Molecular chaperones in the cell

Author(s)

    • Lund, Peter

Bibliographic Information

Molecular chaperones in the cell

edited by Peter Lund

(Frontiers in molecular biology, 37)

Oxford University Press, 2001

  • : pbk

Available at  / 10 libraries

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Note

Includes bibliographical references and index

Description and Table of Contents

Volume

: pbk ISBN 9780199638673

Description

Interest in molecular chaperones has grown exponentially over the last decade. Molecular Chaperones recognise nascet and unfolded polypeptide chains and are often essential for their folding, proteolytic processing, intracellular targeting, and secretion. They are vital for cell growth, with key roles in processes as diverse as signal transduction and stress survival. Much work has already been done in understanding the structure and function of the major molecular chaperones, and more recently the emphasis in research has shifted towrd exploring their precise roles in many different processes with which they are involved inside the cell. This aspect of molecular chaperone biology is the focus of this book. Here, the field's leading experts synthesise our body of knowledge into succinct chapters, and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins and their breath of definition. This book represents an invaluable summary of the state of research in this fast moving highly important branch of molecular biology, which has ramifications for understanding not only many diverse cellular processes, but also give important insights into diseases such as BSE, CJD, and Alzhemier's disease, which invole protein misfolding.

Table of Contents

  • 1. Cellular functions of Cytosolic E.coli chaperones
  • 2. Chaperones in secretion pathways of E.coli
  • 3. The role of chaperone proteins in the import and assembly of proteins in mitochondria and chloroplasts
  • 4. The roles of the cytosolic chaperone, CCt, in normal eukaryotic cell growth
  • 5. The roles of the major cytoplasmic chaperones in normal eukaryotic cell growth: Hsc70 and its cofactors
  • 6. Hsp70 chaperone networks: the role of regulatory co-chaperones in co-ordinating stress responses with cell growth and death
  • 7. Chaperones in signal transduction
  • 8. Molecular chaperone systems in the endoplasmic reticulum
  • 9. The function of chaperones and proteases in protein quality control and intracellular protein degradation
  • 10. Regulation of expression of molecular chaperones
  • 11. partial unfolding as a precursor to amyloidosis: a discussion of the occurrence, role, and Implications
Volume

ISBN 9780199638680

Description

Molecular chaperones recognize nascent polypeptide chains and are essential for their post-translational modification: folding, proteolytic processing, transport, intracellular targeting, and secretion. They are also implicated in normal cell growth, signal transduction and the cell's response to stress. Much work has already been done in understanding the structure and function of the major molecular chaperones, but the emphasis in research has shifted toward exploring their precise roles in the many different processes with which they are involved inside the cell. This aspect of molecular chaperone biology is the focus of this book. Here, the field's leading experts synthesize our body of knowledge into succinct chapters, and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins and their breadth of definition. This book represents a summary of the state of research in this fast-moving and important branch of molecular biology.

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Details

  • NCID
    BA52740568
  • ISBN
    • 0199638683
    • 0199638675
  • Country Code
    uk
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    Oxford ; New York
  • Pages/Volumes
    xx, 281 p.
  • Size
    25 cm
  • Subject Headings
  • Parent Bibliography ID
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