The Molecular Chaperones Interaction Networks in Protein Folding and Degradation
(Sprache: Englisch)
Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain...
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Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases.
This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.
Inhaltsverzeichnis zu „The Molecular Chaperones Interaction Networks in Protein Folding and Degradation “
- The Yeast Chaperone Interaction Network- The Interaction Network of the GroEL Chperonin
- The Chaperone Interaction Network of the Hsp70/Hsp40 system
- The Chaperone Interaction Network of Mammalian CCT
- The mammalian Hsp90 Interaction Network
- The interactome of the Hsp90 molecular chaperone machine and the proteome-wide effects of its pharmacological perturbations
- Regulation of the Hsp90 chaperone machinery
- The Interaction Network of the Extracellular Chaperone Clusterin
- Redox homeostasis in the ER
- Chaperoning hydrophobic proteins through the cytosol
- Chaperone networks leading to cotranslational protein degradation
- Chaperones of the ERAD pathway
- The interaction network required for mitochondrial protein homeostasis
- A chaperone network for muscle assembly
- Chaperones and Proteases of the Mitochondrial Matrix
- The ClpXP target substrate network
- Disaggregase functions of the Hsp104 chaperone
- The N-end Rule Pathway of Protein Degradation
- The Biogenesis of the Eukaryotic Proteasome
- Global Overview of the Proteasomal Degradation Pathway
- Systems-wide analysis of protein ubiquitylation
- Network Motifs
- Patterns in the Transcription Factor Regulatory Network in E. coli
- The Organization of Interaction Networks
- The Role of Spatial Protein Quality Control in Aging
- Protein Homeostasis and Aging
- Protein Homeostasis and Neurodegenerative Diseases
- Designing drugs against Hsp90 for cancer therapy
Bibliographische Angaben
- 2014, 2014, XV, 485 Seiten, 54 farbige Abbildungen, Masse: 16,2 x 24,2 cm, Gebunden, Englisch
- Herausgegeben: Walid A. Houry
- Verlag: Springer, Berlin
- ISBN-10: 1493911295
- ISBN-13: 9781493911295
Sprache:
Englisch
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