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Chaperones
Edited by Makarow, Marja; Braakman, Ineke
Springer
2006
Hardcover XVII, 299 p., 43 illus., 1 in colour ISBN 3540325808
£115.00
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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 - Ville Hietakangas and Lea Sistonen
- The unfolded protein response unfolds - Maho Niwa
Hspp: a protein disaggregase - Johnny M Tkach and John R Glover
- Folding of newly synthesised proteins in the endoplasmic reticulum -
Sanjika Dias-Gunasekara and Adam M Benham
- Quality control of proteins in the mitochondrion -
Mark Nolden, Brigitte Kisters-Woike, Thomas Langer, and Martin Graef
- Chaperone proteins and peroxisomal protein import -
Wim de Jonge, Henk F Tabak, and Ineke Braakman
- Proteasomal degradation of misfolded proteins -
Robert Gauss, Oliver Neuber, and Thomas Sommer
- Template-induced protein misfolding underlying prion diseases -
Luc Bousset, Nicolas Fay, and Ronald Melki
- The Hsp chaperonins from prokaryotes and eukaryotes -
M Giulia Bigotti, Anthony R Clarke, and Steven G Burston
Index
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