Chaperones 16 /
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...
Συγγραφή απο Οργανισμό/Αρχή: | |
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Άλλοι συγγραφείς: | |
Μορφή: | Ηλεκτρονική πηγή Ηλ. βιβλίο |
Γλώσσα: | English |
Έκδοση: |
Berlin, Heidelberg :
Springer Berlin Heidelberg,
2006.
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Σειρά: | Topics in Current Genetics,
16 |
Θέματα: | |
Διαθέσιμο Online: | Full Text via HEAL-Link |
Πίνακας περιεχομένων:
- 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.