Chaperones
Molecular chaperones interact with virtually every newly synthesized protein. Their role is not limited to this, as an increasing number of protein-protein interactions are found to be mediated by molecular chaperones. They reside in large complexes, in every cellular compartment, and to some extent...
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| Other Authors: | , |
| Format: | Electronic eBook |
| Language: | English |
| Published: |
Berlin, Heidelberg :
Springer Berlin Heidelberg : Imprint: Springer,
2006.
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| Edition: | 1st ed. 2006. |
| Series: | Topics in Current Genetics,
16 |
| Subjects: | |
| Online Access: | https://doi.org/10.1007/b100697 |
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Table of Contents:
- Regulation of the Heat Shock Response by Heat Shock Transcription Factors
- The Unfolded Protein Response Unfolds
- Hsp104p: A Protein Disaggregase
- Folding of Newly Synthesised Proteins in the Endoplasmic Reticulum
- Quality Control of Proteins in the Mitochondrion
- Chaperone Proteins and Peroxisomal Protein Import
- Proteasomal Degradation of Misfolded Proteins
- Template-induced Protein Misfolding Underlying Prion Diseases
- The Hsp60 Chaperonins from Prokaryotes and Eukaryotes.