Overview
- An up-to-date review of protein-misfolding diseases which will serve as a complete reference point for readers
- Up-to-date chapters that discuss different diseases associated with protein misfolding and neurodegeneration
- A good reference collection for a broad spectrum of readers
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About this book
Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies described in vitro are still elusive. Deciphering these intricate structure–function correlations will help understanding a complex array of pathogenic mechanisms, some of which may be common across different diseases albeit affecting different cell types and systems.
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Keywords
Table of contents (14 chapters)
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Front Matter
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Back Matter
Editors and Affiliations
Bibliographic Information
Book Title: Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases
Editors: Farid Rahimi, Gal Bitan
DOI: https://doi.org/10.1007/978-94-007-2774-8
Publisher: Springer Dordrecht
eBook Packages: Biomedical and Life Sciences, Biomedical and Life Sciences (R0)
Copyright Information: Springer Science+Business Media B.V. 2012
Hardcover ISBN: 978-94-007-2773-1Published: 13 January 2012
Softcover ISBN: 978-94-007-9895-3Published: 24 February 2014
eBook ISBN: 978-94-007-2774-8Published: 11 January 2012
Edition Number: 1
Number of Pages: VIII, 568
Topics: Biomedicine general, Protein Science, Protein Structure, Neurosciences, Neurobiology, Pathology