- Presents detailed protocols
- Includes troubleshooting tips
- Provides coverage on structural biology, computational methods, and biology
Table of Contents
- Characterization of protein deposition in vivo and ex vivo.
Chapter 1: PMCA for diagnosis and prion propagation studies.
Chapter 2: Fractionation of prion protein aggregates by asymmetrical flow field-flow fractionation.
Chapter 3: Analysis of Amyloid Aggregates Using Agarose Gel Electrophoresis.
Chapter 4: Characterization of Systemic Amyloid Deposits by Mass Spectrometry.
Chapter 5: Proteomics of Polyglutamine Aggregates.
Chapter 6: Merger of Laser Capture Microdissection and Mass Spectrometry: A Window into the Amyloid Plaque Proteome.
Chapter 7: MALDI MS Imaging of Amyloid.
Chapter 8: Imaging polyglutamine deposits in brain tissue.
Chapter 9: X-34 labeling of abnormal protein aggregates during the progression of Alzheimer’s disease.
Chapter 10: Visualizing Pathology Deposits in the Living Brain of Alzheimer’s Disease Patients.
Chapter 11: Micro-Imaging of Amyloid in Mice
Cell and animal models of amyloid formation and toxicity
Chapter 12: An efficient protein transformation protocol for introducing prions into yeast.
Chapter 13: Screening for genetic modifiers of amyloid toxicity in yeast.
Chapter 14: Searching for anti-prion compounds: Cell-based high-throughput in vitro assays and animal testing strategies.
Chapter 15: A Drosophila Model of Alzheimer’s Disease.
Chapter 16: A C. elegans model of polyglutamine disease.
Computational Approaches and Theory
Chapter 17: Nucleation: the Connections between Equilibrium and Kinetic Behavior.
Chapter 18: Computational Approaches to Amyloid beta Fibril Core Structure.
Chapter 19: Amyloid beta-protein aggregations: Ab initio discrete molecular dynamics approaches.
Chapter 20: Computational approaches to fibril structure and formation
- No. of pages: 430
- Language: English
- Copyright: © Academic Press 2006
- Published: October 6, 2006
- Imprint: Academic Press
- Hardcover ISBN: 9780121828172
- eBook ISBN: 9780080522548
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