The Networking of Chaperones by Co-Chaperones
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time. This third edition of the book The N...
Wedi'i Gadw mewn:
| Awdur Corfforaethol: | |
|---|---|
| Awduron Eraill: | , |
| Fformat: | Electronig eLyfr |
| Iaith: | Saesneg |
| Cyhoeddwyd: |
Cham :
Springer International Publishing : Imprint: Springer,
2023.
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| Rhifyn: | 3rd ed. 2023. |
| Cyfres: | Subcellular Biochemistry,
101 |
| Pynciau: | |
| Mynediad Ar-lein: | https://doi.org/10.1007/978-3-031-14740-1 |
| Tagiau: |
Ychwanegu Tag
Dim Tagiau, Byddwch y cyntaf i dagio'r cofnod hwn!
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MARC
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| 245 | 1 | 4 | |a The Networking of Chaperones by Co-Chaperones |h [electronic resource] / |c edited by Adrienne L. Edkins, Gregory L. Blatch. |
| 250 | |a 3rd ed. 2023. | ||
| 264 | 1 | |a Cham : |b Springer International Publishing : |b Imprint: Springer, |c 2023. | |
| 300 | |a XV, 429 p. 53 illus., 46 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 | ||
| 341 | 0 | |b Table of contents navigation |2 onix | |
| 341 | 0 | |b Single logical reading order |2 onix | |
| 341 | 0 | |b Short alternative textual descriptions |2 onix | |
| 341 | 0 | |b Use of color is not sole means of conveying information |2 onix | |
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| 347 | |a text file |b PDF |2 rda | ||
| 490 | 1 | |a Subcellular Biochemistry, |x 2542-8810 ; |v 101 | |
| 505 | 0 | |a Chapter 1: GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones -- Chapter 2: Functions of the Hsp90-Binding FKBP Immunophilins -- Chapter 3: Hsp70/Hsp90 organising protein (Hop): coordinating much more than chaperones -- Chapter 4: Specification of Hsp70 function by Hsp40 Co-Chaperones -- Chapter 5: Cdc37 as a Co-chaperone to Hsp90 -- Chapter 6: p23 and Aha1 – Distinct functions promote client maturation -- Chapter 7: Beyond chaperoning: UCS proteins emerge as regulators of myosin-mediated cellular processes -- Chapter 8: Chaperonin - Co-Chaperonin Interactions -- Chapter 9: Co-chaperones of the human endoplasmic reticulum: an update -- Chapter 10: J Domain Proteins Orchestrate the Multifunctionality of Hsp70s in Mitochondria: Insights from Mechanistic and Evolutionary Analyses -- Chapter 11: Impact of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity -- Chapter 12: CHIP: a co-chaperone for degradation by the proteasome and lysosome -- Chapter 13: HSP70-HSP90 chaperone networking in protein misfolding disease. | |
| 520 | |a Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time. This third edition of the book The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by co-chaperones, a diverse cohort of non-client proteins. Since the second edition was released, not only has knowledge deepened on how co-chaperones act as nodes to network and functionalise chaperones, but an understanding of their broader biological function has started to emerge. The third edition provides new and updated chapters highlighting recent developments and emerging themes on co-chaperones, such as their extracellular functions, their role in human disease and their status as putative drug targets. The book is a useful resourcefor 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. . | ||
| 532 | 8 | |a Accessibility summary: This PDF does not fully comply with PDF/UA standards, but does feature limited screen reader support, described non-text content (images, graphs), bookmarks for easy navigation and searchable, selectable text. Users of assistive technologies may experience difficulty navigating or interpreting content in this document. We recognize the importance of accessibility, and we welcome queries about accessibility for any of our products. If you have a question or an access need, please get in touch with us at accessibilitysupport@springernature.com. | |
| 532 | 8 | |a No reading system accessibility options actively disabled | |
| 532 | 8 | |a Publisher contact for further accessibility information: accessibilitysupport@springernature.com | |
| 650 | 0 | |a Protein folding. | |
| 650 | 0 | |a Proteins . | |
| 650 | 0 | |a Post-translational modification. | |
| 650 | 0 | |a Cytology. | |
| 650 | 0 | |a Biomolecules. | |
| 650 | 0 | |a Physical biochemistry. | |
| 650 | 0 | |a Macromolecules. | |
| 650 | 1 | 4 | |a Protein Folding. |
| 650 | 2 | 4 | |a Protein Biochemistry. |
| 650 | 2 | 4 | |a Post-translational Modifications. |
| 650 | 2 | 4 | |a Cell Biology. |
| 650 | 2 | 4 | |a Structural Biology. |
| 700 | 1 | |a Edkins, Adrienne L. |e editor. |0 (orcid)0000-0002-3615-6651 |1 https://orcid.org/0000-0002-3615-6651 |4 edt |4 http://id.loc.gov/vocabulary/relators/edt | |
| 700 | 1 | |a Blatch, Gregory L. |e editor. |4 edt |4 http://id.loc.gov/vocabulary/relators/edt | |
| 710 | 2 | |a SpringerLink (Online service) | |
| 773 | 0 | |t Springer Nature eBook | |
| 776 | 0 | 8 | |i Printed edition: |z 9783031147395 |
| 776 | 0 | 8 | |i Printed edition: |z 9783031147418 |
| 776 | 0 | 8 | |i Printed edition: |z 9783031147425 |
| 830 | 0 | |a Subcellular Biochemistry, |x 2542-8810 ; |v 101 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/978-3-031-14740-1 |
| 912 | |a ZDB-2-SBL | ||
| 912 | |a ZDB-2-SXB | ||
| 950 | |a Biomedical and Life Sciences (SpringerNature-11642) | ||
| 950 | |a Biomedical and Life Sciences (R0) (SpringerNature-43708) | ||