Chaperones [electronic resource] : 16 / edited by Ineke Braakman.

Call Number
571.6
Title
Chaperones 16 / edited by Ineke Braakman.
Physical Description
XVII, 299 p. 43 illus., 1 illus. in color. online resource.
Series
Topics in Current Genetics, 1610-2096 ; 16
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.
Summary
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.
Added Author
Braakman, Ineke. editor.
SpringerLink (Online service)
Subject
LIFE SCIENCES.
BIOCHEMISTRY.
CELL BIOLOGY.
Life Sciences.
Cell Biology.
Biochemistry, general.
Multimedia
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$a 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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No Reviews to Display
Summary
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.
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.
Subject
LIFE SCIENCES.
BIOCHEMISTRY.
CELL BIOLOGY.
Life Sciences.
Cell Biology.
Biochemistry, general.
Multimedia