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Molecular Chaperones of the Endoplasmic Reticulum
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Authors: Martin Schröder (Durham University, Durham, United Kingdom) 
Book Description:
An important function of the endoplasmic reticulum is the folding of newly synthesized polypeptide chains. Several general and specialized chaperones operate in the endoplasmic reticulum to assist protein folding. This book reviews our current knowledge of molecular chaperones of the ER, including the HSP70 class chaperones BiP and GRP170, their DnaJ and GrpE co-chaperones, the HSP90 class chaperone GRP94, and the lectin chaperones calnexin, calmegin, and calreticulin. This book provides an overview of the biochemistry and physical chemistry of molecular chaperones with emphasis on molecular chaperones of the endoplasmic reticulum.

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Table of Contents:
Preface

Chapter 1. Introduction, pp. 1-7

Chapter 2. Physicochemical Principles Governing Protein Folding, pp. 9-13

Chapter 3. The ER, pp. 15-21

Chapter 4. Molecular Chaperones of the ER, pp. 23-65

Chapter 5. Conclusion, pp. 67-68

Acknowledgments pp.69-70

References pp.71-126

   Series:
      Protein Science and Engineering
   Binding: Softcover
   Pub. Date: 2010
   Pages: 126.pp
   ISBN: 978-1-61668-173-9
   Status: AV
  
Status Code Description
AN Announcing
FM Formatting
PP Page Proofs
FP Final Production
EP Editorial Production
PR At Prepress
AP At Press
AV Available
  
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Molecular Chaperones of the Endoplasmic Reticulum