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Chaperones : 16 /

Contributor(s): Braakman, Ineke [editor.] | SpringerLink (Online service).
Material type: materialTypeLabelBookSeries: Topics in Current Genetics: 16Publisher: Berlin, Heidelberg : Springer Berlin Heidelberg, 2006.Description: XVII, 299 p. 43 illus., 1 illus. in color. online resource.Content type: text Media type: computer Carrier type: online resourceISBN: 9783540325819.Subject(s): Life sciences | Biochemistry | Cell biology | Life Sciences | Cell Biology | Biochemistry, generalDDC classification: 571.6 Online resources: Click here to access online
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.
In: Springer eBooksSummary: 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 even outside cells. These proteins are of interest to a large number of scientists, not only to those interested in protein biosynthesis, but also in relation to protein transport, organelle biogenesis, and cell stress. Whereas excellent reviews on molecular chaperones are published, they often focus on the latest results without reiterating the basics. The goal of this volume was to assemble a collection of reviews on molecular chaperones that would be both timely and basic, which would make them an excellent entrance for novices into the field and suitable for teaching purposes.
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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.

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 even outside cells. These proteins are of interest to a large number of scientists, not only to those interested in protein biosynthesis, but also in relation to protein transport, organelle biogenesis, and cell stress. Whereas excellent reviews on molecular chaperones are published, they often focus on the latest results without reiterating the basics. The goal of this volume was to assemble a collection of reviews on molecular chaperones that would be both timely and basic, which would make them an excellent entrance for novices into the field and suitable for teaching purposes.

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