Rahimi / Bitan | Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases | Buch | sack.de

Rahimi / Bitan Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

2012, 568 Seiten, Kartoniert, Previously published in hardcover, Format (B × H): 157 mm x 236 mm, Gewicht: 861 g
ISBN: 978-94-007-9895-3
Verlag: Springer Netherlands

Rahimi / Bitan Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

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.




Weitere Infos & Material


1. Overview of Fibrillar and Oligomeric Assemblies of Amyloidogenic Proteins; Farid Rahimi and Gal Bitan
2. Pathologic Lesions in Alzheimer disease and Other Neurodegenerative Diseases-Cellular and Molecular Components; Harry V. Vinters, Spencer Tung, and Orestes E. Solis

3. Preparation and Structural Characterization of Pre-fibrillar Assemblies of Amyloidogenic Proteins; Anat Frydman-Marom, Yaron Bram, and Ehud Gazit

4. Biological Targeting and Activity of Pre-fibrillar Abeta Assemblies; Kyle C. Wilcox, Jason Pitt, Adriano Sebollela, Helen Martirosova, Pascale N. Lacor, and William L. Klein

5. The Role of Abeta and Tau Oligomers in the Pathogenesis of Alzheimer's disease; Kiran Bhaskar and Bruce T. Lamb

6. Oligomers of -Synuclein in the Pathogenesis of Parkinson's Disease; Dong-Pyo Hong, Wenbo Zhou, Aaron Santner 3 , and Vladimir N. Uversky

7. Cytotoxic Mechanisms of Islet Amyloid Polypeptide in the Pathogenesis of Type-2 Diabetes Mellitus (T2DM); Theri L. Degaki, Dahabada H. J. Lopes, and Mari C. Sogayar

8. Protein Misfolding and Toxicity in Amyotrophic Lateral Sclerosis; Aaron Kerman and Avijit Chakrabartty

9. Structural Studies of Prion Proteins and Prions; Giuseppe Legname, Gabriele Giachin, Federico Benetti

10. Role of Prion Protein Oligomers in the Pathogenesis of Transmissible Spongiform Encephalopathies; Rodrigo Morales, Claudia A. Duran-Aniotz, and Claudio Soto

11. When More Is Not Better: Expanded Polyglutamine Domains in Neurodegenerative Disease; Regina M. Murphy, Robert H. Walters, Matthew D. Tobelmann, and Joseph P. Bernacki

12. Protein Misfolding and Toxicity in Dialysis-Related Amyloidosis; John P. Hodkinson, Alison E. Ashcroft, Sheena E. Radford

13. Transthyretin Aggregation and Toxicity; Maria J. Saraiva, Isabel S. Cardoso

14. Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases; Jennifer D. Lanning and Stephen C. Meredith


Einige Cookies sind notwendig für den Betrieb der Seite, während andere uns helfen, Ihnen ein optimales Erlebnis unserer Webseite zu ermöglichen.