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Chaperones

Edited by Makarow, Marja; Braakman, Ineke 
Springer  2006  



Hardcover  XVII, 299 p., 43 illus., 1 in colour  ISBN 9783540325802      £175.00
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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Springer : biochemistry : biotechnology : chaperones : molecular biology : prions : proteins

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