The molecular chaperones interaction networks in protein folding and degradation [electronic resource] / Walid A. Houry, editor.
Houry, Walid A., editor.
2014
QP552.M64
Available Online

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Title The molecular chaperones interaction networks in protein folding and degradation [electronic resource] / Walid A. Houry, editor.
ISBN 9781493911301 electronic book
1493911309 electronic book
9781493911295
DOI https://doi.org/10.1007/978-1-4939-1130-1
Published New York, NY : Springer, [2014]
Copyright ©2014
Language English
Description 1 online resource (xv, 485 pages) : illustrations.
Item Number 10.1007/978-1-4939-1130-1 doi
Call Number QP552.M64
Dewey Decimal Classification 572/.6
Summary Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.
Note Includes index.
Bibliography, etc. Note Includes bibliographical references at the end of each chapters and index.
Access Note Access limited to authorized users.
Source of Description Online resource; title from PDF title page (SpringerLink, viewed September 18, 2014).
Added Author Houry, Walid A., editor.
Series Interactomics and systems biology.
Available in Other Form Print version: 9781493911295
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Part I: Global View of the Chaperone Network
Analysis of Chaperone Network Throughput
Part II: Chaperones at the Ribosome
Functions of Ribosome-associated Chaperones and Their Interaction Network
Part III: The Hsp 70 and Hsp40 Chaperone Networks
Yeast Hsp70 and J-protein Chaperones: Function and Interaction Network
The Chaperone Networks: An Hsp70 Perspective
Part IV: The Hsp90 Chaperone Network
The Interaction Network of the Hsp90 Molecular Chaperone
A Global View of the Proteome Perturbations by Hsp90 Inhibitors
Designing Drugs Against Hsp90 for Cancer Therapy
The Candida albicans Hsp90 Chaperone Network is Environmentally Flexible and Evolutionarily Divergent
Part V: The p23 Chaperone Network
Emergence and Characterization of the p23 Molecular Chaperone
Part VI: Chaperones in the ER: Function and Interaction Network
Chaperones of the ERAD Pathway
Chaperones and Proteases of Mitochondria: From Protein Folding and Degradation to Mitophagy
Part VII: The Ubiquitin-Proteasome System Network
The Biogenesis of the Eukaryotic Proteasome
Systems-wide Analysis of Protein Ubiquitylation: We Finally Have the Tiger by the Tail
Part VIII: The Chaperone and Protease Networks in Model Bacteria and Parasites
The Interaction Networks of E. coli Chaperones
Chaperone-Proteases of Mycobacteria
The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites
Index.

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