The Networking of Chaperones by Co-chaperones Control of Cellular Protein Homeostasis /
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 molecul...
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| Other Authors: | , |
| Format: | Electronic eBook |
| Language: | English |
| Published: |
Cham :
Springer International Publishing : Imprint: Springer,
2015.
|
| Edition: | 1st ed. 2015. |
| Series: | Subcellular Biochemistry,
78 |
| Subjects: | |
| Online Access: | https://doi.org/10.1007/978-3-319-11731-7 |
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| 001 | 978-3-319-11731-7 | ||
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| 245 | 1 | 4 | |a The Networking of Chaperones by Co-chaperones |h [electronic resource] : |b Control of Cellular Protein Homeostasis / |c edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins. |
| 250 | |a 1st ed. 2015. | ||
| 264 | 1 | |a Cham : |b Springer International Publishing : |b Imprint: Springer, |c 2015. | |
| 300 | |a XV, 276 p. 35 illus., 31 illus. in color. |b online resource. | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
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| 490 | 1 | |a Subcellular Biochemistry, |x 0306-0225 ; |v 78 | |
| 505 | 0 | |a 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. | |
| 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. | ||
| 650 | 0 | |a Medicine. | |
| 650 | 0 | |a Life sciences. | |
| 650 | 0 | |a Biochemistry. | |
| 650 | 1 | 4 | |a Biomedicine, general. |0 https://scigraph.springernature.com/ontologies/product-market-codes/B0000X |
| 650 | 2 | 4 | |a Life Sciences, general. |0 https://scigraph.springernature.com/ontologies/product-market-codes/L00004 |
| 650 | 2 | 4 | |a Biochemistry, general. |0 https://scigraph.springernature.com/ontologies/product-market-codes/L14005 |
| 700 | 1 | |a Blatch, Gregory Lloyd. |e editor. |4 edt |4 http://id.loc.gov/vocabulary/relators/edt | |
| 700 | 1 | |a Edkins, Adrienne Lesley. |e editor. |4 edt |4 http://id.loc.gov/vocabulary/relators/edt | |
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| 830 | 0 | |a Subcellular Biochemistry, |x 0306-0225 ; |v 78 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/978-3-319-11731-7 |
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