The Networking of Chaperones by Co-chaperones (2^nd Ed., Softcover reprint of the original 1st ed. 2015) Control of Cellular Protein Homeostasis Subcellular Biochemistry Series, Vol. 78

Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.

Preface
List of Contributors
About the Editors
1
GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones
Andreas Bracher and Jacob Verghese

2
Functions of the Hsp90-Binding FKBP Immunophilins
Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox

3
Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins
Swati Baindur-Hudson, Adrienne L. Edkins, and Gregory L. Blatch

4
 Specification of Hsp70 function by Type I and Type II Hsp40
Douglas M. Cyr and Carlos H. Ramos

5
Cdc37 as a Co-chaperone to Hsp90
Stuart K Calderwood

6
p23 and Aha1
Alexandra B Rehn and Johannes Buchner

7
UCS proteins: chaperones for myosin and co-chaperones for Hsp90
Weiming Ni and Odutayo O. Odunuga

8
Chaperonin - Co-chaperonin Interactions
Aileen Boshoff

9
 Co-chaperones of the mammalian endoplasmic reticulum
Armin Melnyk, Heiko Rieger and Richard Zimmermann

10
The evolution and function of co-chaperones in mitochondriaNeta Regev-Rudzki, Kip Gabriel and Dejan Bursać

11
CHIP: a co-chaperone for degradation by the proteasome
Adrienne L. Edkins

12
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease
Emma J. Duncan, Michael E. Cheetham, J. Paul Chapple, and Jacqueline van der Spuy

Index

This is the only book that specifically reviews the knowledge on co-chaperones as opposed to chaperones

Excellent information resource for researchers entering the specialized field of cell stress and chaperones

Excellent information resource for researchers in the broader field of diseases related to protein folding (e.g. Alzheimers)

Includes supplementary material: sn.pub/extras