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The networking of chaperones by co-chaperones = control of cellular protein homeostasis /

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The networking of chaperones by co-chaperones/ edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins.
Reminder of title:	control of cellular protein homeostasis /
other author:	Blatch, Gregory Lloyd.
Published:	Cham :Springer International Publishing : : 2015.,
Description:	xv, 276 p. :ill. (some col.), digital ; : 24 cm.;
Contained By:	Springer eBooks
Subject:	Molecular chaperones. -
Online resource:	http://dx.doi.org/10.1007/978-3-319-11731-7
ISBN:	9783319117317 (electronic bk.)

The networking of chaperones by co-chaperones = control of cellular protein homeostasis /
The networking of chaperones by co-chaperonescontrol of cellular protein homeostasis /[electronic resource] :edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins. - Cham :Springer International Publishing :2015. - xv, 276 p. :ill. (some col.), digital ;24 cm. - Subcellular biochemistry,v.780306-0225 ;. - Subcellular biochemistry ;65.

Preface -- List of Contributors- About the Editors- GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones -- Functions of the Hsp90-Binding FKBP Immunophilins -- Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins -- Specification of Hsp70 function by Type I and Type II Hsp40 -- Cdc37 as a Co-chaperone to Hsp90 -- p23 and Aha1- UCS proteins: chaperones for myosin and co-chaperones for Hsp90 -- Chaperonin - Co-chaperonin Interactions -- Co-chaperones of the mammalian endoplasmic reticulum -- The evolution and function of co-chaperones in mitochondria -- CHIP: a co-chaperone for degradation by the proteasome -- The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease -- Index.

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.

ISBN: 9783319117317 (electronic bk.)

Standard No.: 10.1007/978-3-319-11731-7doiSubjects--Topical Terms:

882817
Molecular chaperones.

LC Class. No.: QP552.M64

Dewey Class. No.: 572.6

The networking of chaperones by co-chaperones = control of cellular protein homeostasis /
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520 $a 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.
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