The Networking of Chaperones by Co-chaperones : Control of Cellular Protein Homeostasis
The Networking of Chaperones by Co-chaperones : Control of Cellular Protein Homeostasis
edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins
- 1 recurso en línea (XV, 276 p.) 35 ilustraciones, 31 ilustraciones en color
- Subcellular Biochemistry 78 0306-0225 .
- Subcellular Biochemistry 78 .
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.
9783319117317
10.1007/978-3-319-11731-7 doi
Proteínas
Bioquímica
QP551 / .N48 2015 EB
610
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.
9783319117317
10.1007/978-3-319-11731-7 doi
Proteínas
Bioquímica
QP551 / .N48 2015 EB
610