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The Networking of Chaperones by Co-c...
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Blatch, Gregory Lloyd.
The Networking of Chaperones by Co-chaperones = Control of Cellular Protein Homeostasis /
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
The Networking of Chaperones by Co-chaperones/ edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins.
其他題名:
Control of Cellular Protein Homeostasis /
其他作者:
Blatch, Gregory Lloyd.
面頁冊數:
XV, 276 p. 35 illus., 31 illus. in color.online resource. :
Contained By:
Springer Nature eBook
標題:
Medicine. -
電子資源:
https://doi.org/10.1007/978-3-319-11731-7
ISBN:
9783319117317
The Networking of Chaperones by Co-chaperones = Control of Cellular Protein Homeostasis /
The Networking of Chaperones by Co-chaperones
Control of Cellular Protein Homeostasis /[electronic resource] :edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins. - 1st ed. 2015. - XV, 276 p. 35 illus., 31 illus. in color.online resource. - Subcellular Biochemistry,780306-0225 ;. - Subcellular Biochemistry,71.
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
Standard No.: 10.1007/978-3-319-11731-7doiSubjects--Topical Terms:
644133
Medicine.
LC Class. No.: R-RZ
Dewey Class. No.: 610
The Networking of Chaperones by Co-chaperones = Control of Cellular Protein Homeostasis /
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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.
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