews (PRON, volume 7)

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Table of contents (19 chapters)

  1. Front Matter

    Pages i-xv
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  2. Introduction: Heat Shock Proteins—From Drosophila Stress Proteins to Mediators of Human Disease

    1. Introduction: Heat Shock Proteins—From Drosophila Stress Proteins to Mediators of Human Disease

      • Stuart K. Calderwood
      Pages 1-4

  3. Stress Response and Molecular Chaperones

    1. Front Matter

      Pages 5-5
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    2. Biology of the Heat Shock Response and Stress Conditioning

      • George A. Perdrizet, Michael J. Rewinski, Emily J. Noonan, Lawrence E. Hightower
      Pages 7-35

    3. Bacterial Stress Sensors

      • Wolfgang Schumann
      Pages 36-56

    4. Unfolded Protein Response: Contributions to Development and Disease

      • Nan Liao, Linda M. Hendershot
      Pages 57-88

  4. Molecular Mechanisms of Stress Protein Expression

    1. Front Matter

      Pages 89-89
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    2. Genetic Models of HSF Function

      • András Orosz, Ivor J. Benjamin
      Pages 91-121

    3. HSF1 and HSP Gene Regulation

      • Richard Voellmy
      Pages 122-139

  5. Cellular Stress Proteins

    1. Front Matter

      Pages 141-141
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    2. Small Heat Shock Proteins in Physiological and Stress-Related Processes

      • Diana Orejuela, Anne Bergeron, Geneviève Morrow, Robert M. Tanguay
      Pages 143-177

    3. Large Mammalian hsp70 Family Proteins, hsp110 and grp170, and Their Roles in Biology and Cancer Therapy

      • Xiang-Yang Wang, Douglas P. Easton, John R. Subjeck
      Pages 178-205

  6. Molecular Chaperones and Protein Folding

    1. Front Matter

      Pages 207-207
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    2. Regulation of Hsp70 Function: Hsp40 Co-Chaperones and Nucleotide Exchange Factors

      • Robert T. Youker, Jeffrey L. Brodsky
      Pages 209-227

    3. Protein Disassembly by Hsp40-Hsp70

      • Samuel J. Landry
      Pages 228-254

    4. Mammalian HSP40/DnaJ Chaperone Proteins in Cytosol

      • Kazutoyo Terada, Masataka Mori
      Pages 255-277

  7. Role of Molecular Chaperones in Cell Regulation

    1. Front Matter

      Pages 279-279
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    2. FKBP Co-Chaperones in Steroid Receptor Complexes

      • Joyce Cheung-Flynn, Sean P. Place, Marc B. Cox, Viravan Prapapanich, David F. Smith
      Pages 281-312

    3. Up and Down Regulation of the Stress Response by the Co-Chaperone Ubiquitin Ligase CHIP

      • Shu-Bing Qian, Cam Patterson
      Pages 313-325

    4. Role of Cdc37 in Protein Kinase Folding

      • Atin K. Mandal, Devi M. Nair, Avrom J. Caplan
      Pages 326-337
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Keywords

About this book

Stressproteinssuchastheheatshockproteins(Hsp)andglucose-regulatedproteins (Grp) are front-line molecules in responses to cellular insult and play key roles in the viability of single cell organisms exposed to environmental stresses. However, the discovery of the roles of Hsp and Grp as molecular chaperones indicates much wider functions in the physiology of cells and organisms. It is now clear that some stress proteins are expressed constitutively and are key mediators of housekeeping protein folding in the day-to-day existence of the cell. The maturation of enzymes, transcriptionfactors,andcellsurfacereceptorsreliesonthesefunctionsofthestress proteins. In addition, the ability of stress proteins to manipulate the structures of target proteins has lent them cell regulatory properties over and above their role in folding the proteome and they play key roles in controlling signal transduction, cell death pathways and transcription. Recently, novel extracellular roles for the Hsp have also emerged as it has become apparent that the Hsp can escape from the cytoplasm of cells and play a signi?cant extracellular role in signaling to neighbor cells and in immunosurveiIlance. As might be expected with such key molecules, dysregulation of Hsp expression over time can lead to disastrous results in terms of the health of the organism. Under-expression of the Hsp is associated with advanced aging and neurodegeneration. Elevated expression is associated with malignant progression. We have aimed in this volume to indicate advances in each oftheseaspectsofstressproteinresearch,withchaptersrangingfrombasicstudies of the role of Hsp in protein folding to reviews examining the breakdown of stress protein regulation in disease. Stuart K.

Editors and Affiliations

  • Department of Radiation Oncology, Harbard Medical School, Beth, Israel

    Stuart K. Calderwood

  • Deaconess Medical Center, Boston

    Stuart K. Calderwood

Bibliographic Information

  • Book Title: Cell Stress Proteins

  • Editors: Stuart K. Calderwood

  • Series Title: Protein Reviews

  • DOI: https://doi.org/10.1007/978-0-387-39717-7

  • Publisher: Springer New York, NY

  • eBook Packages: Biomedical and Life Sciences, Biomedical and Life Sciences (R0)

  • Copyright Information: Springer-Verlag New York 2007

  • Hardcover ISBN: 978-0-387-39714-6Published: 03 May 2007

  • Softcover ISBN: 978-1-4419-2291-5Published: 25 November 2010

  • eBook ISBN: 978-0-387-39717-7Published: 13 February 2009

  • Edition Number: 1

  • Number of Pages: XVI, 460

  • Number of Illustrations: 27 b/w illustrations, 11 illustrations in colour

  • Topics: Protein Science, Microbiology, Immunology, Biochemistry, general

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