Overview
- Editors:
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Peter Bross
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Research Unit for Molecular Medicine, Skejby Sygehus, Aarhus, Denmark
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Niels Gregersen
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Research Unit for Molecular Medicine, Skejby Sygehus, Aarhus, Denmark
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Table of contents (24 protocols)
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General Concepts and Models
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- Niels Gregersen, Lars Bolund, Peter Bross
Pages 3-16
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- Peter Bross, Niels Gregersen
Pages 17-26
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- Marina S. Gelman, Ron R. Kopito
Pages 27-37
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- Lene Diness Jakobsen, Poul Henning Jensen
Pages 57-66
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- Melissa D. Scott, Judith Frydman
Pages 67-76
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- Christina M. Coughlan, Jeffrey L. Brodsky
Pages 77-90
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General Methods
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- Jane Nøhr, Karsten Kristiansen, Anne-M. Krogsdam
Pages 93-101
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- Anne-M. Krogsdam, Karsten Kristiansen, Jane Nøhr
Pages 103-109
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- Jane Nøhr, Karsten Kristiansen, Anne-M. Krogsdam
Pages 111-125
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- Jane Nøhr, Karsten Kristiansen
Pages 127-131
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- Annemieke Jansens, Ineke Braakman
Pages 133-145
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Techniques in Conformational Disease Research
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Front Matter
Pages 147-147
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- Gabriele Dodt, Claudia Walter
Pages 165-173
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- Ines Santisteban, Francisco X. Arredondo-Vega, Shannon Daniels, Michael S. Hershfield
Pages 175-182
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About this book
For decades it has been known that structured conformations are important for the proper functioning of most cellular proteins. However, appreciation that protein folding to the functional conformations as well as the structural maintenance of protein molecules are very complex processes has only emerged during the last ten years. The intimate interplay uncovered by this scientific development led us to realize that perturbations of the protein folding process and disturbances of conformational maintenance are major disease mechanisms. This development has given rise to the concept of conformational diseases and the broader signature of protein folding diseases, comprising diseases in which mutations or environmental stresses may result in a partial misfolding that leads then to alternative conformations capable of disturbing cellular processes. This may happen by self-association (aggregation), as in prion and Alzheimer’s diseases, or by incorporation of alternatively folded subunits into structural entities, as in collagen diseases. Another possibility is that folding to the native structure is impaired or abolished, resulting in decreased stea- state levels of the correctly folded protein, as is observed in cystic fibrosis and 1-antitrypsin deficiency, as well as in many enzyme deficiencies. In addition, deficiencies of proteins that are engaged in assisting and supervising protein folding (protein quality control) may impair the folding of many other proteins, resulting in pathological phenotypes. Examples of this are the spastic paraplegia attributable to mutations in mitochondrial protease/chaperone complexes.
Reviews
"...a very sound book that provides a solid background in conformational disease and presents the reader with helpful experimental protocols for studying protein folding folding and misfolding." - Pharmaceutical Research
"...this book will be a very useful took for specialists in protein chemistry, molecular biology and basic medicine, and also for teachers and their students studying principles of proteomics." Biochemistry