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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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autor Corporativo: SpringerLink (Online service)
Otros Autores: Makarow, Marja (Editor ), Braakman, Ineke (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Berlin, Heidelberg : Springer Berlin Heidelberg : Imprint: Springer, 2006.
Edición:1st ed. 2006.
Colección:Topics in Current Genetics, 16
Temas:
Cytology.
Biochemistry.
Cell Biology.
Acceso en línea:Texto Completo
Tabla de Contenidos:
  • 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.

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