Summary and Info
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates.The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequ. Read more... Front Cover; Amyloid, Prions, and Other Protein Aggregates; Copyright Page; Table of Contents; Contributors to Volume 309; Preface; Volumes in Series; Section I: Characterization of in Vivo Protein Deposition; A. Identification and Isolation of Aggregates; Chapter 1. Staining Methods for Identification of Amyloid in Tissue; Chapter 2. Isolation and Characterization of Amyloid Fibrils from Tissue; Chapter 3. Isolating Inclusion Bodies from Bacteria; Chapter 4. Isolation of Amyloid Deposits from Brain; B. Isolation and Characterization of Protein Deposit Components Chapter 5. Microextraction and Purification Techniques Applicable to Chemical Characterization of Amyloid Proteins in Minute Amounts of TissueChapter 6. Purification of Paired Helical Filament Tau and Normal Tau from Human Brain Tissue; Chapter 7. Chemical Modifications of Deposited Amyloid-B Peptides; C. Characterization of Aggregates in Situ and in Vitro; Chapter 8. Monoclonal Antibodies Specific for the Native, Disease-Associated Isoform of Prion Protein; Chapter 9. Assays of Protease-Resistant Prion Protein and Its Formation Chapter 10. In Situ Methods for Detection and Localization of Markers of Oxidative Stress: Application in Neurodegenerative DisordersChapter 11. Advanced Glycation End Products: Detection and Reversal; Chapter 12. Analysis of Transglutaminase-Catalyzed Isopeptide Bonds in Paired Helical Filaments and Neurofibrillary Tangles from Alzheimer's Disease; Section II: Characterization of in Vitro Protein Deposition; A. Managing the Aggregation Process; Chapter 13. Methodological and Chemical Factors Affecting Amyloid-B Peptide Amyloidogenicity Chapter 14. In Vitro Immunoglobulin Light Chain Fibrillo- genesisChapter 15. Inhibition of Aggregation Side Reactions during in Vitro Protein Folding; Chapter 16. Inhibition of Stress-Induced Aggregation of Protein Therapeutics; B. Aggregation Theory; Chapter 17. Analysis of Protein Aggregation Kinetics; C. Monitoring Aggregate Growth by Dye Binding; Chapter 18. Quantification of B-Sheet Amyloid Fibril Structures with Thioflavin T; Chapter 19. Quantifying Amyloid by Congo Red Spectral Assay; Chapter 20. Kinetic Analysis of Amyloid Fibril Formation D. Measurement and Characterization of Assembly IntermediatesChapter 21. Small-Zone, High-Speed Gel Filtration Chromatog- raphy to Detect Protein Aggregation Associated with Light Chain Pathologies; Chapter 22. Detection of Early Aggregation Intermediates by Native Gel Electrophoresis and Native Western Blotting; E. Monitoring Aggregate Growth by Measuring Solid-Phase Accumulation; Chapter 23. Deposition of Soluble Amyloid-B onto Amyloid Templates: Identification of Amyloid Fibril Extension Inhibitors
More About the Author
John Norman Abelson (born 1938 in Grand Coulee, Washington) is an American molecular biologist with expertise in biophysics, biochemistry, and genetics.
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