The Networking of Chaperones by Co-Chaperones
The Networking of Chaperones by Co-Chaperones [electronic resource] /
edited by Adrienne L. Edkins, Gregory L. Blatch.
- 3rd ed. 2023.
- XV, 429 p. 53 illus., 46 illus. in color. online resource.
- Subcellular Biochemistry, 101 2542-8810 ; .
- Subcellular Biochemistry, 101 .
Acceso multiusuario
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.
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 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. .
9783031147401
Protein folding.
Proteins .
Post-translational modification.
Cytology.
Biomolecules.
Physical biochemistry.
Macromolecules.
Protein Folding.
Protein Biochemistry.
Post-translational Modifications.
Cell Biology.
Structural Biology.
QP551-552 QD431.25.S85
572.633
Acceso multiusuario
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.
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 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. .
9783031147401
Protein folding.
Proteins .
Post-translational modification.
Cytology.
Biomolecules.
Physical biochemistry.
Macromolecules.
Protein Folding.
Protein Biochemistry.
Post-translational Modifications.
Cell Biology.
Structural Biology.
QP551-552 QD431.25.S85
572.633
